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wiki_9500_chunk_0 | Glycoside hydrolase family 6 | In molecular biology, glycoside hydrolase family 6 is a family of glycoside hydrolases EC 3.2.1., which are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycoside hydrolases, based... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9501_chunk_0 | Glycoside hydrolase family 6 | The active site of CBHII is located at the C-terminal end of a parallel beta barrel, in an enclosed tunnel through which the cellulose threads. Two aspartic acid residues, located in the centre of the tunnel are the probable catalytic residues. == References == | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9502_chunk_0 | Glycoside hydrolase family 62 | In molecular biology, glycoside hydrolase family 62 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycoside h... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9503_chunk_0 | Glycoside hydrolase family 63 | In molecular biology, glycoside hydrolase family 63 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycoside h... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9504_chunk_0 | Glycoside hydrolase family 63 | They catalyse the specific cleavage of the non-reducing terminal glucose residue from Glc(3)Man(9)GlcNAc(2). Mannosyl oligosaccharide glucosidase EC 3.2.1.106 is the first enzyme in the N-linked oligosaccharide processing pathway. == References == | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9505_chunk_0 | Glycoside hydrolase family 65 | In molecular biology, glycoside hydrolase family 65 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycoside h... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9506_chunk_0 | Glycoside hydrolase family 65 | Maltose phosphorylase (MP) is a dimeric enzyme that catalyzes the conversion of maltose and inorganic phosphate into beta-D-glucose-1-phosphate and glucose. It consists of three structural domains. The C-terminal domain forms a two layered jelly roll motif. | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9507_chunk_0 | Glycoside hydrolase family 65 | This domain is situated at the base of the catalytic domain, however its function remains unknown. The central domain is the catalytic domain, which binds a phosphate ion that is proximal the highly conserved Glu. The arrangement of the phosphate and the glutamate is thought to cause nucleophilic attack on the anomeric... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9508_chunk_0 | Glycoside hydrolase family 65 | The catalytic domain also forms the majority of the dimerisation interface. The N-terminal domain is believed to be essential for catalytic activity although its precise function remains unknown. == References == | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9509_chunk_0 | Glycoside hydrolase family 66 | In molecular biology, glycoside hydrolase family 66 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycoside h... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9510_chunk_0 | Glycoside hydrolase family 67 | In molecular biology, glycoside hydrolase family 67 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycoside h... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9511_chunk_0 | Glycoside hydrolase family 67 | This classification is available on the CAZy web site, and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes.Glycoside hydrolase family 67 includes alpha-glucuronidases, these are components of an ensemble of enzymes central to the recycling of photosynthetic biomass, remove the alpha-1... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9512_chunk_0 | Glycoside hydrolase family 68 | In molecular biology, glycoside hydrolase family 68 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycoside h... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9513_chunk_0 | Glycoside hydrolase family 7 | In molecular biology, glycoside hydrolase family 7 is a family of glycoside hydrolases EC 3.2.1., which are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycoside hydrolases, based... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9514_chunk_0 | Glycoside hydrolase family 7 | Structurally, cellulases and xylanases frequently consist of a catalytic domain joined to a cellulose-binding domain (CBD) via a linker region that is rich in proline and/or hydroxy-amino acids. In type I exoglucanases, the CBD domain is found at the C-terminal extremity of these enzyme (this short domain forms a hairp... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9515_chunk_0 | Glycoside hydrolase family 70 | In molecular biology, glycoside hydrolase family 70 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycoside h... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9516_chunk_0 | Glycoside hydrolase family 70 | This classification is available on the CAZy web site, and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes.This family includes glucosyltransferases or sucrose 6-glycosyl transferases (GTF-S) (EC 2.4.1.5CAZY GH_70) which catalyse the transfer of D-glucopyramnosyl units from sucrose on... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9517_chunk_0 | Glycoside hydrolase family 71 | In molecular biology, glycoside hydrolase family 71 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycoside h... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9518_chunk_0 | Glycoside hydrolase family 72 | In molecular biology, glycoside hydrolase family 72 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycoside h... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9519_chunk_0 | Glycoside hydrolase family 72 | This classification is available on the CAZy web site, and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes.This family includes yeast glycolipid proteins anchored to the membrane. It includes Candida albicans pH-regulated protein, which is required for apical growth and plays a role i... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9520_chunk_0 | Glycoside hydrolase family 73 | In molecular biology, glycoside hydrolase family 73 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycoside h... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9521_chunk_0 | Glycoside hydrolase family 75 | In molecular biology, glycoside hydrolase family 75 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycoside h... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9522_chunk_0 | Glycoside hydrolase family 76 | In molecular biology, glycoside hydrolase family 76 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycoside h... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9523_chunk_0 | Glycoside hydrolase family 77 | In molecular biology, glycoside hydrolase family 77 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycoside h... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9524_chunk_0 | Glycoside hydrolase family 78 | In molecular biology, glycoside hydrolase family 78 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycoside h... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9525_chunk_0 | Glycoside hydrolase family 79 | In molecular biology, glycoside hydrolase family 79 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycoside h... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9526_chunk_0 | Glycoside hydrolase family 79 | Heparan sulphate proteoglycans (HSPGs) play a key role in the self- assembly, insolubility and barrier properties of basement membranes and extracellular matrices. Hence, cleavage of heparan sulphate (HS) affects the integrity and functional state of tissues and thereby fundamental normal and pathological phenomena inv... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9527_chunk_0 | Glycoside hydrolase family 79 | The enzyme is synthesized as a latent approximately 65 kDa protein that is processed at the N-terminus into a highly active approximately 50 kDa form. Experimental evidence suggests that heparanase may facilitate both tumour cell invasion and neovascularisation, both critical steps in cancer progression. The enzyme is ... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9528_chunk_0 | Glycoside hydrolase family 8 | In molecular biology, glycoside hydrolase family 8 is a family of glycoside hydrolases EC 3.2.1., which are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycoside hydrolases, based... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9529_chunk_0 | Glycoside hydrolase family 80 | In molecular biology, glycoside hydrolase family 80 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycoside h... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9530_chunk_0 | Glycoside hydrolase family 81 | In molecular biology, glycoside hydrolase family 81 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycoside h... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9531_chunk_0 | Glycoside hydrolase family 85 | In molecular biology, glycoside hydrolase family 85 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycoside h... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9532_chunk_0 | Glycoside hydrolase family 88 | In molecular biology, glycoside hydrolase family 88 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycoside h... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9533_chunk_0 | Glycoside hydrolase family 89 | In molecular biology, glycoside hydrolase family 89 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycoside h... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9534_chunk_0 | Glycoside hydrolase family 89 | The enzyme consist of three structural domains, the N-terminal domain has an alpha-beta fold, the central domain has a TIM barrel fold, and the C-terminal domain has an all alpha helical fold.Alpha-N-acetylglucosaminidase is a lysosomal enzyme required for the stepwise degradation of heparan sulphate. Mutations on the ... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9535_chunk_0 | Glycoside hydrolase family 9 | In molecular biology, glycoside hydrolase family 9 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycoside hy... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9536_chunk_0 | Glycoside hydrolase family 92 | In molecular biology, glycoside hydrolase family 92 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycoside h... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9537_chunk_0 | Glycoside hydrolase family 97 | In molecular biology, glycoside hydrolase family 97 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycoside h... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9538_chunk_0 | Glycoside hydrolase family 97 | This classification is available on the CAZy web site, and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes.Glycoside hydrolase family 97 (GH97) is a bacterial family. The central part of the GH97 family protein sequences represents a typical and complete (beta/alpha)8-barrel or cataly... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9539_chunk_0 | Glycoside hydrolase family 98 | In molecular biology, glycoside hydrolase family 98 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycoside h... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9540_chunk_0 | Group II pyridoxal-dependent decarboxylases | In molecular biology, group II pyridoxal-dependent decarboxylases are family of enzymes including aromatic-L-amino-acid decarboxylase (L-dopa decarboxylase or tryptophan decarboxylase) EC 4.1.1.28, which catalyses the decarboxylation of tryptophan to tryptamine, tyrosine decarboxylase EC 4.1.1.25, which converts tyrosi... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9541_chunk_0 | Group III pyridoxal-dependent decarboxylases | In molecular biology, group III pyridoxal-dependent decarboxylases are a family of bacterial enzymes comprising ornithine decarboxylase EC 4.1.1.17, lysine decarboxylase EC 4.1.1.18 and arginine decarboxylase EC 4.1.1.19.Pyridoxal-5'-phosphate-dependent amino acid decarboxylases can be divided into four groups based on... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9542_chunk_0 | Group IV pyridoxal-dependent decarboxylases | In molecular biology, group IV pyridoxal-dependent decarboxylases are a family of enzymes comprising ornithine decarboxylase EC 4.1.1.17, lysine decarboxylase EC 4.1.1.18, arginine decarboxylase EC 4.1.1.19 and diaminopimelate decarboxylaseEC 4.1.1.20. It is also known as the Orn/Lys/Arg decarboxylase class-II family. ... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9543_chunk_0 | Heat Shock Factor | In molecular biology, heat shock factors (HSF), are the transcription factors that regulate the expression of the heat shock proteins. A typical example is the heat shock factor of Drosophila melanogaster. | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9544_chunk_0 | Holdase | In molecular biology, holdases are a particular kind of molecular chaperones that assist the non-covalent folding of proteins in an ATP-independent manner. Examples of holdases are DnaJ and Hsp33. Holdases bind to protein folding intermediates to prevent their aggregation but without directly refolding them. They stand... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9545_chunk_0 | Housekeeping genes | In molecular biology, housekeeping genes are typically constitutive genes that are required for the maintenance of basic cellular function, and are expressed in all cells of an organism under normal and patho-physiological conditions. Although some housekeeping genes are expressed at relatively constant rates in most n... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9546_chunk_0 | Housekeeping genes | The key criterion for the use of a housekeeping gene in this manner is that the chosen housekeeping gene is uniformly expressed with low variance under both control and experimental conditions. Validation of housekeeping genes should be performed before their use in gene expression experiments such as RT-PCR. Recently ... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9547_chunk_0 | Nucleic acid hybridisation | In molecular biology, hybridization (or hybridisation) is a phenomenon in which single-stranded deoxyribonucleic acid (DNA) or ribonucleic acid (RNA) molecules anneal to complementary DNA or RNA. Though a double-stranded DNA sequence is generally stable under physiological conditions, changing these conditions in the l... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9548_chunk_0 | Hydroxymethylglutaryl-CoA synthase | In molecular biology, hydroxymethylglutaryl-CoA synthase or HMG-CoA synthase EC 2.3.3.10 is an enzyme which catalyzes the reaction in which acetyl-CoA condenses with acetoacetyl-CoA to form 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA). This reaction comprises the second step in the mevalonate-dependent isoprenoid biosynthe... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9549_chunk_0 | Hydroxymethylglutaryl-CoA synthase | This results in shunting of excess acetyl-CoA into the ketone synthesis pathway via HMG-CoA, leading to the development of diabetic ketoacidosis. The 3 substrates of this enzyme are acetyl-CoA, H2O, and acetoacetyl-CoA, whereas its two products are (S)-3-hydroxy-3-methylglutaryl-CoA and CoA. In humans, the protein is e... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9550_chunk_0 | Insertional mutagenesis | In molecular biology, insertional mutagenesis is the creation of mutations in DNA by the addition of one or more base pairs. Such insertional mutations can occur naturally, mediated by viruses or transposons, or can be artificially created for research purposes in the lab. | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9551_chunk_0 | Intercellular adhesion molecule | In molecular biology, intercellular adhesion molecules (ICAMs) and vascular cell adhesion molecule-1 (VCAM-1) are part of the immunoglobulin superfamily. They are important in inflammation, immune responses and in intracellular signalling events. The ICAM family consists of five members, designated ICAM-1 to ICAM-5. | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9552_chunk_0 | Intercellular adhesion molecule | They are known to bind to leucocyte integrins CD11/CD18 such as LFA-1 and Macrophage-1 antigen, during inflammation and in immune responses. In addition, ICAMs may exist in soluble forms in human plasma, due to activation and proteolysis mechanisms at cell surfaces. Mammalian intercellular adhesion molecules include: I... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9553_chunk_0 | Kanamycin nucleotidyltransferase | In molecular biology, kanamycin nucleotidyltransferase EC 2.7.7.- (KNTase) is an enzyme which is involved in conferring resistance to aminoglycoside antibiotics. It catalyses the transfer of a nucleoside monophosphate group from a nucleotide to kanamycin. This enzyme is dimeric with each subunit being composed of two d... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9554_chunk_0 | Kanamycin nucleotidyltransferase | The C-terminal domain contains five alpha helices, four of which are organised into an up-and-down alpha helical bundle. Residues found in this domain may contribute to this enzyme's active site. == References == | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9555_chunk_0 | Linker DNA | In molecular biology, linker DNA is double-stranded DNA (38-53 base pairs long) in between two nucleosome cores that, in association with histone H1, holds the cores together. Linker DNA is seen as the string in the "beads and string model", which is made by using an ionic solution on the chromatin. Linker DNA connects... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9556_chunk_0 | Linker DNA | Linker DNA may be degraded by endonucleases.The linkers are short double stranded DNA segments which are formed of oligonucleotides. These contain target sites for the action of one or more restriction enzymes. The linkers can be synthesized chemically and can be ligated to the blunt end of foreign DNA or vector DNA. T... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9557_chunk_0 | ArgJ protein family | In molecular biology, members of the ArgJ protein family are bifunctional protein that catalyses the first (EC 2.3.1.35) and fifth steps (EC 2.3.1.1) in arginine biosynthesis. The structure has been determined for glutamate N-acetyltransferase 2 (ornithine acetyltransferase), an ArgJ-like protein from Streptomyces clav... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9558_chunk_0 | KIN2/PAR-1/MARK kinase family | In molecular biology, members of the KIN2/PAR-1/MARK kinase family of proteins are kinases that are conserved from yeast to human and share the same domain organisation: an N-terminal kinase domain and a C-terminal kinase associated domain 1 (KA1). Some members of this family also contain an UBA domain (ubiquitin-assoc... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9559_chunk_0 | KIN2/PAR-1/MARK kinase family | Some proteins known to contain a KA1 domain are listed below: Mammalian MAP/microtubule affinity-regulating kinases (MARK 1, 2, 3). They regulate polarity in neuronal cell models and appear to function redundantly in phosphorylating microtubule-associated proteins and in regulating microtubule stability. Mammalian mate... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9560_chunk_0 | KIN2/PAR-1/MARK kinase family | It phosphorylates ZNF622 and may contribute to its redirection to the nucleus. It may be involved in the inhibition of spliceosome assembly during mitosis. Caenorhabditis elegans and Drosophila PAR-1 protein, required for establishing polarity in embryos where it is asymmetrically distributed. | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9561_chunk_0 | Monocistronic mRNA | In molecular biology, messenger ribonucleic acid (mRNA) is a single-stranded molecule of RNA that corresponds to the genetic sequence of a gene, and is read by a ribosome in the process of synthesizing a protein. mRNA is created during the process of transcription, where an enzyme (RNA polymerase) converts the gene int... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9562_chunk_0 | Monocistronic mRNA | This exon sequence constitutes mature mRNA. Mature mRNA is then read by the ribosome, and, utilising amino acids carried by transfer RNA (tRNA), the ribosome creates the protein. This process is known as translation. | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9563_chunk_0 | Monocistronic mRNA | All of these processes form part of the central dogma of molecular biology, which describes the flow of genetic information in a biological system. As in DNA, genetic information in mRNA is contained in the sequence of nucleotides, which are arranged into codons consisting of three ribonucleotides each. Each codon code... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9564_chunk_0 | Monocistronic mRNA | The translation of codons into amino acids requires two other types of RNA: transfer RNA, which recognizes the codon and provides the corresponding amino acid, and ribosomal RNA (rRNA), the central component of the ribosome's protein-manufacturing machinery. The concept of mRNA was developed by Sydney Brenner and Franc... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9565_chunk_0 | Methylation induced premeiotically | In molecular biology, methylation induced premeiotically (MIP) is a process by which cytosines within repeated DNA sequences are de novo methylated prior to the sexual cycle. This process was first described in the ascomycete Ascobolus immersens. MIP is dependent upon the gene masc1 which encodes a cytosine methyltrans... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9566_chunk_0 | Methylation induced premeiotically | At least one major function of the process appears to be genome defense. Related functions have been found in other fungi, including Neurospora and Aspergillus species. == References == | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9567_chunk_0 | Mir-130 microRNA precursor family | In molecular biology, miR-130 microRNA precursor is a small non-coding RNA that regulates gene expression. This microRNA has been identified in mouse (MI0000156, MI0000408), and in human (MI0000448, MI0000748). miR-130 appears to be vertebrate-specific miRNA and has now been predicted or experimentally confirmed in a r... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9568_chunk_0 | Mir-130 microRNA precursor family | In this case, the mature sequence is excised from the 3' arm of the hairpin. It has been found that miR-130 is upregulated in a type of cancer called hepatocellular carcinoma. It has been shown that miR-130a is expressed in the hematopoietic stem/progenitor cell compartment but not in mature blood cells. | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9569_chunk_0 | Mir-148/mir-152 microRNA precursor family | In molecular biology, miR-148 is a microRNA whose expression has been demonstrated in human (MI0000253), mouse (MI0000550), rat (MI0000616) and zebrafish (MI0002015). miR-148 has also been predicted in chicken (MI0001189). These predicted hairpin precursor sequence are related to those of miR-152, which has been expres... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9570_chunk_0 | Mir-194 microRNA precursor family | In molecular biology, miR-194 microRNA precursor is a small non-coding RNA gene that regulated gene expression. Its expression has been verified in mouse (MI0000236, MI0000733) and in human (MI0000488, MI0000732). mir-194 appears to be a vertebrate-specific miRNA and has now been predicted or experimentally confirmed i... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9571_chunk_0 | Mir-160 microRNA precursor family | In molecular biology, mir-160 is a microRNA that has been predicted or experimentally confirmed in a range of plant species including Arabidopsis thaliana (mouse-ear cress) and Oryza sativa (rice). miR-160 is predicted to bind complementary sites in the untranslated regions of auxin response factor genes to regulate th... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9572_chunk_0 | Mir-221 microRNA | In molecular biology, mir-221 microRNA (and its paralogue, mir-222) is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. mir-221 is an oncogenic microRNA. | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9573_chunk_0 | Mir-221 microRNA | It targets CD117, which then prevents cell migration and proliferation in endothelial cells. miR-221 is known as an anti angiogenic miRNA. Recent important studies have reported that miR-221 is also involved in induction of angiogenesis. | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9574_chunk_0 | Mir-221 microRNA | RNA induced Silencing Complex (RISC) proteins SND1 and AEG-1 induces miR-221 expression in Liver cancer. In liver cancer miR-221 induces the tumor angiogenesis. miR-221 detection in human faeces can be a non-invasive screening marker for colorectal cancer. | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9575_chunk_0 | Mir-337 microRNA precursor family | In molecular biology, mir-337 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9576_chunk_0 | Mir-46/mir-47/mir-281 microRNA precursor family | In molecular biology, mir-46 (MI0000017) and mir-47 (MI0000018) are microRNA expressed in C. elegans from related hairpin precursor sequences. The predicted hairpin precursor sequences for Drosophila mir-281 (MI0000366, MI0000370) are also related and, hence, belong to this family. The hairpin precursors (represented h... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9577_chunk_0 | Mir-720 microRNA precursor family | In molecular biology, mir-720 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9578_chunk_0 | Biostasis | In molecular biology, molecular chaperones are proteins that assist in the folding, unfolding, assembly, or disassembly of other macromolecular structures. Under typical conditions, molecular chaperones facilitate changes in shape (conformational change) of macromolecules in response to changes in environmental factors... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9579_chunk_0 | Chaperone proteins | In molecular biology, molecular chaperones are proteins that assist the conformational folding or unfolding of large proteins or macromolecular protein complexes. There are a number of classes of molecular chaperones, all of which function to assist large proteins in proper protein folding during or after synthesis, an... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9580_chunk_0 | Chaperone proteins | One major function of molecular chaperones is to prevent the aggregation of misfolded proteins, thus many chaperone proteins are classified as heat shock proteins, as the tendency for protein aggregation is increased by heat stress. The majority of molecular chaperones do not convey any steric information for protein f... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9581_chunk_0 | Multicopper oxidase | In molecular biology, multicopper oxidases are enzymes which oxidise their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre; dioxygen binds to the trinuclear centre and, following the transfer of four electrons, is reduced to two molecules of water. The... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9582_chunk_0 | Multicopper oxidase | Multicopper oxidases include: Ceruloplasmin EC 1.16.3.1 (ferroxidase), a 6-domain enzyme found in the serum of mammals and birds that oxidizes different inorganic and organic substances; exhibits internal sequence homology that appears to have evolved from the triplication of a Cu-binding domain similar to that of lacc... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9583_chunk_0 | Multicopper oxidase | Ascorbate oxidase EC 1.10.3.3, a 3-domain enzyme found in higher plants. Nitrite reductase EC 1.7.2.1, a 2-domain enzyme containing type-1 and type-2 copper centres.In addition to the above enzymes there are a number of other proteins that are similar to the multi-copper oxidases in terms of structure and sequence, som... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9584_chunk_0 | Mutagenesis (molecular biology technique) | In molecular biology, mutagenesis is an important laboratory technique whereby DNA mutations are deliberately engineered to produce libraries of mutant genes, proteins, strains of bacteria, or other genetically modified organisms. The various constituents of a gene, as well as its regulatory elements and its gene produ... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9585_chunk_0 | Mutagenesis (molecular biology technique) | Many methods of mutagenesis exist today. Initially, the kind of mutations artificially induced in the laboratory were entirely random using mechanisms such as UV irradiation. Random mutagenesis cannot target specific regions or sequences of the genome; however, with the development of site-directed mutagenesis, more sp... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9586_chunk_0 | Mutagenesis (molecular biology technique) | Since 2013, development of the CRISPR/Cas9 technology, based on a prokaryotic viral defense system, has allowed for the editing or mutagenesis of a genome in vivo. Site-directed mutagenesis has proved useful in situations that random mutagenesis is not. Other techniques of mutagenesis include combinatorial and insertio... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9587_chunk_0 | Nuclear RNase P | In molecular biology, nuclear ribonuclease P (RNase P) is a ubiquitous endoribonuclease, found in archaea, bacteria and eukarya as well as chloroplasts and mitochondria. Its best characterised enzyme activity is the generation of mature 5′-ends of tRNAs by cleaving the 5′-leader elements of precursor-tRNAs. Cellular RN... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9588_chunk_0 | Nuclear RNase P | Similarly, archaeal RNase P RNA has been shown to be weakly catalytically active in the absence of its respective protein cofactors. Isolated eukaryotic RNase P RNA has not been shown to retain its catalytic function, but is still essential for the catalytic activity of the holoenzyme. Although the archaeal and eukaryo... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9589_chunk_0 | Olfactory marker protein | In molecular biology, olfactory marker protein is a protein involved in signal transduction. It is a highly expressed, cytoplasmic protein found in mature olfactory sensory receptor neurons of all vertebrates. OMP is a modulator of the olfactory signal transduction cascade. The crystal structure of OMP reveals a beta s... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9590_chunk_0 | Open reading frame | In molecular biology, open reading frames (ORFs) are defined as spans of DNA sequence between the start and stop codons. Usually, this is considered within a studied region of a prokaryotic DNA sequence, where only one of the six possible reading frames will be "open" (the "reading", however, refers to the RNA produced... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9591_chunk_0 | Open reading frame | The transcription termination site is located after the ORF, beyond the translation stop codon. If transcription were to cease before the stop codon, an incomplete protein would be made during translation.In eukaryotic genes with multiple exons, introns are removed and exons are then joined together after transcription... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9592_chunk_0 | Origin Recognition Complex | In molecular biology, origin recognition complex (ORC) is a multi-subunit DNA binding complex (6 subunits) that binds in all eukaryotes and archaea in an ATP-dependent manner to origins of replication. The subunits of this complex are encoded by the ORC1, ORC2, ORC3, ORC4, ORC5 and ORC6 genes. ORC is a central componen... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9593_chunk_0 | Origin Recognition Complex | Cdt1), and the Mcm2-Mcm7 complex. Pre-RC assembly during G1 is required for replication licensing of chromosomes prior to DNA synthesis during S phase. Cell cycle-regulated phosphorylation of Orc2, Orc6, Cdc6, and MCM by the cyclin-dependent protein kinase Cdc28 regulates initiation of DNA replication, including blocki... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9594_chunk_0 | Origin Recognition Complex | In yeast, ORC also plays a role in the establishment of silencing at the mating-type loci Hidden MAT Left (HML) and Hidden MAT Right (HMR). ORC participates in the assembly of transcriptionally silent chromatin at HML and HMR by recruiting the Sir1 silencing protein to the HML and HMR silencers.Both Orc1 and Orc5 bind ... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9595_chunk_0 | Origin Recognition Complex | Only the Orc1-5 subunits are required for origin binding; Orc6 is essential for maintenance of pre-RCs once formed. Interactions within ORC suggest that Orc2-3-6 may form a core complex. A 2020 report suggests that budding yeast ORC dimerizes in a cell cycle dependent manner to control licensing. | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9596_chunk_0 | Ornatin | In molecular biology, ornatin is a potent glycoprotein IIb-IIIa (GP IIb-IIIa) antagonist and platelet aggregation inhibitor isolated from Placobdella ornata (Turtle leech). The protein is 41-52 amino acids in length and contains the RGD recognition motif common in adhesion proteins, and 6 conserved cysteine residues. T... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9597_chunk_0 | Pertactin | In molecular biology, pertactin (PRN) is a highly immunogenic virulence factor of Bordetella pertussis, the bacterium that causes pertussis. Specifically, it is an outer membrane protein that promotes adhesion to tracheal epithelial cells. PRN is purified from Bordetella pertussis and is used for the vaccine production... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9598_chunk_0 | Pertactin | The N-terminal signal sequences promotes the secretion of PRN into the periplasm through the bacterial secretion system (Sec) and consequently, the translocation into the outer membrane where it is proteolytically cleaved. The loops in the right handed β-helix of the N-terminus that protrudes out of cell surface (regio... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
wiki_9599_chunk_0 | Protein aggregates | In molecular biology, protein aggregation is a phenomenon in which intrinsically-disordered or mis-folded proteins aggregate (i.e., accumulate and clump together) either intra- or extracellularly. Protein aggregates have been implicated in a wide variety of diseases known as amyloidoses, including ALS, Alzheimer's, Par... | https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus |
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