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https://en.wikipedia.org/wiki/Thiamine%20diphosphokinase | In enzymology, a thiamine diphosphokinase () is an enzyme that catalyzes the chemical reaction
ATP + thiamine AMP + thiamine diphosphate
Thus, the two substrates of this enzyme are ATP and thiamine, whereas its two products are AMP and thiamine diphosphate.
This enzyme belongs to the family of transferases, specifically those transferring two phosphorus-containing groups (diphosphotransferases). The systematic name of this enzyme class is ATP:thiamine diphosphotransferase. Other names in common use include thiamin kinase, thiamine pyrophosphokinase, ATP:thiamin pyrophosphotransferase, thiamin pyrophosphokinase, thiamin pyrophosphotransferase, thiaminokinase, thiamin:ATP pyrophosphotransferase, and TPTase. This enzyme participates in thiamine metabolism.
Structural studies
As of late 2007, six structures have been solved for this class of enzymes, with PDB accession codes , , , , , and .
References
EC 2.7.6
Enzymes of known structure |
https://en.wikipedia.org/wiki/Thiamine%20kinase | In enzymology, a thiamine kinase () is an enzyme that catalyzes the chemical reaction
ATP + thiamine ADP + thiamine phosphate
Thus, the two substrates of this enzyme are ATP and thiamine, whereas its two products are ADP and thiamine phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:thiamine phosphotransferase. Other names in common use include thiamin kinase (phosphorylating), thiamin phosphokinase, ATP:thiamin phosphotransferase, and thiamin kinase. This enzyme participates in thiamine metabolism.
References
EC 2.7.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Thiamine-phosphate%20kinase | In enzymology, a thiamine-phosphate kinase () is an enzyme that catalyzes the chemical reaction
ATP + thiamine phosphate ADP + thiamine diphosphate
Thus, the two substrates of this enzyme are ATP and thiamine phosphate, whereas its two products are ADP and thiamine diphosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. The systematic name of this enzyme class is ATP:thiamine-phosphate phosphotransferase. Other names in common use include thiamin-monophosphate kinase, thiamin monophosphatase, and thiamin monophosphokinase. This enzyme participates in thiamine metabolism.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 2.7.4
Enzymes of known structure |
https://en.wikipedia.org/wiki/Triokinase | In enzymology, a triokinase () is an enzyme that catalyzes the chemical reaction
ATP + D-glyceraldehyde ADP + D-glyceraldehyde 3-phosphate
Thus, the two substrates of this enzyme are ATP and D-glyceraldehyde, whereas its two products are ADP and D-glyceraldehyde 3-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:D-glyceraldehyde 3-phosphotransferase. This enzyme is also called triose kinase. This enzyme participates in fructose metabolism.
References
EC 2.7.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Triphosphate%E2%80%94protein%20phosphotransferase | In enzymology, a triphosphate-protein phosphotransferase () is an enzyme that catalyzes the chemical reaction
triphosphate + [microsomal-membrane protein] diphosphate + phospho-[microsomal-membrane protein]
Thus, the two substrates of this enzyme are triphosphate and microsomal-membrane protein, whereas its two products are diphosphate and [[phospho-[microsomal-membrane protein]]].
Classification
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups that are not covered by other phosphotransferase families.
Nomenclature
The systematic name of this enzyme class is triphosphate:[microsomal-membrane-protein] phosphotransferase. Other names in common use include diphosphate:microsomal-membrane-protein O-phosphotransferase, (erroneous), DiPPT (erroneous), pyrophosphate:protein phosphotransferase (erroneous), diphosphate-protein phosphotransferase (erroneous), diphosphate:[microsomal-membrane-protein] O-phosphotransferase, and (erroneous).
References
EC 2.7.99
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Triphosphoribosyl-dephospho-CoA%20synthase | In enzymology, a triphosphoribosyl-dephospho-CoA synthase () is an enzyme that catalyzes the chemical reaction
ATP + 3-dephospho-CoA 2'-(5"-triphosphoribosyl)-3'-dephospho-CoA + adenine
Thus, the two substrates of this enzyme are ATP and 3-dephospho-CoA, whereas its two products are 2'-(5''-triphosphoribosyl)-3'-dephospho-CoA and adenine.
This enzyme belongs to the family of transferases, specifically those transferring non-standard substituted phosphate groups. The systematic name of this enzyme class is ATP:3-dephospho-CoA 5"-triphosphoribosyltransferase. Other names in common use include 2'-(5"-triphosphoribosyl)-3-dephospho-CoA synthase, ATP:dephospho-CoA 5-triphosphoribosyl transferase, and CitG. This enzyme participates in two-component system - general.
References
EC 2.7.8
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/CCA%20tRNA%20nucleotidyltransferase | CCA tRNA nucleotidyltransferase (, CCA-adding enzyme, tRNA adenylyltransferase, tRNA CCA-pyrophosphorylase, tRNA-nucleotidyltransferase, transfer-RNA nucleotidyltransferase, transfer ribonucleic acid nucleotidyl transferase, CTP(ATP):tRNA nucleotidyltransferase, transfer ribonucleate adenylyltransferase, transfer ribonucleate adenyltransferase, transfer RNA adenylyltransferase, transfer ribonucleate nucleotidyltransferase, ATP (CTP):tRNA nucleotidyltransferase, ribonucleic cytidylic cytidylic adenylic pyrophosphorylase, transfer ribonucleic adenylyl (cytidylyl) transferase, transfer ribonucleic-terminal trinucleotide nucleotidyltransferase, transfer ribonucleate cytidylyltransferase, ribonucleic cytidylyltransferase, -C-C-A pyrophosphorylase, ATP(CTP)-tRNA nucleotidyltransferase, tRNA adenylyl(cytidylyl)transferase, CTP:tRNA cytidylyltransferase) is an enzyme with systematic name CTP,CTP,ATP:tRNA cytidylyl,cytidylyl,adenylyltransferase. This enzyme catalyses the following chemical reaction
a tRNA precursor + 2 CTP + ATP a tRNA with a 3' CCA end + 3 diphosphate (overall reaction)
(1a) a tRNA precursor + CTP a tRNA with a 3' cytidine end + diphosphate
(1b) a tRNA with a 3' cytidine + CTP a tRNA with a 3' CC end + diphosphate
(1c) a tRNA with a 3' CC end + ATP a tRNA with a 3' CCA end + diphosphate
The acylation of all tRNAs with an amino acid occurs at the terminal ribose of a 3' CCA sequence.
See also
TRNT1
References
External links
EC 2.7.7 |
https://en.wikipedia.org/wiki/TRNA%20nucleotidyltransferase | In enzymology, a tRNA nucleotidyltransferase () is an enzyme that catalyzes the chemical reaction
tRNAn+1 + phosphate tRNAn + a nucleoside diphosphate
where tRNA-N is a product of transcription, and tRNA Nucleotidyltransferase catalyzes this cytidine-cytidine-adenosine (CCA) addition to form the tRNA-NCCA product.
Function
Protein synthesis takes place in cytosolic ribosomes, mitochondria (mitoribosomes), and in plants, the plastids (chloroplast ribosomes). Each of these compartments requires a complete set of functional tRNAs to carry out protein synthesis. The production of mature tRNAs requires processing and modification steps such as the addition of a 3’-terminal cytidine-cytidine-adenosine (CCA). Since no plant tRNA genes encode this particular sequence, a tRNA nucleotidyltransferase must add this sequence post-transcriptionally and therefore is present in all three compartments.
In eukaryotes, multiple forms of tRNA nucleotidyltransferases are synthesized from a single gene and are distributed to different subcellular compartments in the cell. There are multiple in-frame start codons which allow for the production of variant forms of the enzyme containing different targeting information predominantly found in the N-terminal sequence of the protein (reference). In vivo experiments show that the N-terminal sequences are used as transit peptides for import into the mitochondria and plastids. Comparison studies using available tRNA nucleotidyltransferase sequences h |
https://en.wikipedia.org/wiki/Tropomyosin%20kinase | In enzymology, a tropomyosin kinase () is an enzyme that catalyzes the chemical reaction
ATP + tropomyosin ADP + O-phosphotropomyosin
Thus, the two substrates of this enzyme are ATP and tropomyosin, whereas its two products are ADP and O-phosphotropomyosin.
This enzyme belongs to the family of transferases, specifically those transferring a phosphate group to the sidechain oxygen atom of serine or threonine residues in proteins (protein-serine/threonine kinases). The systematic name of this enzyme class is ATP:tropomyosin O-phosphotransferase. Other names in common use include tropomyosin kinase (phosphorylating), and STK.
References
EC 2.7.11
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%28tyrosine%203-monooxygenase%29%20kinase | In enzymology, a [tyrosine 3-monooxygenase] kinase () is an enzyme that catalyzes the chemical reaction
ATP + [tyrosine-3-monooxygenase] ADP + phospho-[tyrosine-3-monooxygenase]
Thus, the two substrates of this enzyme are ATP and tyrosine 3-monooxygenase, whereas its two products are ADP and phospho-(tyrosine-3-monooxygenase).
This enzyme belongs to the family of transferases, specifically those transferring a phosphate group to the sidechain oxygen atom of serine or threonine residues in proteins (protein-serine/threonine kinases). The systematic name of this enzyme class is ATP:[tyrosine-3-monoxygenase] phosphotransferase. Other names in common use include pheochromocytoma tyrosine hydroxylase-associated kinase, STK4, and tyrosine 3-monooxygenase kinase (phosphorylating). This enzyme participates in MAPK signaling pathway and non-small cell lung cancer.
References
EC 2.7.11
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/UDP-glucose%E2%80%94glycoprotein%20glucose%20phosphotransferase | In enzymology, an UDP-glucose—glycoprotein glucose phosphotransferase () is an enzyme that catalyzes the chemical reaction
UDP-glucose + glycoprotein D-mannose UMP + glycoprotein 6-(D-glucose-1-phospho)-D-mannose
Thus, the two substrates of this enzyme are UDP-glucose and glycoprotein D-mannose, whereas its two products are UMP and glycoprotein 6-(D-glucose-1-phospho)-D-mannose.
This enzyme belongs to the family of transferases, specifically those transferring non-standard substituted phosphate groups. The systematic name of this enzyme class is UDP-glucose:glycoprotein-D-mannose glucosephosphotransferase. Other names in common use include UDP-glucose:glycoprotein glucose-1-phosphotransferase, GlcPTase, Glc-phosphotransferase, and uridine diphosphoglucose-glycoprotein glucose-1-phosphotransferase.
References
EC 2.7.8
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/UDP-glucose%E2%80%94hexose-1-phosphate%20uridylyltransferase | In enzymology, an UDP-glucose—hexose-1-phosphate uridylyltransferase () is an enzyme that catalyzes the chemical reaction
UDP-glucose + alpha-D-galactose 1-phosphate alpha-D-glucose 1-phosphate + UDP-galactose
Thus, the two substrates of this enzyme are UDP-glucose and alpha-D-galactose 1-phosphate, whereas its two products are alpha-D-glucose 1-phosphate and UDP-galactose.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is UDP-glucose:alpha-D-galactose-1-phosphate uridylyltransferase. Other names in common use include uridyl transferase, hexose-1-phosphate uridylyltransferase, uridyltransferase, and hexose 1-phosphate uridyltransferase. This enzyme participates in galactose metabolism and nucleotide sugars metabolism.
Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes , , , and .
References
EC 2.7.7
Enzymes of known structure |
https://en.wikipedia.org/wiki/UDP-N-acetylglucosamine%20diphosphorylase | In enzymology, an UDP-N-acetylglucosamine diphosphorylase () is an enzyme that catalyzes the chemical reaction
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate diphosphate + UDP-N-acetyl-D-glucosamine
Thus, the two substrates of this enzyme are UTP and[N-acetyl-alpha-D-glucosamine 1-phosphate, whereas its two products are diphosphate and UDP-N-acetyl-D-glucosamine. This enzyme participates in aminosugars metabolism.
Nomenclature
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is UTP:N-acetyl-alpha-D-glucosamine-1-phosphate uridylyltransferase. Other names in common use include UDP-N-acetylglucosamine pyrophosphorylase, uridine diphosphoacetylglucosamine pyrophosphorylase, UTP:2-acetamido-2-deoxy-alpha-D-glucose-1-phosphate, uridylyltransferase, UDP-GlcNAc pyrophosphorylase, GlmU uridylyltransferase, Acetylglucosamine 1-phosphate uridylyltransferase, UDP-acetylglucosamine pyrophosphorylase, uridine diphosphate-N-acetylglucosamine pyrophosphorylase, uridine diphosphoacetylglucosamine phosphorylase, and acetylglucosamine 1-phosphate uridylyltransferase.
References
EC 2.7.7
Enzymes of known structure |
https://en.wikipedia.org/wiki/UMP%20kinase | In enzymology, an UMP kinase () is an enzyme that catalyzes the chemical reaction
ATP + UMP ADP + UDP
Thus, the two substrates of this enzyme are ATP and UMP, whereas its two products are ADP and UDP.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. The systematic name of this enzyme class is ATP:UMP phosphotransferase. Other names in common use include uridylate kinase, UMPK, uridine monophosphate kinase, PyrH, UMP-kinase, and SmbA. This enzyme participates in pyrimidine metabolism.
Structural studies
As of March 2010, 19 structures have been solved for this class of enzymes, and are deposited in the PDB. All have a 3-layer (aba) sandwich) architecture (CATH code 3.40.1160.10). These include accession codes , , , and .
Search for all UMP Kinases in the PDB using the enzyme Browser at PDBe. (input the EC number)
References
EC 2.7.4
Enzymes of known structure |
https://en.wikipedia.org/wiki/Cytochrome%20c%20oxidase%20subunit%20III | Cytochrome c oxidase subunit III (COX3) is an enzyme that in humans is encoded by the MT-CO3 gene. It is one of main transmembrane subunits of cytochrome c oxidase. It is also one of the three mitochondrial DNA (mtDNA) encoded subunits (MT-CO1, MT-CO2, MT-CO3) of respiratory complex IV. Variants of it have been associated with isolated myopathy, severe encephalomyopathy, Leber hereditary optic neuropathy, mitochondrial complex IV deficiency, and recurrent myoglobinuria .
Structure
The MT-CO3 gene produces a 30 kDa protein composed of 261 amino acids. COX3, the protein encoded by this gene, is a member of the cytochrome c oxidase subunit 3 family. This protein is located on the inner mitochondrial membrane. COX3 is a multi-pass transmembrane protein: in human, it contains 7 transmembrane domains at positions 15–35, 42–59, 81–101, 127–147, 159–179, 197–217, and 239–259.
Function
Cytochrome c oxidase () is the terminal enzyme of the respiratory chain of mitochondria and many aerobic bacteria. It catalyzes the transfer of electrons from reduced cytochrome c to molecular oxygen:
4 cytochrome c+2 + 4 H+ + O2 4 cytochrome c+3 + 2 H2O
This reaction is coupled to the pumping of four additional protons across the mitochondrial or bacterial membrane.
Cytochrome c oxidase is an oligomeric enzymatic complex that is located in the mitochondrial inner membrane of eukaryotes and in the plasma membrane of aerobic prokaryotes. The core structure of prokaryotic and eukaryotic cytochrom |
https://en.wikipedia.org/wiki/Undecaprenol%20kinase | In enzymology, an undecaprenol kinase () is an enzyme that catalyzes the chemical reaction
ATP + undecaprenol ADP + undecaprenyl phosphate
Thus, the two substrates of this enzyme are ATP and undecaprenol, whereas its two products are ADP and undecaprenyl phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:undecaprenol phosphotransferase. Other names in common use include isoprenoid alcohol kinase, isoprenoid alcohol phosphokinase, C55-isoprenoid alcohol phosphokinase, isoprenoid alcohol kinase (phosphorylating), C55-isoprenoid alcohol kinase, C55-isoprenyl alcohol phosphokinase, and polyisoprenol kinase. This enzyme participates in peptidoglycan biosynthesis.
References
EC 2.7.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Undecaprenyl-phosphate%20galactose%20phosphotransferase | In enzymology, an undecaprenyl-phosphate galactose phosphotransferase () is an enzyme that catalyzes the chemical reaction
UDP-galactose + undecaprenyl phosphate UMP + alpha-D-galactosyl-diphosphoundecaprenol
Thus, the two substrates of this enzyme are UDP-galactose and undecaprenyl phosphate, whereas its two products are UMP and alpha-D-galactosyl-diphosphoundecaprenol.
This enzyme belongs to the family of transferases, specifically those transferring non-standard substituted phosphate groups. The systematic name of this enzyme class is UDP-galactose:undecaprenyl-phosphate galactose phosphotransferase. Other names in common use include poly(isoprenol)-phosphate galactose phosphotransferase, poly(isoprenyl)phosphate galactosephosphatetransferase, and undecaprenyl phosphate galactosyl-1-phosphate transferase.
References
EC 2.7.8
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Uridine%20kinase | In enzymology, an uridine kinase () is an enzyme that catalyzes the chemical reaction
ATP + uridine ADP + UMP
Thus, the two substrates of this enzyme are ATP and uridine, whereas its two products are ADP and UMP.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:uridine 5'-phosphotransferase. Other names in common use include pyrimidine ribonucleoside kinase, uridine-cytidine kinase, uridine kinase (phosphorylating), and uridine phosphokinase. This enzyme participates in pyrimidine metabolism.
Structural studies
As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , and .
References
EC 2.7.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/UTP%E2%80%94hexose-1-phosphate%20uridylyltransferase | In enzymology, an UTP—hexose-1-phosphate uridylyltransferase () is an enzyme that catalyzes the chemical reaction
UTP + alpha-D-galactose 1-phosphate diphosphate + UDP-galactose
Thus, the two substrates of this enzyme are UTP and alpha-D-galactose 1-phosphate, whereas its two products are diphosphate and UDP-galactose.
Enzyme family
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is UTP:alpha-D-hexose-1-phosphate uridylyltransferase. Other names in common use include galactose-1-phosphate uridylyltransferase, galactose 1-phosphate uridylyltransferase, alpha-D-galactose 1-phosphate uridylyltransferase, galactose 1-phosphate uridyltransferase, UDPgalactose pyrophosphorylase, uridine diphosphate galactose pyrophosphorylase, and uridine diphosphogalactose pyrophosphorylase. This enzyme participates in galactose metabolism and nucleotide sugars metabolism.
Structural studies
, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and .
References
EC 2.7.7
Enzymes of known structure |
https://en.wikipedia.org/wiki/UTP-monosaccharide-1-phosphate%20uridylyltransferase | In enzymology, an UTP-monosaccharide-1-phosphate uridylyltransferase () is an enzyme that catalyzes the chemical reaction
UTP + a monosaccharide 1-phosphate diphosphate + UDP-monosaccharide
Thus, the two substrates of this enzyme are UTP and monosaccharide 1-phosphate, whereas its two products are diphosphate and UDP-monosaccharide.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is '''. Other names in common use include UDP-sugar pyrophosphorylase, and PsUSP'''.
References
EC 2.7.7
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/UTP%E2%80%94xylose-1-phosphate%20uridylyltransferase | In enzymology, an UTP—xylose-1-phosphate uridylyltransferase () is an enzyme that catalyzes the chemical reaction
UTP + alpha-D-xylose 1-phosphate diphosphate + UDP-xylose
Thus, the two substrates of this enzyme are UTP and alpha-D-xylose 1-phosphate, whereas its two products are diphosphate and UDP-xylose.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is UTP:alpha-D-xylose-1-phosphate uridylyltransferase. Other names in common use include xylose-1-phosphate uridylyltransferase, uridylyltransferase, xylose 1-phosphate, UDP-xylose pyrophosphorylase, uridine diphosphoxylose pyrophosphorylase, and xylose 1-phosphate uridylyltransferase. This enzyme participates in nucleotide sugars metabolism.
References
EC 2.7.7
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Viomycin%20kinase | In enzymology, viomycin kinase () is an enzyme that catalyzes the chemical reaction
ATP + viomycin ADP + O-phosphoviomycin
Thus, the two substrates of this enzyme are ATP and viomycin, whereas its two products are ADP and O-phosphoviomycin.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:viomycin O-phosphotransferase. Other names in common use include viomycin phosphotransferase, and capreomycin phosphotransferase.
References
EC 2.7.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Xylitol%20kinase | In enzymology, a xylitol kinase () is an enzyme that catalyzes the chemical reaction
ATP + xylitol ADP + xylitol 5-phosphate
Thus, the two substrates of this enzyme are ATP and xylitol, whereas its two products are ADP and xylitol 5-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:xylitol 5-phosphotransferase.
References
EC 2.7.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Xylulokinase | In enzymology, a xylulokinase () is an enzyme that catalyzes the chemical reaction
ATP + D-xylulose ADP + D-xylulose 5-phosphate
Thus, the two substrates of this enzyme are ATP and D-xylulose, whereas its two products are ADP and D-xylulose 5-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:D-xylulose 5-phosphotransferase. Other names in common use include xylulokinase (phosphorylating), and D-xylulokinase. This enzyme participates in pentose and glucuronate interconversions.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
Applications
Hydrogen production
In 2014 a low-temperature , atmospheric-pressure enzyme-driven process to convert xylose into hydrogen with nearly 100% of the theoretical yield was announced. The process employs 13 enzymes, including xylulokinase.
References
Further reading
EC 2.7.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Somatic%20antigen | A somatic antigen is an antigen located in the cell wall of a gram-positive or gram-negative bacterium.
See also
Lipopolysaccharide
References
Bacterial proteins
Bacteriology |
https://en.wikipedia.org/wiki/RasGEF%20domain | RasGEF domain is domain found in the CDC25 family of guanine nucleotide exchange factors for Ras-like small GTPases.
Ras proteins are membrane-associated molecular switches that bind GTP and GDP and slowly hydrolyze GTP to GDP. The balance between the GTP bound (active) and GDP bound (inactive) states is regulated by the opposite action of proteins activating the GTPase activity and that of proteins which promote the loss of bound GDP and the uptake of fresh GTP. The latter proteins are known as guanine-nucleotide dissociation stimulators (GDSs) (or also as guanine-nucleotide releasing (or exchange) factors (GRFs)). Proteins that act as GDS can be classified into at least two families, on the basis of sequence similarities, the CDC24 family (see ) and this CDC25 (RasGEF) family.
The size of the proteins of the CDC25 family range from 309 residues (LTE1) to 1596 residues (sos). The sequence similarity shared by all these proteins is limited to a region of about 250 amino acids generally located in their C-terminal section (currently the only exceptions are sos and ralGDS where this domain makes up the central part of the protein). This domain has been shown, in CDC25 an SCD25, to be essential for the activity of these proteins.
Human proteins containing this domain
KNDC1; PLCE1; RALGDS; RALGPS1; RALGPS2; RAPGEF1; RAPGEF2; RAPGEF3;
RAPGEF4; RAPGEF5; RAPGEF6; RAPGEFL1; RASGEF1A; RASGEF1B; RASGEF1C; RASGRF1; RASGRF2;
RASGRP1; RASGRP2; RASGR |
https://en.wikipedia.org/wiki/RhoGAP%20domain | RhoGAP domain is an evolutionary conserved protein domain of
GTPase activating proteins towards Rho/Rac/Cdc42-like small GTPases.
Human proteins containing this domain
ABR; ARHGAP1; ARHGAP10; ARHGAP11A; ARHGAP11B; ARHGAP12; ARHGAP15; ARHGAP17;
ARHGAP18; ARHGAP19; ARHGAP20; ARHGAP21; ARHGAP22; ARHGAP23; ARHGAP24; ARHGAP25;
ARHGAP26; ARHGAP27; ARHGAP28; ARHGAP29; ARHGAP30; ARHGAP4; ARHGAP5; ARHGAP6;
ARHGAP8; ARHGAP9; BCR; BPGAP1; C1; C5orf5; CDGAP; CENTD1;
CENTD2; CENTD3; CHN1; CHN2; DEPDC1; DEPDC1A; DEPDC1B; DLC1;
FAM13A1; FKSG42; GMIP; GRLF1; HMHA1; INPP5B; KIAA1688; LOC553158;
MYO9A; MYO9B; OCRL; OPHN1; PIK3R1; PIK3R2; PRR5; RACGAP1;
RACGAP1P; RALBP1; RICH2; RICS; SH3BP1; SLIT1; SNX26; SRGAP1;
SRGAP2; SRGAP3; STARD13; STARD8; SYDE1; SYDE2;
Notes
References
Protein domains
Peripheral membrane proteins |
https://en.wikipedia.org/wiki/GGL%20domain | GGL domain is domain found in the gamma subunit of the heterotrimeric G protein complex and in regulators of G protein signaling RGS proteins.
Human proteins containing this domain
GNG4; GNG10; GNG11
GNGT1
RGS6; RGS7; RGS9; RGS11
See also
Beta-gamma complex
References
Further reading
Protein domains
Peripheral membrane proteins |
https://en.wikipedia.org/wiki/Transmembrane%20domain%20of%20ABC%20transporters | ABC transporter transmembrane domain is the main transmembrane structural unit of ATP-binding cassette transporter proteins, consisting of six alpha helixes that traverse the plasma membrane. Many members of the ABC transporter family () have two such regions.
This family appears to correspond to ABC1 by TCDB classification.
Subfamilies
Sulphate ABC transporter permease protein 2
Phosphate transport system permease protein 2
Phosphonate uptake transporter
Nitrate transport permease
NifC-like ABC-type porter
Phosphate ABC transporter, permease protein PstC
Molybdate ABC transporter, permease protein
Nickel ABC transporter, permease subunit NikB
Nickel ABC transporter, permease subunit NikC
Ectoine/hydroxyectoine ABC transporter, permease protein EhuD
Ectoine/hydroxyectoine ABC transporter, permease protein EhuC
Human proteins containing this domain
ABCB1; ABCB10; ABCB11; ABCB4; ABCB5; ABCB6; ABCB7; ABCB8;
ABCB9; ABCC1; ABCC10; ABCC11; ABCC12; ABCC13; ABCC2; ABCC3;
ABCC4; ABCC5; ABCC6; ABCC8; ABCC9; CFTR;
TAP1; TAP2; TAPL;
References
ATP-binding cassette transporters
Protein domains
Protein families |
https://en.wikipedia.org/wiki/Discoidin%20domain | Discoidin domain (also known as F5/8 type C domain, or C2-like domain) is major protein domain of many blood coagulation factors.
Blood coagulation factors V and VIII contain a C-terminal, twice repeated, domain of about 150 amino acids, which is often called "C2-like domain" (that is unrelated to the C2 domain). In the Dictyostelium discoideum (Slime mold) cell adhesion protein discoidin, a related domain, named discoidin I-like domain, DLD, or DS, has been found which shares a common C-terminal region of about 110 amino acids with the FA58C domain, but whose N-terminal 40 amino acids are much less conserved. Similar domains have been detected in other extracellular and membrane proteins. In coagulation factors V and VIII the repeated domains compose part of a larger functional domain which promotes binding to anionic phospholipids on the surface of platelets and endothelial cells. The C-terminal domain of the second FA58C repeat (C2) of coagulation factor VIII has been shown to be responsible for phosphatidylserine-binding and essential for activity. FA58C contains two conserved cysteines in most proteins, which link the extremities of the domain by a disulfide bond. A further disulfide bond is located near the C-terminal of the second FA58C domain in MFGM .
Human proteins containing this domain
AEBP1; BTBD9; CASPR4; CNTNAP1; CNTNAP2; CNTNAP3; CNTNAP4; CNTNAP5; CPXM1; CPXM2; DCBLD1; DCBLD2; DDR1; DDR2; EDIL3;
F5; F8; |
https://en.wikipedia.org/wiki/G%C3%B6ttelborn%20Solar%20Park | Gottelborn Solar Park () is an 8.4-MWp photovoltaic power station located in Göttelborn, in Quierschied municipality, Germany. The power plant was constructed by City Solar in two stages. The first stage was completed in August, 2004, followed by the second stage three years later in November 2007.
The first stage of the plant includes 23,500 solar modules from the French manufacturer "Photowatt" at an estimated efficiency of 14%, with a nominal power output of 4 MWp and occupies a total area of The construction of the second stage required another 50,000 PV modules.
See also
Photovoltaic power stations
Solar power in Germany
References
External links
Power plant photos
Photovoltaic power stations in Germany
Economy of Saarland
Saarbrücken (district) |
https://en.wikipedia.org/wiki/MacDowell%E2%80%93Mansouri%20action | The MacDowell–Mansouri action (named after S. W. MacDowell and Freydoon Mansouri) is an action that is used to derive Einstein's field equations of general relativity.
It can usefully be formulated in terms of Cartan geometry.
References
Further reading
Wise, D. (2010). “MacDowell-Mansouri gravity and Cartan geometry”. Class. Quantum Grav. 27, 155010.
Reid, James A.; Wang, Charles H.-T. (2014). "Conformal holonomy in MacDowell-Mansouri gravity". J. Math. Phys. 55, 032501.
General relativity |
https://en.wikipedia.org/wiki/Bavaria%20Solarpark | The Bavaria Solarpark is a group of three photovoltaic power stations in different locations in Germany.
Its total capacity amounts to 10 megawatts (MW) and consists of the following distinct solar farms south of Neumarkt in der Oberpfalz, in Bavaria:
The 6.3 MW Solarpark Mühlhausen
The 1.9 MW Solarpark Günching
The 1.9 MW Solarpark Minihof
The Bavaria Solarpark was constructed and is operated by the American company SunPower.
It consists of 57,600 solar panels (model PowerLight NT-5AE3D by Sharp) mounted on SunPower's solar trackers and covers a total area of 40 hectares (99 acres).
Inaugurated on 30 June 2005, the solar farm was grid-connected six months later in December 2005.
For a few months, the Solarpark Mühlhausen was the world's largest photovoltaic power station.
See also
Photovoltaic power stations
Solar power in Germany
References
Photovoltaic power stations in Germany |
https://en.wikipedia.org/wiki/Geiseltalsee%20Solarpark | Geiseltalsee Solarpark, also known as Geiseltalsee, is a 4 MWp photovoltaic power plant located in Merseburg, Germany. The power plant was constructed by BP Solar using 24,864 BP solar modules. The power station was completed in 2004
See also
Photovoltaic power stations
Solar power in Germany
References
Photovoltaic power stations in Germany |
https://en.wikipedia.org/wiki/Sigmodal | Sigmodal (Rectidon) is a barbiturate derivative. It has sedative, hypnotic and anticonvulsant properties, and was used in surgical anaesthesia in the 1950s, and frequently appeared in drug mixtures in the 60s.
It was never widely used compared to better known barbiturates such as thiopental, and has now been replaced by newer drugs with a better safety profile.
References
Barbiturates
Sedatives
Organobromides
GABAA receptor positive allosteric modulators |
https://en.wikipedia.org/wiki/Royal%20Leerdam%20Crystal | Royal Leerdam Crystal (also known as Royal Leerdam) was a Dutch producer of glassware products based in Leerdam, the Netherlands.
History
It was established in 1878 as a department within a glassware producing factory, , itself founded in 1765. From 1938 until 2002 it was part of the Schiedam-based Vereenigde Glasfabrieken. In 2002, the factory became part of the American glass and tableware company Libbey Inc. In 2008, Royal Leerdam was purchased by De Koninklijke Porceleyne Fles, becoming part of the Royal Delft Group. In September 2020, as a result of the COVID-19 pandemic, the glass-making facilities were shut. In 2022, Libbey Glass sold the company to the Dutch Anders Invest Industrie Fonds. There are about 600 employees in the Netherlands and Portugal with annual sales of about €120 million. In the Netherlands, the headquarters and a glass factory are in Leerdam and there is a distribution center in Gorinchem. The total acquisition price was not disclosed. The management of the company will stay on and cooperation with Libbey will be continued.
Designing and glassblowing
Designing and glassblowing were in the past strictly separated. Several well-known designers as Hendrik Petrus Berlage, Karel de Bazel, Andries Copier, Sybren Valkema, and Willem Heesen have contributed to the Royal Leerdam reputation with a wide range of designer glassware. Best known has become the so-called range of products Gilde Glass (1930) by Andries Copier, as an example of both simplicity an |
https://en.wikipedia.org/wiki/Protein%20xylosyltransferase | In enzymology, a protein xylosyltransferase () is an enzyme that catalyzes the chemical reaction in which a beta-D-xylosyl residue is transferred from UDP-D-xylose to the sidechain oxygen atom of a serine residue in a protein.
This enzyme belongs to the family of glycosyltransferases, specifically the pentosyltransferases. The systematic name of this enzyme class is UDP-D-xylose:protein beta-D-xylosyltransferase. Other names in common use include UDP-D-xylose:core protein beta-D-xylosyltransferase, UDP-D-xylose:core protein xylosyltransferase, UDP-D-xylose:proteoglycan core protein beta-D-xylosyltransferase, UDP-xylose-core protein beta-D-xylosyltransferase, uridine diphosphoxylose-core protein beta-xylosyltransferase, and uridine diphosphoxylose-protein xylosyltransferase. This enzyme participates in the biosynthesis of chondroitin sulfate and glycan structures.
Human proteins
XYLT1
XYLT2
See also
Xylosyltransferase
References
EC 2.4.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Xyloglucan%204-glucosyltransferase | In enzymology, a xyloglucan 4-glucosyltransferase () is an enzyme that catalyzes the chemical reaction in which a beta-D-glucosyl residue is transferred from UDP-glucose to another glucose residue in xyloglucan, linked by a beta-1,4-D-glucosyl-D-glucose bond.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-glucose:xyloglucan 1,4-beta-D-glucosyltransferase. Other names in common use include uridine diphosphoglucose-xyloglucan 4beta-glucosyltransferase, xyloglucan 4beta-D-glucosyltransferase, and xyloglucan glucosyltransferase.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Xyloglucan%206-xylosyltransferase | In enzymology, a xyloglucan 6-xylosyltransferase () is an enzyme that catalyzes the chemical reaction in which an alpha-D-xylosyl residue is transferred from UDP-D-xylose to a glucose residue in xyloglucan, being attached by an alpha-1,6-D-xylosyl-D-glucose bond.
This enzyme belongs to the family of glycosyltransferases, specifically the pentosyltransferases. The systematic name of this enzyme class is UDP-D-xylose:xyloglucan 1,6-alpha-D-xylosyltransferase. Other names in common use include uridine diphosphoxylose-xyloglucan 6alpha-xylosyltransferase, and xyloglucan 6-alpha-D-xylosyltransferase.
References
EC 2.4.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Xyloglucan%3Axyloglucosyl%20transferase | In enzymology, a xyloglucan:xyloglucosyl transferase () is an enzyme that catalyzes the chemical reaction in which a beta-(1,4) bond in the backbone of a xyloglucan in broken; the xyloglucanyl segment is then transferred to the O4 of the non-reducing terminal glucose residue of either xyloglucan or an oligosaccharide thereof.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is xyloglucan:xyloglucan xyloglucanotransferase. Other names in common use include endo-xyloglucan transferase, and xyloglucan endotransglycosylase.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 2.4.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Phosphatidylinositol%20a-mannosyltransferase | In enzymology, a phosphatidylinositol alpha-mannosyltransferase () is an enzyme that catalyzes the chemical reaction in which at least one alpha-D-mannose residues are transferred from GDP-mannose to positions 6, 2 and others in 1-phosphatidyl-myo-inositol.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is GDP-mannose:1-phosphatidyl-1D-myo-inositol alpha-D-mannosyltransferase. Other names in common use include GDP mannose-phosphatidyl-myo-inositol alpha-mannosyltransferase, GDPmannose:1-phosphatidyl-myo-inositol alpha-D-mannosyltransferase, guanosine diphosphomannose-phosphatidyl-inositol, alpha-mannosyltransferase, and phosphatidyl-myo-inositol alpha-mannosyltransferase.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Peptide-O-fucosyltransferase | In enzymology, a peptide-O-fucosyltransferase () is an enzyme that catalyzes the chemical reaction in which an alpha-L-fucosylpyranoside residue is transferred from GDP-beta-L-fucose to the sidechain oxygen atom of a serine or threonine residue in a protein.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is GDP-beta-L-fucose:polypeptide O-alpha-L-fucosyltransferase. Other names in common use include GDP-L-fucose:polypeptide fucosyltransferase, GDP-fucose protein O-fucosyltransferase, and GDP-fucose:polypeptide fucosyltransferase.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Oligosaccharide%204-alpha-D-glucosyltransferase | In enzymology, an oligosaccharide 4-alpha-D-glucosyltransferase () is an enzyme that catalyzes the chemical reaction in which the non-reducing terminal alpha-D-glucose residue is transferred from a 1,4-alpha-D-glucan to the 4-position of an alpha-D-glucan. This enzyme is useful in hydrolyzing oligosaccharides.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is 1,4-alpha-D-glucan:1,4-alpha-D-glucan 4-alpha-D-glucosyltransferase. Other names in common use include amylase III, and 1,4-alpha-glucan:1,4-alpha-glucan 4-alpha-glucosyltransferase.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/O-fucosylpeptide%203-beta-N-acetylglucosaminyltransferase | In enzymology, an O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase () is an enzyme that catalyzes the chemical reaction in which a beta-D-GlcNAc residue is transferred from UDP-D-GlcNAc to the fucose residue of a fucosylated protein.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-D-GlcNAc:O-L-fucosylpeptide 3-beta-N-acetyl-D-glucosaminyltransferase. This enzyme is also called O-fucosylpeptide beta-1,3-N-acetylglucosaminyltransferase. This enzyme participates in notch signaling pathway.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 2.4.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Initiation-specific%20alpha-1%2C6-mannosyltransferase | In enzymology, an initiation-specific alpha-1,6-mannosyltransferase () is an enzyme that catalyzes the chemical reaction in which an alpha-D-mannosyl residue is transferred from GDP-mannose to a lipid-linked oligosaccharide, being linked by an alpha-1,6-D-mannosyl-D-mannose bond.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is GDP-mannose:oligosaccharide 1,6-alpha-D-mannosyltransferase. Other names in common use include alpha-1,6-mannosyltransferase, GDP-mannose:oligosaccharide 1,6-alpha-D-mannosyltransferase, GDP-mannose:glycolipid 1,6-alpha-D-mannosyltransferase, and glycolipid 6-alpha-mannosyltransferase. This enzyme participates in high-mannose type n-glycan biosynthesis.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glycolipid%202-alpha-mannosyltransferase | In enzymology, a glycolipid 2-alpha-mannosyltransferase () is an enzyme that catalyzes the chemical reaction in which an alpha-D-mannosyl residue is transferred from GDP-mannose to lipid-linked oligosaccharide, being attached by an alpha-1,2-D-mannosyl-D-mannose bond.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is GDP-mannose:glycolipid 1,2-alpha-D-mannosyltransferase. Other names in common use include guanosine diphosphomannose-oligosaccharide-lipid, mannosyltransferase, GDP-mannose-oligosaccharide-lipid mannosyltransferase, and oligosaccharide-lipid mannosyltransferase.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and .
References
EC 2.4.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Glycolipid%203-alpha-mannosyltransferase | In enzymology, a glycolipid 3-alpha-mannosyltransferase () is an enzyme that catalyzes the chemical reaction in which an alpha-D-mannosyl residue is transferred from GDP-mannose to a lipid-linked oligosaccharide, being attached by an alpha-1,3-D-mannosyl-D-mannose bond.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is GDP-mannose:glycolipid 1,3-alpha-D-mannosyltransferase. Other names in common use include mannosyltransferase II, guanosine diphosphomannose-oligosaccharide-lipid II, mannosyltransferase, and GDP-mannose-oligosaccharide-lipid mannosyltransferase II. This enzyme participates in the biosynthesis of n-glycan and glycan structures.
References
EC 2.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glycoprotein-fucosylgalactoside%20a-N-acetylgalactosaminyltransferase | In enzymology, a glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase () is an enzyme that catalyzes the chemical reaction
UDP-N-acetyl-D-galactosamine + glycoprotein-alpha-L-fucosyl-(1,2)-D-galactose UDP + glycoprotein-N-acetyl-alpha-D-galactosaminyl-(1,3)-[alpha-L-fucosyl- (1,2)]-D-galactose
Thus, the two substrates of this enzyme are UDP-N-acetyl-D-galactosamine and glycoprotein-alpha-L-fucosyl-(1,2)-D-galactose, whereas its 3 products are UDP, [[glycoprotein-N-acetyl-alpha-D-galactosaminyl-(1,3)-[alpha-L-fucosyl-]], and [[(1,2)]-D-galactose]].
This enzyme belongs to the family of transferases, specifically those glycosyltransferases hexosyltransferases. The systematic name of this enzyme class is UDP-N-acetyl-D-galactosamine:glycoprotein-alpha-L-fucosyl-(1,2)-D-ga lactose 3-N-acetyl-D-galactosaminyltransferase. Other names in common use include A-transferase, histo-blood group A glycosyltransferase, (Fucalpha1→2Galalpha1→3-N-acetylgalactosaminyltransferase), UDP-GalNAc:Fucalpha1→2Galalpha1→3-N-acetylgalactosaminyltransferase, alpha-3-N-acetylgalactosaminyltransferase, blood-group substance alpha-acetyltransferase, blood-group substance A-dependent acetylgalactosaminyltransferase, fucosylgalactose acetylgalactosaminyltransferase, histo-blood group A acetylgalactosaminyltransferase, histo-blood group A transferase, UDP-N-acetyl-D-galactosamine:alpha-L-fucosyl-1,2-D-galactose, and 3-N-acetyl-D-galactosaminyltransferase. This enzyme participates in 3 |
https://en.wikipedia.org/wiki/Ch%C3%A2teau%20La%20Tour%20Haut-Brion | Château La Tour Haut-Brion was a Bordeaux wine estate from the Pessac-Léognan appellation within Graves, and was ranked as a Cru Classé for red wine in the Classification of Graves wine of 1953 and 1959. It was located in close vicinity of the city of Bordeaux, in the commune of Talence, adjoining Château La Mission Haut-Brion.
The estate's final vintage was 2005, after the owners (Domaine Clarence Dillon) decided to discontinue the label. Since then, the fruit from La Tour Haut-Brion has been used in the production of Château La Mission Haut-Brion.
History
Vines were first laid into the ground by the Rostaing family in the 16th century, when the estate was called La Tour de Rostaing, or La Tour d'Esquivens, who also cultivated the vineyards of Arrejedhuys, which became La Mission Haut-Brion. At the onset of the French Revolution the estate belonged to the Saige family. Despite the execution of the estate's heir, his mother the widow Saige refused to evacuate the château, and expropriation of the estate was avoided.
Not until the 19th century did the owners at the time, the Cayrou brothers, add the name of 'Haut-Brion'. Records show that by the 1850 Féret, the full name of La Tour Haut-Brion was acknowledged.
It was acquired by Louis Uzac in 1858 who made restorations and several modernising changes, and in 1890 it was sold to Victor Coustau. After Coustau's death in 1924, the Woltner family, proprietors of neighbouring vineyards Château la Mission Haut-Brion and Château |
https://en.wikipedia.org/wiki/Gamma%20delta%20T%20cell | Gamma delta T cells (γδ T cells) are T cells that have a γδ T-cell receptor (TCR) on their surface. Most T cells are αβ (alpha beta) T cells with TCR composed of two glycoprotein chains called α (alpha) and β (beta) TCR chains. In contrast, γδ T cells have a TCR that is made up of one γ (gamma) chain and one δ (delta) chain. This group of T cells is usually less common than αβ T cells, but are at their highest abundance in the gut mucosa, within a population of lymphocytes known as intraepithelial lymphocytes (IELs).
The antigenic molecules that activate gamma delta T cells are still largely unknown. However, γδ T cells are peculiar in that they do not seem to require antigen processing and major-histocompatibility-complex (MHC) presentation of peptide epitopes, although some recognize MHC class Ib molecules. γδ T cells are believed to have a prominent role in recognition of lipid antigens. They are of an invariant nature and may be triggered by alarm signals, such as heat shock proteins (HSP).
A γδ-T-cell sub-population exists within the epidermal compartment of mice skin. Originally referred to as Thy-1+ dendritic epidermal cells (Thy1+DEC), these cells are more commonly known as dendritic epidermal T cells (DETC). DETCs arise during fetal development and express an invariant and canonical Vγ3 Vδ1 T-cell receptor (using Garman nomenclature).
Innate and adaptive immunity
The conditions that lead to responses of gamma delta T cells are not fully understood, and current con |
https://en.wikipedia.org/wiki/Classification%20of%20Graves%20wine | The wines of Graves in the wine-growing region of Bordeaux were classified in 1953 by a jury appointed by Institute National des Appellations d'Origine, and approved by the Minister of Agriculture in August of that year. The selection was revised with a few additions in February 1959. The classification concerns both red and white wines, and all chateaux belong to the appellation Pessac-Léognan, which eventually came into effect on September 9, 1987.
The 1959 classification
See also
Regional wine classification
Bordeaux wine regions
History of Bordeaux wine
Notes and references
a. Also rated as a Premier Cru in the Bordeaux Wine Official Classification of 1855.
b. Château La Tour Haut-Brion was discontinued after the 2005 vintage.
General
Footnotes
External links
Union of Classed Growths of Graves official site
Appellations
French wine
Bordeaux
Graves wine |
https://en.wikipedia.org/wiki/Stratifin | Stratifin (also known as 14-3-3 protein sigma or 14-3-3σ protein) is a protein encoded by the SFN gene in humans. The protein is named for its presence in stratified epithelial cells.
Interactions
Stratifin has been shown to interact with PLK4, ERRFI1, MARK3, JUB and YWHAG.
References
Further reading
14-3-3 proteins |
https://en.wikipedia.org/wiki/Diablo%20homolog | Diablo homolog (DIABLO) is a mitochondrial protein that in humans is encoded by the DIABLO (direct IAP binding protein with low pI) gene on chromosome 12. DIABLO is also referred to as second mitochondria-derived activator of caspases or SMAC. This protein binds inhibitor of apoptosis proteins (IAPs), thus freeing caspases to activate apoptosis. Due to its proapoptotic function, SMAC is implicated in a broad spectrum of tumors, and small molecule SMAC mimetics have been developed to enhance current cancer treatments.
Structure
Protein
This gene encodes a 130 Å-long, arch-shaped homodimer protein. The full-length protein product spans 239 residues, 55 of which comprise the mitochondrial-targeting sequence (MTS) at its N-terminal. However, once the full-length protein is imported into the mitochondria, this sequence is excised to produce the 184-residue mature protein. This cleavage also exposes four residues at the N-terminal, Ala-Val-Pro-Ile (AVPI), which is the core of the IAP binding domain and crucial for inhibiting XIAP. Specifically, the tetrapeptide sequence binds the BIR3 domain of XIAP to form a stable complex between SMAC and XIAP. The homodimer structure also facilitates SMAC-XIAP binding via the BIR2 domain, though it does not form until the protein is released into the cytoplasm as a result of outer mitochondrial membrane permeabilization. Thus, monomeric SMAC mutants can still bind the BIR3 domain but not the BIR2 domain, which compromises the protein’s inhibit |
https://en.wikipedia.org/wiki/Arrestin%20beta%201 | Arrestin, beta 1, also known as ARRB1, is a protein which in humans is encoded by the ARRB1 gene.
Function
Members of arrestin/beta-arrestin protein family are thought to participate in agonist-mediated desensitization of G protein-coupled receptors and cause specific dampening of cellular responses to stimuli such as hormones, neurotransmitters, or sensory signals. Arrestin beta 1 is a cytosolic protein and acts as a cofactor in the beta-adrenergic receptor kinase (BARK) mediated desensitization of beta-adrenergic receptors. Besides the central nervous system, it is expressed at high levels in peripheral blood leukocytes, and thus the BARK/beta-arrestin system is believed to play a major role in regulating receptor-mediated immune functions. Alternatively spliced transcripts encoding different isoforms of arrestin beta 1 have been described, however, their exact functions are not known.
Beta-arrestin has been shown to play a role as a scaffold that binds intermediates and may direct G-protein signaling by connecting receptors to clathrin-mediated endocytosis.
Interactions
Arrestin beta 1 has been shown to interact with
Arf6,
PTHLH,
DVL2
Mdm2,
OPRD1,
PSCD2, and
RALGDS.
References
Further reading
External links |
https://en.wikipedia.org/wiki/DMPK | DMPK may refer to:
Dystrophia myotonica protein kinase or myotonic dystrophy protein kinase
Drug metabolism and pharmacokinetics |
https://en.wikipedia.org/wiki/DM1 | DM1 can refer to
Diabetes mellitus type 1
A form of Myotonic dystrophy
Myotonin-protein kinase, that is, dystrophia myotonica 1 or dystrophia myotonica protein kinase, a ubiquitous protein whose abnormal expression is associated with myotonic dystrophy in ways not yet well understood
Mertansine, a maytansinoid cytotoxic agent used in trastuzumab emtansine and other antibody-drug conjugates
The Lippisch DM-1 a German delta wing research glider
An office based variant of the ICL Series 39 mainframe manufactured by International Computers Limited (ICL) in the 1980s
SpaceX DM1, an orbital test of Dragon 2 spacecraft
DM-1, one of the designations carried by a US Navy destroyer |
https://en.wikipedia.org/wiki/Easy%20as%20Pie%20%28Billy%20%22Crash%22%20Craddock%20album%29 | Easy as Pie is an album by country singer Billy "Crash" Craddock. It was released on ABC/Dot Records in 1976.
Track listing
"Easy as Pie" (Rory Bourke, Gene Dobbins, Johnny Wilson)
"She's About a Mover"
"Think I'll Go Somewhere (And Cry Myself To Sleep)"
"You Can't Cry It Away"
"Another Woman"
"I Need Someone to Love"
"Walk Softly" (Van McCoy)
"Has A Cat Got A Tail"
"The First Time"
"You Rubbed It In All Wrong" (John Adrian)
"There Won't Be Another Now"
Billy "Crash" Craddock albums
1976 albums |
https://en.wikipedia.org/wiki/4F2%20cell-surface%20antigen%20heavy%20chain | 4F2 cell-surface antigen heavy chain is a protein that in humans is encoded by the SLC3A2 (solute carrier family 3 member 2) gene.
SLC3A2 comprises the heavy subunit of the large neutral amino acid transporter (LAT1) that is also known as CD98 (cluster of differentiation 98).
Function
SLC3A2 is a member of the solute carrier family and encodes a cell surface, transmembrane protein with an alpha-amylase domain. The protein exists as the heavy chain of a heterodimer, covalently bound through di-sulfide bonds to one of several possible light chains. It associates with integrins and mediates integrin-dependent signaling related to normal cell growth and tumorigenesis. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.
LAT1 is a heterodimeric membrane transport protein that preferentially transports neutral branched (valine, leucine, isoleucine) and aromatic (tryptophan, tyrosine, phenylalanine) amino acids. LAT is highly expressed in brain capillaries (which form the blood brain barrier) relative to other tissues.
A functional LAT1 transporter is composed of two proteins encoded by two distinct genes:
4F2hc/CD98 heavy subunit protein encoded by the SLC3A2 gene (this gene)
CD98 light subunit protein encoded by the SLC7A5 gene
Interactions
SLC3A2 has been shown to interact with SLC7A7.
Additionally, SLC3A2 is a constituent member of the system xc- cystine/glutamate antiporter, complexing with SLC7A11.
See also
Heterodime |
https://en.wikipedia.org/wiki/Gene%20Sarazen%20Jun%20Classic | The Gene Sarazen Jun Classic, sometimes shortened to Jun Classic, was a professional golf tournament that was held in Japan from 1977 to 1999. It was an event on the Japan Golf Tour from 1978. It was named in honour of Gene Sarazen, and played at the Jun Classic Country Club and the Rope Club in Tochigi Prefecture.
Tournament hosts
Winners
Notes
References
External links
Japan Golf Tour's Official site
Home page of the Jun Classic C.C.
Former Japan Golf Tour events
Defunct golf tournaments in Japan
Sport in Tochigi Prefecture
1977 establishments in Japan
1999 disestablishments in Japan
Recurring sporting events established in 1977
Recurring sporting events disestablished in 1999
Gene Sarazen |
https://en.wikipedia.org/wiki/DNA%20polymerase%20beta | DNA polymerase beta, also known as POLB, is an enzyme present in eukaryotes. In humans, it is encoded by the POLB gene.
Function
In eukaryotic cells, DNA polymerase beta (POLB) performs base excision repair (BER) required for DNA maintenance, replication, recombination, and drug resistance.
The mitochondrial DNA of mammalian cells is constantly under attack from oxygen radicals released during ATP production. Mammalian cell mitochondria contain an efficient base excision repair system employing POLB that removes some frequent oxidative DNA damages. POLB thus has a key role in maintaining the stability of the mitochondrial genome.
An analysis of the fidelity of DNA replication by polymerase beta in the neurons from young and very aged mice indicated that aging has no significant effect on the fidelity of DNA synthesis by polymerase beta. This finding was considered to provide evidence against the error catastrophe theory of aging.
Base excision repair
Cabelof et al. measured the ability to repair DNA damage by the BER pathway in tissues of young (4-month-old) and old (24-month-old) mice. In all tissues examined (brain, liver, spleen and testes) the ability to repair DNA damage declined significantly with age, and the reduction in repair capability correlated with decreased levels of DNA polymerase beta at both the protein and messenger RNA levels. Numerous investigators have reported an accumulation of DNA damage with age, especially in brain and liver. Cabelof et al |
https://en.wikipedia.org/wiki/POLB | POLB may refer to:
DNA polymerase beta, human enzyme
DNA polymerase II, bacterial enzyme
Port of Long Beach |
https://en.wikipedia.org/wiki/Short%20division | In arithmetic, short division is a division algorithm which breaks down a division problem into a series of easier steps. It is an abbreviated form of long division — whereby the products are omitted and the partial remainders are notated as superscripts.
As a result, a short division tableau is shorter than its long division counterpart — though sometimes at the expense of relying on mental arithmetic, which could limit the size of the divisor.
For most people, small integer divisors up to 12 are handled using memorised multiplication tables, although the procedure could also be adapted to the larger divisors as well.
As in all division problems, a number called the dividend is divided by another, called the divisor. The answer to the problem would be the quotient, and in the case of Euclidean division, the remainder would be included as well.
Using short division, arbitrarily large dividends can be handled.
Tableau
Short division does not use the slash (/) or division sign (÷) symbols. Instead, it displays the dividend, divisor, and quotient (when it is found) in a tableau. An example is shown below, representing the division of 500 by 4. The quotient is 125.
Alternatively, the bar may be placed below the number, which means the sum proceeds down the page. This is in distinction to long division, where the space under the dividend is required for workings:
Example
The procedure involves several steps. As an example, consider 950 divided by 4:
Using the alterna |
https://en.wikipedia.org/wiki/Element%20One | Element One is Lawrence Technological University's race team from Detroit, Michigan that competed in the 2008 Formula Zero Championship, the world's first hydrogen fuel cell race series.
About the Team
The Element One team, formed in January 2007, had over 20 members from the Colleges of Engineering and Arts and Sciences. The team officially entered the competition and submitted initial designs on June 12, 2007. The Element One team placed in the top three during their Step 3 design. The team completed their final design, Step 4 of the design competition, in March 2008. On March 14, 2008, Formula Zero announced that Element One placed 1st in the design competition and was one of six teams to receive a 'race package' from the organizers, which consists of an 8-kW Hydrogenics fuel cell power module and a hydrogen storage cylinder. Teams awarded the race package were permitted to build and race their hydrogen powered race vehicle in the 2008–2009 race series. Races were expected to be held in locations such as the UK, the Netherlands, Spain, the U.S., and several other planned locations.
The first race took place on August 22, 2008 in Rotterdam, the Netherlands. Unfortunately, Element One did not race at the event due to issues with ground clearance. Nonetheless, the team managed to get the vehicle running immediately after the race at the Formula Zero Rotterdam test facility. A video of the vehicle running can be found here. Although it did not race, the Element One vehicl |
https://en.wikipedia.org/wiki/Quantile%20regression | Quantile regression is a type of regression analysis used in statistics and econometrics. Whereas the method of least squares estimates the conditional mean of the response variable across values of the predictor variables, quantile regression estimates the conditional median (or other quantiles) of the response variable. Quantile regression is an extension of linear regression used when the conditions of linear regression are not met.
Advantages and applications
One advantage of quantile regression relative to ordinary least squares regression is that the quantile regression estimates are more robust against outliers in the response measurements. However, the main attraction of quantile regression goes beyond this and is advantageous when conditional quantile functions are of interest. Different measures of central tendency and statistical dispersion can be used to more comprehensively analyze the relationship between variables.
In ecology, quantile regression has been proposed and used as a way to discover more useful predictive relationships between variables in cases where there is no relationship or only a weak relationship between the means of such variables. The need for and success of quantile regression in ecology has been attributed to the complexity of interactions between different factors leading to data with unequal variation of one variable for different ranges of another variable.
Another application of quantile regression is in the areas of growth char |
https://en.wikipedia.org/wiki/Memory%20divider | A memory divider is a ratio which is used to determine the operating clock frequency of computer memory in accordance with front side bus (FSB) frequency, if the memory system is dependent on FSB clock speed. Along with memory latency timings, memory dividers are extensively used in overclocking memory subsystems to find stable, working memory states at higher FSB frequencies. The ratio between DRAM and FSB is commonly referred to as "DRAM:FSB ratio".
Memory dividers are only applicable to those chipsets in which memory speed is dependent on FSB speeds. Certain chipsets like nVidia 680i have separate memory and FSB lanes due to which memory clock and FSB clock are asynchronous and memory dividers are not used there. Setting memory speeds and overclocking memory systems in such chipsets are different issues which do not use memory dividers. This article is only applicable to those chipsets in which the memory clock is dependent on FSB clock.
Overview
Memory Dividers allow system memory to run slower than or faster than the actual FSB (Front Side Bus) speed. Ideally, Front Side Bus and system memory should run at the same clock speed because FSB connects system memory to the CPU, but it is sometimes desired to run the FSB and system memory at different clock speeds. It is possible to run FSB and memory clock at different clock speeds, within certain limits of the motherboard and corresponding chipset. So, settings termed as Memory Divider or FSB/DRAM settings are available a |
https://en.wikipedia.org/wiki/Sema%20domain | The Sema domain is a structural domain of semaphorins, which are a large family of secreted and transmembrane proteins, some of which function as repellent signals during axon guidance. Sema domains also occur in the hepatocyte growth factor receptor (Uniprot: ), Plexin-A3 (Uniprot: ) and in viral proteins.
CD100 (also called SEMA4D) is associated with PTPase and serine kinase activity. CD100 increases PMA, CD3 and CD2 induced T cell proliferation, increases CD45 induced T cell adhesion, induces B cell homotypic adhesion and down-regulates B cell expression of CD23.
The Sema domain is characterised by a conserved set of cysteine residues, which form four disulfide bonds to stabilise the structure. The Sema domain fold is a variation of the beta propeller topology, with seven blades radially
arranged around a central axis. Each blade contains a four- stranded (strands A to D) antiparallel beta sheet. The inner strand of each blade (A) lines the channel at the centre of the propeller, with strands B and C of the same repeat radiating outward, and strand D of the next repeat forming the outer edge of the blade. The large size of the Sema domain is not due to a single inserted domain but results from the presence of additional secondary structure elements inserted in most of the blades. The Sema domain uses a 'loop and hook' system to close the circle between the first and the last blades. The blades are constructed sequentially with an N-terminal beta- strand closing the cir |
https://en.wikipedia.org/wiki/PLAT%20domain | In molecular biology the PLAT domain is a protein domain that is found in a variety of membrane or lipid associated proteins. It is called the PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain<ref
name="PUB00018111"></ref> or LH2 (Lipoxygenase homology) domain. The known structure
of pancreatic lipase shows this domain binds to procolipase , which mediates membrane association.
This domain forms a beta-sandwich composed of two β-sheets of four β-strands each.
Human proteins containing this domain
ALOX12; ALOX12B; ALOX12P2; ALOX15; ALOX15B; ALOX5; ALOXE3; LIPC;
LIPG; LOXHD1; LPL; PKD1; PKD1L1; PKD1L2; PKD1L3; PKDREJ;
PNLIP; PNLIPRP1; PNLIPRP2; PNLIPRP3; RAB6IP1;
References
Protein domains
Peripheral membrane proteins |
https://en.wikipedia.org/wiki/Patatin-like%20phospholipase | Family of patatin-like phospholipases consists of various patatin glycoproteins from the total soluble protein from potato tubers, and also some proteins found in vertebrates. Patatin is a storage protein but it also has the enzymatic activity of phospholipase, catalysing the cleavage of fatty acids from membrane lipids.
Subfamilies
Protein of unknown function UPF0028
Human proteins containing this domain
PNPLA1; PNPLA2; PNPLA3; PNPLA4; PNPLA5; PNPLA6; PNPLA7; PNPLA8;
References
Protein domains
Protein families
Single-pass transmembrane proteins
Hydrolases |
https://en.wikipedia.org/wiki/P120%20catenin | p120 catenin, or simply p120, also called catenin delta-1, is a protein that in humans is encoded by the CTNND1 gene.
Function
This gene encodes a member of the Armadillo protein family, which function in adhesion between cells and signal transduction. Multiple translation initiation codons and alternative splicing result in many different isoforms being translated. Not all of the full-length natures of the described transcript variants have been determined.
Clinical significance
Either loss or cytoplasmic localization of p120 is a common feature in the progression of several types of carcinoma.
Interactions
CTNND1 has been shown to interact with:
β-Catenin,
CDH1,
CDH2,
Collagen, type XVII, alpha 1,
Cortactin,
FYN,
MUC1,
Nephrin,
PSEN1,
PTPN6,
PTPRJ,
PTPRM,
VE-cadherin,
YES1, and
ZBTB33
See also
δ-Catenin
Catenin
CTNND2
References
Further reading
External links
Catenins
Armadillo-repeat-containing proteins |
https://en.wikipedia.org/wiki/SPI1 | Transcription factor PU.1 is a protein that in humans is encoded by the SPI1 gene.
Function
This gene encodes an ETS-domain transcription factor that activates gene expression during myeloid and B-lymphoid cell development. The nuclear protein binds to a purine-rich sequence known as the PU-box found on enhancers of target genes, and regulates their expression in coordination with other transcription factors and cofactors. The protein can also regulate alternative splicing of target genes. Multiple transcript variants encoding different isoforms have been found for this gene.
The PU.1 transcription factor is essential for hematopoiesis and cell fate decisions. PU.1 can physically interact with a variety of regulatory factors like TFIID, GATA-2, GATA-1 and c-Jun. The protein-protein interactions between these factors can regulate PU.1-dependent cell fate decisions. PU.1 can modulate the expression of 3000 genes in hematopoietic cells including cytokines. It is expressed in monocytes, granulocytes, B and NK cells but is absent in T cells, reticulocytes and megakaryocytes. Its transcription is regulated by various mechanisms .
PU.1 is an essential regulator of the pro-fibrotic system. In fibrotic conditions, PU.1 expression is perturbed in fibrotic diseases, resulting in upregulation of fibrosis-associated genes sets in fibroblasts. Disruption of PU.1 in fibrotic fibroblasts leads to them returning into their resting state from pro-fibrotic fibroblasts. PU.1 is seen to be hi |
https://en.wikipedia.org/wiki/YY1 | YY1 (Yin Yang 1) is a transcriptional repressor protein in humans that is encoded by the YY1 gene.
Function
YY1 is a ubiquitously distributed transcription factor belonging to the GLI-Kruppel class of zinc finger proteins. The protein is involved in repressing and activating a diverse number of promoters. Hence, the YY in the name stands for "yin-yang." YY1 may direct histone deacetylases and histone acetyltransferases to a promoter in order to activate or repress the promoter, thus implicating histone modification in the function of YY1. YY1 promotes enhancer-promoter chromatin loops by forming dimers and promoting DNA interactions. Its dysregulation disrupts enhancer-promoter loops and gene expression.
Clinical significance
YY1 heterozygous deletions, missense, and nonsense mutations cause Gabriele-DeVries syndrome (GADEVS), an autosomal dominant neurodevelopmental disorder characterized by intellectual disability, dysmorphic facial features, feeding problems, intrauterine growth restriction, variable cognitive impairment, behavioral problems and other congenital malformations. A website is available in order to collect and share clinical information between clinicians and the families of affected individuals.
Interactions
YY1 has been shown to interact with:
ATF6,
EP300
FKBP3
HDAC3
Histone deacetylase 2
Myc
NOTCH1
RYBP and
SAP30
Serine—tRNA ligase
References
Further reading
External links
Transcription factors |
https://en.wikipedia.org/wiki/Glycine%20receptor%2C%20alpha%201 | Glycine receptor subunit alpha-1 is a protein that in humans is encoded by the GLRA1 gene.
Function
The inhibitory glycine receptor mediates postsynaptic inhibition in the spinal cord and other regions of the central nervous system. It is a pentameric receptor composed solely of alpha subunits. The GLRB gene encodes the alpha subunit of the receptor.
Clinical significance
Mutations in the gene have been associated with hyperekplexia, a neurologic syndrome associated with an exaggerated startle reaction.
See also
Glycine receptor
Stiff person syndrome
Hyperekplexia
References
Further reading
External links
Ion channels |
https://en.wikipedia.org/wiki/CYP3A5 | Cytochrome P450 3A5 is a protein that in humans is encoded by the CYP3A5 gene.
Tissue distribution
CYP3A5 encodes a member of the cytochrome P450 superfamily of enzymes. Like most of the cytochrome P450, the CYP3A5 is expressed in the prostate and the liver. It is also expressed in epithelium of the small intestine and large intestine for uptake and in small amounts in the bile duct, nasal mucosa, kidney, adrenal cortex, epithelium of the gastric mucosa with intestinal metaplasia, gallbladder, intercalated ducts of the pancreas, chief cells of the parathyroid and the corpus luteum of the ovary (at protein level).
Clinical significance
The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. This protein localizes to the endoplasmic reticulum and its expression is induced by glucocorticoids and some pharmacological agents. The enzyme metabolizes drugs such as nifedipine and cyclosporine as well as the steroid hormones testosterone, progesterone and androstenedione. This gene is part of a cluster of cytochrome P450 genes on chromosome 7q21.1. This cluster includes a pseudogene, CYP3A5P1, which is very similar to CYP3A5. This similarity has caused some difficulty in determining whether cloned sequences represent the gene or the pseudogene.
CYP3A4/3A5 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electro |
https://en.wikipedia.org/wiki/Fucosyltransferase%203 | Galactoside 3(4)-L-fucosyltransferase is an enzyme that in humans is encoded by the FUT3 gene.
Function
The Lewis histo-blood group system comprises a set of fucosylated glycosphingolipids that are synthesized by exocrine epithelial cells and circulate in body fluids. The glycosphingolipids function in embryogenesis, tissue differentiation, tumor metastasis, inflammation, and bacterial adhesion. They are secondarily absorbed to red blood cells giving rise to their Lewis phenotype. This gene is a member of the fucosyltransferase family, which catalyzes the addition of fucose to precursor polysaccharides in the last step of Lewis antigen biosynthesis. It encodes an enzyme with alpha(1,3)-fucosyltransferase and alpha(1,4)-fucosyltransferase activities. Mutations in this gene are responsible for the majority of Lewis antigen-negative phenotypes. Multiple alternatively spliced variants, encoding the same protein, have been found for this gene.
See also
Cluster of differentiation
References
Further reading
External links
Clusters of differentiation |
https://en.wikipedia.org/wiki/Delta-like%201 | Delta-like protein 1 is a protein that in humans is encoded by the DLL1 gene.
Function
DLL1 is a human homolog of the Notch Delta ligand and is a member of the delta/serrate/jagged family. It plays a role in mediating cell fate decisions during hematopoiesis. It may play a role in cell-to-cell communication.
Interactions
Delta-like 1 has been shown to interact with NOTCH2
References
Further reading |
https://en.wikipedia.org/wiki/Diazepam%20binding%20inhibitor | Acyl-CoA-binding protein in humans belongs to the family of Acyl-CoA-binding proteins.
This gene encodes diazepam binding inhibitor, a protein that is regulated by hormones and is involved in lipid metabolism and the displacement of beta-carbolines and benzodiazepines, which modulate signal transduction at type A gamma-aminobutyric acid receptors located in brain synapses. The protein is conserved from yeast to mammals, with the most highly conserved domain consisting of seven contiguous residues that constitute the hydrophobic binding site for medium- and long-chain acyl-Coenzyme A esters. Diazepam binding inhibitor also mediates the feedback regulation of pancreatic secretion and the postprandial release of cholecystokinin, in addition to its role as a mediator in corticotropin-dependent synthesis of steroids in the adrenal gland.
Three pseudogenes located on chromosomes 6, 8 and 16 have been identified. Multiple transcript variants encoding different isoforms have also been described for this gene.
See also
Diazepam
References
Further reading |
https://en.wikipedia.org/wiki/GJB6 | Gap junction beta-6 protein (GJB6), also known as connexin 30 (Cx30) — is a protein that in humans is encoded by the GJB6 gene. Connexin 30 (Cx30) is one of several gap junction proteins expressed in the inner ear. Mutations in gap junction genes have been found to lead to both syndromic and nonsyndromic deafness. Mutations in this gene are associated with Clouston syndrome (i.e., hydrotic ectodermal dysplasia).
Function
The connexin gene family codes for the protein subunits of gap junction channels that mediate direct diffusion of ions and metabolites between the cytoplasm of adjacent cells. Connexins span the plasma membrane 4 times, with amino- and carboxy-terminal regions facing the cytoplasm. Connexin genes are expressed in a cell type-specific manner with overlapping specificity. The gap junction channels have unique properties depending on the type of connexins constituting the channel.[supplied by OMIM]
Connexin 30 is prevalent in the two distinct gap junction systems found in the cochlea: the epithelial cell gap junction network, which couple non-sensory epithelial cells, and the connective tissue gap junction network, which couple connective tissue cells. Gap junctions serve the important purpose of recycling potassium ions that pass through hair cells during mechanotransduction back to the endolymph.
Connexin 30 has been found to be co-localized with connexin 26. Cx30 and Cx26 have also been found to form heteromeric and heterotypic channels. The bioche |
https://en.wikipedia.org/wiki/TYH | TYH or tyh may refer to:
Tsan Yuk Hospital, a public hospital in Sai Ying Pun, Hong Kong
Tyrosine hydroxylase the enzyme responsible for catalyzing the conversion of L-tyrosine to L-DOPA
tyh, the ISO 639-3 code for the O'du language in Vietnam and Laos
Thank You Hashem |
https://en.wikipedia.org/wiki/Flap%20structure-specific%20endonuclease%201 | Flap endonuclease 1 is an enzyme that in humans is encoded by the FEN1 gene.
Function
The protein encoded by this gene removes 5' overhanging "flaps" (or short sections of single stranded DNA that "hang off" because their nucleotide bases are prevented from binding to their complementary base pair—despite any base pairing downstream) in DNA repair and processes the 5' ends of Okazaki fragments in lagging strand DNA synthesis. Direct physical interaction between this protein and AP endonuclease 1 during long-patch base excision repair provides coordinated loading of the proteins onto the substrate, thus passing the substrate from one enzyme to another. The protein is a member of the XPG/RAD2 endonuclease family and is one of ten proteins essential for cell-free DNA replication. DNA secondary structure can inhibit flap processing at certain trinucleotide repeats in a length-dependent manner by concealing the 5' end of the flap that is necessary for both binding and cleavage by the protein encoded by this gene. Therefore, secondary structure can deter the protective function of this protein, leading to site-specific trinucleotide expansions.
Interactions
Flap structure-specific endonuclease 1 has been shown to interact with:
APEX1,
BLM
CDK2,
CCNA2,
EP300,
HNRNPA1,
PCNA, and
WRN.
Over expression of FEN1 in cancers
FEN1 is over-expressed in the majority of cancers of the breast, prostate, stomach, neuroblastomas, pancreatic, and lung.
FEN1 is an essential enzy |
https://en.wikipedia.org/wiki/Neuropilin%201 | Neuropilin-1 is a protein that in humans is encoded by the NRP1 gene. In humans, the neuropilin 1 gene is located at 10p11.22. This is one of two human neuropilins.
Function
NRP1 is a membrane-bound coreceptor to a tyrosine kinase receptor for both vascular endothelial growth factor (for example, VEGFA) and semaphorin (for example, SEMA3A) family members. NRP1 plays versatile roles in angiogenesis, axon guidance, cell survival, migration, and invasion.[supplied by OMIM]
Interactions
Neuropilin 1 has been shown to interact with Vascular endothelial growth factor A.
Role in COVID-19
Research has shown that neuropilin 1 facilitates entry of SARS-CoV-2 into cells, making it a possible target for future antiviral drugs.
Implication in cancer
Neuropilin 1 has been implicated in the vascularization and progression of cancers. NRP1 expression has been shown to be elevated in a number of human patient tumor samples, including brain, prostate, breast, colon, and lung cancers and NRP1 levels are positively correlated with metastasis.
In prostate cancer NRP1 has been demonstrated to be an androgen-suppressed gene, upregulated during the adaptive response of prostate tumors to androgen-targeted therapies and a prognostic biomarker of clinical metastasis and lethal PCa. In vitro and in vivo mouse studies have shown membrane bound NRP1 to be proangiogenic and that NRP1 promotes the vascularization of prostate tumors.
Elevated NRP1 expression is also correlated with the invasiv |
https://en.wikipedia.org/wiki/Metal-induced%20gap%20states | In bulk semiconductor band structure calculations, it is assumed that the crystal lattice (which features a periodic potential due to the atomic structure) of the material is infinite. When the finite size of a crystal is taken into account, the wavefunctions of electrons are altered and states that are forbidden within the bulk semiconductor gap are allowed at the surface. Similarly, when a metal is deposited onto a semiconductor (by thermal evaporation, for example), the wavefunction of an electron in the semiconductor must match that of an electron in the metal at the interface. Since the Fermi levels of the two materials must match at the interface, there exists gap states that decay deeper into the semiconductor.
Band-bending at the metal-semiconductor interface
As mentioned above, when a metal is deposited onto a semiconductor, even when the metal film as small as a single atomic layer, the Fermi levels of the metal and semiconductor must match. This pins the Fermi level in the semiconductor to a position in the bulk gap. Shown to the right is a diagram of band-bending interfaces between two different metals (high and low work functions) and two different semiconductors (n-type and p-type).
Volker Heine was one of the first to estimate the length of the tail end of metal electron states extending into the semiconductor's energy gap. He calculated the variation in surface state energy by matching wavefunctions of a free-electron metal to gapped states in an undop |
https://en.wikipedia.org/wiki/EPH%20receptor%20A2 | EPH receptor A2 (ephrin type-A receptor 2) is a protein that in humans is encoded by the EPHA2 gene.
Function
This gene belongs to the ephrin receptor subfamily of the protein-tyrosine kinase family. EPH and EPH-related receptors have been implicated in mediating developmental events, particularly in the nervous system. Receptors in the EPH subfamily typically have a single kinase domain and an extracellular region containing a Cys-rich domain and 2 fibronectin type III repeats. The ephrin receptors are divided into two groups based on the similarity of their extracellular domain sequences and their affinities for binding ephrin-A and ephrin-B ligands. This gene encodes a protein that binds ephrin-A ligands.
Clinical significance
It may be implicated in BRAF mutated melanomas becoming resistant to BRAF-inhibitors and MEK inhibitors. It is also the receptor by which Kaposi's sarcoma-associated herpesvirus (KSHV) enters host cells; small molecule inhibitors of EphA2 have shown some ability to block KSHV entry into human cells.
Interactions
EPH receptor A2 has been shown to interact with:
Ephrin_A1
ACP1
Grb2,
PIK3R1, and
SHC1.
It was also shown that doxazosin is a small molecule agonist of EPH receptor A2.
References
Further reading
External links
Tyrosine kinase receptors |
https://en.wikipedia.org/wiki/Collagen%2C%20type%20IV%2C%20alpha%203 | Collagen alpha-3(IV) chain is a protein that in humans is encoded by the COL4A3 gene.
Type IV collagen, the major structural component of basement membranes, is a multimeric protein composed of 3 alpha subunits; this gene encodes the alpha 3 subunit. These subunits are encoded by 6 different genes, alpha 1 through alpha 6, each of which can form a triple helix structure with 2 other subunits to form type IV collagen. In Goodpasture's syndrome, autoantibodies bind to the collagen molecules in the basement membranes of alveoli and glomeruli. The epitopes that elicit these autoantibodies are localized largely to the non-collagenous C-terminal domain of the protein. A specific kinase phosphorylates amino acids in this same C-terminal region and the expression of this kinase is upregulated during pathogenesis. There are multiple alternate transcripts that appear to be unique to this human alpha 3 gene and alternate splicing is restricted to the six exons that encode this C-terminal domain. This gene is also linked to an autosomal recessive form of Alport syndrome. The mutations contributing to this syndrome are also located within the exons that encode this C-terminal region. Like the other members of the type IV collagen gene family, this gene is organized in a head-to-head conformation with another type IV collagen gene so that each gene pair shares a common promoter. Some exons of this gene are interspersed with exons of an uncharacterized gene which is on the opposite strand. |
https://en.wikipedia.org/wiki/Collagen%2C%20type%20IV%2C%20alpha%201 | Collagen alpha-1(IV) chain (COL4A1) is a protein that in humans is encoded by the COL4A1 gene on chromosome 13. It is ubiquitously expressed in many tissues and cell types. COL4A1 is a subunit of the type IV collagen and plays a role in angiogenesis. Mutations in the gene have been linked to diseases of the brain, muscle, kidney, eye, and cardiovascular system. The COL4A1 gene also contains one of 27 SNPs associated with increased risk of coronary artery disease.
Structure
Gene
The COL4A1 gene resides on chromosome 13 at the band 13q34 and contains 54 exons.[5] This gene produces 2 isoforms through alternative splicing.
Protein
COL4A1 belongs to the type IV collagen family and contains three domains: a short N-terminal domain, a long triple-helical 7S domain at its center, and a non-collagenous 1 (NC1) domain at its C-terminal. The triple-helical domain contains interrupted G-X-Y repeats, which is suspected to allow flexibility of the domain. The NC1 domain is composed of two trimeric caps, each containing two alpha 1 fragments and one alpha 2 fragment, that form a sixfold propeller arranged around an axial tunnel. The interaction between these two caps occurs along a large planar interface and is stabilized by a covalent cross-link between the alpha 1 and alpha 2 chains across the two caps.
Function
Type IV collagen is the major structural component of basement membranes, which contains two or three COL4A1 proteins. Thus, COL4A1 is abundant and found in all types of |
https://en.wikipedia.org/wiki/T-cell%20surface%20glycoprotein%20CD3%20epsilon%20chain | CD3e molecule, epsilon also known as CD3E is a polypeptide which in humans is encoded by the CD3E gene which resides on chromosome 11.
Function
The protein encoded by this gene is the CD3-epsilon polypeptide, which together with CD3-gamma, -delta and -zeta, and the T-cell receptor alpha/beta and gamma/delta heterodimers, forms the T cell receptor-CD3 complex. This complex plays an important role in coupling antigen recognition to several intracellular signal-transduction pathways. The genes encoding the epsilon, gamma and delta polypeptides are located in the same cluster on chromosome 11. The epsilon polypeptide plays an essential role in T-cell development.
Clinical significance
Defects in this gene cause severe immunodeficiency. This gene has also been linked to a susceptibility to type I diabetes in women.
Interactions
T-cell surface glycoprotein CD3 epsilon chain has been shown to interact with TOP2B, CD3EAP and NCK2.
See also
CD3 (immunology)
Cluster of differentiation
References
Further reading
Clusters of differentiation |
https://en.wikipedia.org/wiki/Retinoblastoma-like%20protein%201 | Retinoblastoma-like 1 (p107), also known as RBL1, is a protein that in humans is encoded by the RBL1 gene.
Function
The protein encoded by this gene is similar in sequence and possibly function to the product of the retinoblastoma 1 (RB1) gene. The RB1 gene product is a tumor suppressor protein that appears to be involved in cell cycle regulation, as it is phosphorylated in the S to M phase transition and is dephosphorylated in the G1 phase of the cell cycle. Both the RB1 protein and the product of this gene can form a complex with adenovirus E1A protein and SV40 Large T-antigen, with the SV40 large T-antigen binding only to the unphosphorylated form of each protein. In addition, both proteins can inhibit the transcription of cell cycle genes containing E2F binding sites in their promoters. Due to the sequence and biochemical similarities with the RB1 protein, it is thought that the protein encoded by this gene may also be a tumor suppressor. Two transcript variants encoding different isoforms have been found for this gene.
Interactions
Retinoblastoma-like protein 1 has been shown to interact with:
BEGAIN,
BRCA1,
BRF1,
Cyclin A2,
Cyclin-dependent kinase 2,
E2F1,
HDAC1,
MYBL2
Mothers against decapentaplegic homolog 3,
Prohibitin, and
RBBP8.
See also
Pocket protein family
References
Further reading
External links
Transcription factors |
https://en.wikipedia.org/wiki/Valosin-containing%20protein | Valosin-containing protein (VCP) or transitional endoplasmic reticulum ATPase (TER ATPase) also known as p97 in mammals and CDC48 in S. cerevisiae, is an enzyme that in humans is encoded by the VCP gene. The TER ATPase is an ATPase enzyme present in all eukaryotes and archaebacteria. Its main function is to segregate protein molecules from large cellular structures such as protein assemblies, organelle membranes and chromatin, and thus facilitate the degradation of released polypeptides by the multi-subunit protease proteasome.
VCP/p97/CDC48 is a member of the AAA+ (extended family of ATPases associated with various cellular activities) ATPase family. Enzymes of this family are found in all species from bacteria to humans. Many of them are important chaperones that regulate folding or unfolding of substrate proteins. VCP is a type II AAA+ ATPase, which means that it contains two tandem ATPase domains (named D1 and D2, respectively) (Figure 1). The two ATPase domains are connected by a short polypeptide linker. A domain preceding the D1 domain (N-terminal domain) and a short carboxyl-terminal tail are involved in interaction with cofactors. The N-domain is connected to the D1 domain by a short N-D1 linker.
Most known substrates of VCP are modified with ubiquitin chains and degraded by the 26S proteasome. Accordingly, many VCP coenzymes and adaptors have domains that can recognize ubiquitin. It has become evident that the interplays between ubiquitin and VCP cofactors ar |
https://en.wikipedia.org/wiki/Ataxin%203 | Ataxin-3 is a protein that in humans is encoded by the ATXN3 gene.
Clinical significance
Machado–Joseph disease, also known as spinocerebellar ataxia-3, is an autosomal dominant neurologic disorder. The protein encoded by the ATXN3 gene contains CAG repeats in the coding region, and the expansion of these repeats from the normal 13-36 to 68-79 is the cause of Machado–Joseph disease. This disorder is thus a trinucleotide repeat disorder type I known as a polyglutamine (PolyQ) disease. There is an inverse correlation between the age of onset and CAG repeat numbers. Alternatively spliced transcript variants encoding different isoforms have been described for this gene.
Interactions
Ataxin 3 has been shown to interact with:
RAD23A,
RAD23B, and
VCP.
Model organisms
Model organisms have been used in the study of ATXN3 function. A conditional knockout mouse line called Atxn3tm1a(KOMP)Wtsi was generated at the Wellcome Trust Sanger Institute. Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion. Additional screens performed: - In-depth immunological phenotyping - in-depth bone and cartilage phenotyping
References
Further reading
External links
GeneReviews/NCBI/NIH/UW entry on Spinocerebellar Ataxia Type 3
Proteins |
https://en.wikipedia.org/wiki/Matrix%20metallopeptidase%2013 | Collagenase 3 is an enzyme that in humans is encoded by the MMP13 gene. It is a member of the matrix metalloproteinase (MMP) family. Like most MMPs, it is secreted as an inactive pro-form. MMP-13 has an predicted molecular weight around 54 kDa. It is activated once the pro-domain is cleaved, leaving an active enzyme composed of the catalytic domain and the hemopexin-like domain . Although the actual mechanism has not been described, the hemopexin domain participates in collagen degradation, the catalytic domain alone being particularly inefficient in collagen degradation. During embryonic development, MMP-13 is expressed in the skeleton as required for restructuring the collagen matrix for bone mineralization. In pathological situations it is highly overexpressed; this occurs in human carcinomas, rheumatoid arthritis and osteoarthritis.
Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMPs are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. The protein encoded by this gene cleaves type II collagen more efficiently than types I and III. It may be involved in articular cartilage turnover and cartilage pathophysiology associated with osteoarthritis. The gene is part of a cluster of MMP genes which loc |
https://en.wikipedia.org/wiki/OxMetrics | OxMetrics is an econometric software including the Ox programming language for econometrics and statistics, developed by Jurgen Doornik and David Hendry. OxMetrics originates from PcGive, one of the first econometric software for personal computers, initiated by David Hendry in the 1980s at the London School of Economics.
OxMetrics builds on the Ox programming language of Jurgen Doornik developed at University of Oxford. describes the history of econometric software packages.
OxMetrics is a family of software packages for the econometric and financial analysis of time series, forecasting, econometric model selection and for the statistical analysis of cross-sectional data and panel data.
The main modules apart from PcGive for dynamic econometric models (ARDL, VAR, GARCH, Switching, Autometrics), panel data models (DPD), limited dependent models, are STAMP for structural time series modelling, "SsfPack" for State space methods and "G@RCH" for financial volatility modelling. present many empirical examples in PcGive for OxMetrics in their econometrics textbook. give modern examples in their time series analysis textbook.
See also
Econometric software
Comparison of statistical packages
References
External links
OxMetrics Homepage
PcGive
STAMP software
G@RCH software
Comparison of mathematical programs for data analysis ScientificWeb
Support
Ox mailing list
Econometrics software
Statistical programming languages
Proprietary commercial software for Linux |
https://en.wikipedia.org/wiki/Vector%20Graphic | Vector Graphic, Inc., was an early microcomputer company founded in 1976, the same year as Apple Computer, during the pre-IBM PC era, along with the NorthStar Horizon, IMSAI, and MITS Altair.
History
The first product was a memory card for the S-100 bus. A full microcomputer using the Z80 microprocessor, the Vector 1, was introduced in 1977. There were several Vector Graphic models produced. The Vector 1+ had a floppy disk drive. The Vector Graphic 3 had a fixed keyboard housed anchoring a combined screen terminal and CPU case. The Vector Graphic 4 was a transitional 8-bit and 16-bit hybrid model.
Although primarily used with the CP/M operating system, the Vector 3 ran several others including OASIS, Micropolis Disk Operating System (MDOS), and Micropolis Z80 Operating System (MZOS).
Early Vector Graphic models used the Micropolis floppy disk controller and Micropolis floppy disk drives. Later models were designed with the integrated floppy drive-hard drive controller and used Tandon floppy drives.
Almost all used unusual 100-track per inch 5 ¼-inch floppy drives and 16-sector hard sector media. Some models included 8-inch floppy drives and hard disk drives.
Vector Graphic sales peaked in 1982, by which time the company was publicly traded, at $36 million. It faltered soon after due to several factors. The introduction of the IBM PC in August 1981 shifted the market and smaller players lost momentum. The Vector 4 was accidentally pre-announced in April 1982, the same |
https://en.wikipedia.org/wiki/Aubin%E2%80%93Lions%20lemma | In mathematics, the Aubin–Lions lemma (or theorem) is the result in the theory of Sobolev spaces of Banach space-valued functions, which provides a compactness criterion that is useful in the study of nonlinear evolutionary partial differential equations. Typically, to prove the existence of solutions one first constructs approximate solutions (for example, by a Galerkin method or by mollification of the equation), then uses the compactness lemma to show that there is a convergent subsequence of approximate solutions whose limit is a solution.
The result is named after the French mathematicians Jean-Pierre Aubin and Jacques-Louis Lions. In the original proof by Aubin, the spaces X0 and X1 in the statement of the lemma were assumed to be reflexive, but this assumption was removed by Simon, so the result is also referred to as the Aubin–Lions–Simon lemma.
Statement of the lemma
Let X0, X and X1 be three Banach spaces with X0 ⊆ X ⊆ X1. Suppose that X0 is compactly embedded in X and that X is continuously embedded in X1. For , let
(i) If then the embedding of into is compact.
(ii) If and then the embedding of into is compact.
See also
Lions–Magenes lemma
Notes
References
(Theorem II.5.16)
(Sect.7.3)
(Proposition III.1.3)
Banach spaces
Theorems in functional analysis
Lemmas in analysis
Measure theory |
https://en.wikipedia.org/wiki/Shock-capturing%20method | In computational fluid dynamics, shock-capturing methods are a class of techniques for computing inviscid flows with shock waves. The computation of flow containing shock waves is an extremely difficult task because such flows result in sharp, discontinuous changes in flow variables such as pressure, temperature, density, and velocity across the shock.
Method
In shock-capturing methods, the governing equations of inviscid flows (i.e. Euler equations) are cast in conservation form and any shock waves or discontinuities are computed as part of the solution. Here, no special treatment is employed to take care of the shocks themselves, which is in contrast to the shock-fitting method, where shock waves are explicitly introduced in the solution using appropriate shock relations (Rankine–Hugoniot relations). The shock waves predicted by shock-capturing methods are generally not sharp and may be smeared over several grid elements. Also, classical shock-capturing methods have the disadvantage that unphysical oscillations (Gibbs phenomenon) may develop near strong shocks.
Euler equations
The Euler equations are the governing equations for inviscid flow. To implement shock-capturing methods, the conservation form of the Euler equations are used. For a flow without external heat transfer and work transfer (isoenergetic flow), the conservation form of the Euler equation in Cartesian coordinate system can be written as
where the vectors , , , and are given by
where is the total ener |
https://en.wikipedia.org/wiki/Oncoantigen | An oncoantigen is a surface or soluble tumor antigen that supports tumor growth. A major problem of cancer immunotherapy is the selection of tumor cell variants that escape immune recognition. The notion of oncoantigen was set forth in the context of cancer immunoprevention to define a class of persistent tumor antigens not prone to escape from immune recognition.
Features of oncoantigens
Extracellular localization
Localization of oncoantigens outside tumor cells allows recognition by antibodies if downregulation of class I major histocompatibility complex (MHC-I) molecules prevents T cell recognition. Most tumor antigens are intracellular proteins. Circulating antibodies do not penetrate inside cells, hence intracellular proteins are only recognized by T cells as MHC-I-bound antigenic peptides exposed on the surface of tumor cells. However downmodulation or complete loss of MHC-I expression occurs in most human tumors, making them altogether invisible to the immune system of the host. When tumor cells downregulate MHC-I, only antigens expressed on the cell surface and/or secreted in the extracellular fluids can be recognized by antibodies.
Support of the neoplastic phenotype
Loss of oncoantigen expression is unlikely, because oncoantigens support tumor growth. Loss of tumor antigen expression is another cause of escape from immune recognition. This occurs because most tumor antigens are not essential for tumor growth. Hence loss of expression does not decrease the fitness |
https://en.wikipedia.org/wiki/EN%2062262 | The European Standard EN 62262 — the equivalent of international standard IEC 62262 (2002) — relates to IK (impact protection) ratings. This is an international numeric classification for the degrees of protection provided by enclosures for electrical equipment against external mechanical impacts. It provides a means of specifying the capacity of an enclosure to protect its contents from external impacts. The IK Code was originally defined in European Standard BS EN 50102 (1995, amended 1998). Following its adoption as an international standard in 2002, the European standard was renumbered EN 62262.
Before the advent of the IK code, a third numeral had been occasionally added to the closely related IP Code on ingress protection, to indicate the level of impact protection — e.g. IP66(9). Nonstandard use of this system was one of the factors leading to the development of this standard, which uses a separate two numeral code to distinguish it from the old differing systems. The standard came into effect in October 1995 and conflicting national standards had to be withdrawn by April 1997.
IK ratings help to classify products by its resistance to impacts by Kinetic energy, while EN 62262 specifies the way enclosures should be mounted when tests are carried out, the atmospheric conditions that should prevail, the number of impacts (5) and their (even) distribution, and the size, style, material, dimensions etc. of the various types of hammer designed to produce the energy levels |
https://en.wikipedia.org/wiki/Packet%20concatenation | Packet concatenation is a computer networking optimization that coalesces multiple packets under a single header. The use of packet containment reduces the overhead at the physical and link layers.
See also
Frame aggregation
Packet aggregation
References
Computer networking
Packets (information technology) |
https://en.wikipedia.org/wiki/Haberlin | Häberlin, anglicized Haberlin or Haeberlin, is a Germanic surname common in Germany, Austria, and Switzerland. Through widespread diffusion of ethnic Germans during the late 1700s to early 1900s across Northeastern Europe, the name is also common in countries such as the Czech Republic, Poland, and Lithuania. The name has its origins in an Old German term meaning 'grower of oats'. In Switzerland it is often rendered as Haeberli. It may refer to:
Brian Haberlin (born 1963), comic book creator
Eduard Häberlin (1820–1884), Swiss politician
Friedrich Heinrich Häberlin (1834–1897), Swiss politician, brother of Eduard
Georg Heinrich Häberlin (1644–1699), German Lutheran theologian
Heinrich Häberlin (1868–1947), Swiss politician, son of Friedrich Heinrich and nephew of Eduard
Paul Häberlin (1878–1960), Swiss philosopher
Carl Haeberlin (1870–1954), sometimes also spelled Häberlin, German physician and natural historian
Herman Karl Haeberlin (1890–1918), German-American anthropologist
Paul Haeberlin (chef) (1923–2008), French chef
Carl von Häberlin (1832–1911), German painter
See also
Häberli
Heaberlin
German-language surnames
Swiss-German surnames |
https://en.wikipedia.org/wiki/Algorithms%20%2B%20Data%20Structures%20%3D%20Programs | Algorithms + Data Structures = Programs is a 1976 book written by Niklaus Wirth covering some of the fundamental topics of system engineering, computer programming, particularly that algorithms and data structures are inherently related. For example, if one has a sorted list one will use a search algorithm optimal for sorted lists.
The book was one of the most influential computer science books of the time and, like Wirth's other work, was extensively used in education.
The Turbo Pascal compiler written by Anders Hejlsberg was largely inspired by the Tiny Pascal compiler in Niklaus Wirth's book.
Chapter outline
Chapter 1 - Fundamental Data Structures
Chapter 2 - Sorting
Chapter 3 - Recursive Algorithms
Chapter 4 - Dynamic Information Structures
Chapter 5 - Language Structures and Compilers
Appendix A - the ASCII character set
Appendix B - Pascal syntax diagrams
See also
Code: The Hidden Language of Computer Hardware and Software
References
External links
ETH Zurich / N. Wirth / Books / Compilerbau: Algorithms + Data Structures = Programs (archive.org link)
N. Wirth, Algorithms and Data Structures (1985 edition, updated for Oberon in August 2004. Pdf at ETH Zurich) (archive.org link)
Computer programming books
History of computing
Computer science books
1976 non-fiction books
Prentice Hall books |
https://en.wikipedia.org/wiki/Tundra%20climate | The tundra climate is a polar climate sub-type located in high latitudes and high mountains. It is classified as ET according to Köppen climate classification. It is a climate which at least one month has an average temperature high enough to melt snow (), but no month with an average temperature in excess of .
It is important to note the existence of another variation called alpine tundra. Alpine tundra refers to the tundra environment found at high altitudes, usually above the treeline. It is mostly located at high elevation montane grasslands and shrublands, including the puna and páramo in South America, subalpine heath in New Guinea and East Africa, steppes of the Tibetan plateaus, as well as other similar subalpine habitats around the world. This type of tundra climate exhibits similar characteristics to its polar counterpart but is specifically associated with elevated landscapes.
Despite the potential diversity of climates in the ET category involving precipitation, extreme temperatures, and relative wet and dry seasons, this category is rarely subdivided. Rainfall and snowfall are generally slight due to the low vapor pressure of water in the chilly atmosphere, but as a rule potential evapotranspiration is extremely low, allowing soggy terrain of swamps and bogs even in places that get precipitation typical of deserts of lower and middle latitudes. The amount of native tundra biomass depends more on the local temperature than the amount of precipitation.
There als |
https://en.wikipedia.org/wiki/Retinitis%20pigmentosa%20GTPase%20regulator | X-linked retinitis pigmentosa GTPase regulator is a GTPase-binding protein that in humans is encoded by the RPGR gene. The gene is located on the X-chromosome and is commonly associated with X-linked retinitis pigmentosa (XLRP). In photoreceptor cells, RPGR is localized in the connecting cilium which connects the protein-synthesizing inner segment to the photosensitive outer segment and is involved in the modulation of cargo trafficked between the two segments.
Function
This gene encodes a protein with a series of six RCC1-like domains (RLDs), characteristic of the highly conserved guanine nucleotide exchange factors. Mutations in this gene have been associated with X-linked retinitis pigmentosa (XLRP). Multiple alternatively spliced transcript variants that encode different isoforms of this gene have been reported, but the full-length natures of only some have been determined.
The two major isoforms are RPGRconst, the default isoform, composed of exons 1-19, and RPGRORF15 which retains part of intron 15 as the terminal exon. ORF15 is the terminal exon of RPGRORF15 and is a mutational hotspot accounting for ~60% of RPGR patients with heterogeneous diseases ranging from XLRP to cone-rod degeneration and macular degeneration. Alternatively, the RPGRconst isoform contains a putative prenylation domain on its C-terminal end which is involved in posttranslational modification and allows membrane-association and protein trafficking. The C-terminal domain of the RPGRconst isofor |
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