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c_kwpmg25at5by | 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... | Mir-194 microRNA precursor family |
c_1203k84gdgen | 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... | Mir-160 microRNA precursor family |
c_iapeyftka0ns | Specifically, 3 of A. thaliana's 23 auxin-response factor genes are thought to be post-transcriptionally regulated by mir-160. When one of these targets (ARF17) is manipulated to become miRNA-resistant, several developmental defects can be observed in the host plant. This experiment has been repeated with another mir-1... | Mir-160 microRNA precursor family |
c_363jmmg37xd7 | 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. | Mir-221 microRNA |
c_3uskrbv7c22a | 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. | Mir-221 microRNA |
c_j0s121wvswk1 | 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. | Mir-221 microRNA |
c_iwuptk2hpude | In molecular biology, mir-337 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | Mir-337 microRNA precursor family |
c_6du3okbxyn60 | 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... | Mir-46/mir-47/mir-281 microRNA precursor family |
c_jw8ppn727eqd | In molecular biology, mir-720 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | Mir-720 microRNA precursor family |
c_d5kidzupete0 | 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... | Biostasis |
c_xoaj22zf1n7z | 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... | Chaperone proteins |
c_j750z22iieo0 | 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... | Chaperone proteins |
c_sary7us8vlwn | Various approaches have been applied to study the structure, dynamics and functioning of chaperones. Bulk biochemical measurements have informed us on the protein folding efficiency, and prevention of aggregation when chaperones are present during protein folding. Recent advances in single-molecule analysis have brough... | Chaperone proteins |
c_ajb6hdxgo9ed | 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... | Multicopper oxidase |
c_yxp8htnkd105 | 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... | Multicopper oxidase |
c_l8rb7lz711m3 | 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... | Multicopper oxidase |
c_nsx9pv90jth1 | 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... | Mutagenesis (molecular biology technique) |
c_83absfy5qw14 | 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... | Mutagenesis (molecular biology technique) |
c_co7acf3rtp3i | 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... | Mutagenesis (molecular biology technique) |
c_2nghm6y7nyg6 | 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... | Nuclear RNase P |
c_pwrqbcmg7sp8 | 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... | Nuclear RNase P |
c_vd9vuvcabrne | 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... | Olfactory marker protein |
c_s70hrp5l178x | 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... | Open reading frame |
c_058w37nko0m2 | 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... | Open reading frame |
c_t2mm9br2dyq5 | An alternative definition says that an ORF is a sequence that has a length divisible by three and is bounded by stop codons. This more general definition can be useful in the context of transcriptomics and metagenomics, where a start or stop codon may not be present in the obtained sequences. Such an ORF corresponds to... | Open reading frame |
c_4ci55bkqwsvp | 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... | Origin Recognition Complex |
c_tsc41x3c1lrz | 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... | Origin Recognition Complex |
c_th3uk9e635o5 | 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 ... | Origin Recognition Complex |
c_b3d0r389a2rt | The ATPase activity of Orc1 is involved in formation of the pre-RC. ATP binding by Orc5 is crucial for the stability of ORC as a whole. | Origin Recognition Complex |
c_mo11dlkfhyd3 | 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. | Origin Recognition Complex |
c_wrgacl3atlba | 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... | Ornatin |
c_bh6vhfl97bfz | The sequences of ornatin B, C, D and E are highly similar, while A2 and A3 are less similar, lacking the N-terminal 9 residues. Ornatins share ~40% identity with decorsin, a GP IIb-IIIa antagonist isolated from the leech (Macrobdella decora). == References == | Ornatin |
c_nazujruk4w12 | 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... | Pertactin |
c_2cbi1j4od2od | 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... | Pertactin |
c_wi4nuznxidpq | Another loop of the extending β-helix is region 2 (R2) which contains Pro-Gln-Pro (PQP) repeats towards the C-terminus. This protein’s contribution to immunity is still premature. Reports suggest that R1 and R2 are immunogenic regions, however, recent studies regarding genetic variation of those regions prove otherwise... | Pertactin |
c_wb4wszhjs6hh | 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... | Protein aggregates |
c_6lkungtlqp2o | Protein structures are stabilized by non-covalent interactions and disulfide bonds between two cysteine residues. The non-covalent interactions include ionic interactions and weak van der Waals interactions. Ionic interactions form between an anion and a cation and form salt bridges that help stabilize the protein. | Protein aggregates |
c_us1mziavu72a | Van der Waals interactions include nonpolar interactions (i.e. London dispersion force) and polar interactions (i.e. hydrogen bonds, dipole-dipole bond). These play an important role in a protein's secondary structure, such as forming an alpha helix or a beta sheet, and tertiary structure. Interactions between amino ac... | Protein aggregates |
c_hbfqgksaabg4 | When there are changes in the non-covalent interactions, as may happen with a change in the amino acid sequence, the protein is susceptible to misfolding or unfolding. In these cases, if the cell does not assist the protein in re-folding, or degrade the unfolded protein, the unfolded/misfolded protein may aggregate, in... | Protein aggregates |
c_28mxxf18ifov | In molecular biology, protein catabolism is the breakdown of proteins into smaller peptides and ultimately into amino acids. Protein catabolism is a key function of digestion process. Protein catabolism often begins with pepsin, which converts proteins into polypeptides. | Protein breakdown |
c_8z12f0tv7zol | These polypeptides are then further degraded. In humans, the pancreatic proteases include trypsin, chymotrypsin, and other enzymes. In the intestine, the small peptides are broken down into amino acids that can be absorbed into the bloodstream. These absorbed amino acids can then undergo amino acid catabolism, where th... | Protein breakdown |
c_tqerct17erlf | In molecular biology, protein fold classes are broad categories of protein tertiary structure topology. They describe groups of proteins that share similar amino acid and secondary structure proportions. Each class contains multiple, independent protein superfamilies (i.e. are not necessarily evolutionarily related to ... | Protein fold class |
c_o18r8f7zoiww | In molecular biology, protein threading, also known as fold recognition, is a method of protein modeling which is used to model those proteins which have the same fold as proteins of known structures, but do not have homologous proteins with known structure. It differs from the homology modeling method of structure pre... | Fold recognition |
c_szu1u9o7yyai | In molecular biology, proteins containing the carboxyl transferase domain include biotin-dependent carboxylases. This domain carries out the following reaction: transcarboxylation from biotin to an acceptor molecule. There are two recognised types of carboxyl transferase. | Carboxyl transferase domain |
c_qg6p0gd4nv34 | One of them uses acyl-CoA and the other uses 2-oxo acid as the acceptor molecule of carbon dioxide. All of the members in this family use acyl-CoA as the acceptor molecule. == References == | Carboxyl transferase domain |
c_3vjdviflzkri | In molecular biology, quantitation of nucleic acids is commonly performed to determine the average concentrations of DNA or RNA present in a mixture, as well as their purity. Reactions that use nucleic acids often require particular amounts and purity for optimum performance. To date, there are two main approaches used... | Quantification of nucleic acids |
c_9ttxb9uvy4ss | In molecular biology, repeat-induced point mutation or RIP is a process by which DNA accumulates G:C to A:T transition mutations. Genomic evidence indicates that RIP occurs or has occurred in a variety of fungi while experimental evidence indicates that RIP is active in Neurospora crassa, Podospora anserina, Magnaporth... | Point mutation |
c_teo5ipyil0rn | Repeats with as low as 80% nucleotide identity may also be subject to RIP. Though the exact mechanism of repeat recognition and mutagenesis are poorly understood, RIP results in repeated sequences undergoing multiple transition mutations. | Point mutation |
c_5zytzhxcood0 | The RIP mutations do not seem to be limited to repeated sequences. Indeed, for example, in the phytopathogenic fungus L. maculans, RIP mutations are found in single copy regions, adjacent to the repeated elements. These regions are either non-coding regions or genes encoding small secreted proteins including avirulence... | Point mutation |
c_plfrdyezax3r | The degree of RIP within these single copy regions was proportional to their proximity to repetitive elements.Rep and Kistler have speculated that the presence of highly repetitive regions containing transposons, may promote mutation of resident effector genes. So the presence of effector genes within such regions is s... | Point mutation |
c_tvos35nwhexb | In molecular biology, restriction fragment length polymorphism (RFLP) is a technique that exploits variations in homologous DNA sequences, known as polymorphisms, populations, or species or to pinpoint the locations of genes within a sequence. The term may refer to a polymorphism itself, as detected through the differi... | Restriction Fragment Length Polymorphism |
c_xvleimz1q2el | In molecular biology, ribosomal s6 kinase (rsk) is a family of protein kinases involved in signal transduction. There are two subfamilies of rsk, p90rsk, also known as MAPK-activated protein kinase-1 (MAPKAP-K1), and p70rsk, also known as S6-H1 Kinase or simply S6 Kinase. There are three variants of p90rsk in humans, r... | Ribosomal s6 kinase |
c_xgk060cz4uo3 | In molecular biology, sirohaem synthase (or siroheme synthase) (CysG) is a multi-functional enzyme with S-adenosyl-L-methionine (SAM)-dependent bismethyltransferase, dehydrogenase and ferrochelatase activities. Bacterial sulphur metabolism depends on the iron-containing porphinoid sirohaem. CysG synthesizes sirohaem fr... | Sirohaem synthase |
c_wxndprre5ufw | In molecular biology, small Cajal body specific RNA 4 (also known as ACA26) is believed to be a guide RNA of the H/ACA box class, since it has the predicted hairpin-hinge-hairpin-tail structure, conserved H/ACA-box motifs, and is found associated with GAR1. In particular, ACA26 is predicted to guide the pseudouridylati... | Small Cajal body specific RNA 4 |
c_04ghwh688cbx | In molecular biology, small nucleolar RNA R71 (also known as snoRNA R71) is a non-coding RNA (ncRNA) molecule which functions in the modification of other small nuclear RNAs (snRNAs). This type of modifying RNA is usually located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is k... | Plant small nucleolar RNA R71 |
c_ea2sby0jcc95 | In molecular biology, small nucleolar RNA SNORA10 and small nuclear RNA SNORA64 are homologous members of the H/ACA class of small nucleolar RNA (snoRNA). This family of ncRNAs involved in the maturation of ribosomal RNA. snoRNA in this family act as guides in the modification of uridines to pseudouridines. This family... | Small nucleolar RNA SNORA64/SNORA10 family |
c_d5q7utdn7mo7 | In molecular biology, small nucleolar RNA SNORA11 (also known as U107) is a non-coding RNA (ncRNA) molecule which functions in the biogenesis (modification) of other small nuclear RNAs (snRNAs). This type of modifying RNA is located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It i... | Small nucleolar RNA SNORA11 |
c_a6dqhv9gfkjs | U107 has a predicted hairpin-hinge-hairpin-tail structure and is predicted to be a member of the H/ACA box class of snoRNAs that guide the sites of modification of uridines to pseudouridines. This snoRNA was identified by RT-PCR from blood cells and its expression confirmed by Northern blot analysis. There is no predic... | Small nucleolar RNA SNORA11 |
c_fcn9y5rdq8s5 | In molecular biology, small nucleolar RNA SNORA72 (also known as U72) is a non-coding RNA (ncRNA) molecule which functions in the biogenesis (modification) of other small nuclear RNAs (snRNAs). This type of modifying RNA is located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is... | Small nucleolar RNA SNORA72 |
c_eijolvd6sq18 | ACA30 was originally cloned from HeLa cells and belongs to the H/ACA box class of snoRNAs as it has the predicted hairpin-hinge-hairpin-tail structure, has the conserved H/ACA-box motifs and is found associated with GAR1 protein. snoRNA ACA72 is predicted to guide the pseudouridylation of U55 of 5.8S ribosomal RNA (rRN... | Small nucleolar RNA SNORA72 |
c_e9e7bnntg3lo | In molecular biology, small nucleolar RNA derived microRNAs are microRNAs (miRNA) derived from small nucleolar RNA (snoRNA). MicroRNAs are usually derived from precursors known as pre-miRNAs, these pre-miRNAs are recognised and cleaved from a pri-miRNA precursor by the Pasha and Drosha proteins. However some microRNAs,... | Small nucleolar RNA-derived microRNA |
c_dek6lp5qfygn | In molecular biology, small nucleolar RNAs (snoRNAs) are a class of small RNA molecules that primarily guide chemical modifications of other RNAs, mainly ribosomal RNAs, transfer RNAs and small nuclear RNAs. There are two main classes of snoRNA, the C/D box snoRNAs, which are associated with methylation, and the H/ACA ... | Small nucleolar RNA |
c_bdzixo998thb | In molecular biology, snR54 is a non-coding RNA that is a member of the C/D class of snoRNA which contain the C box motif (UGAUGA) and D box motif (CUGA). Most of the members of the box C/D family function in directing site-specific 2'-O-methylation of substrate RNAs. This snoRNA was first identified by a computational... | Small nucleolar RNA snR54 |
c_1swhuo7e4sep | In molecular biology, snR64 is an RNA molecule belonging to the C/D class of small nucleolar RNA (snoRNA), which contain the C (UGAUGA) and D (CUGA) box motifs. Similar to most members of the box C/D family, snR64 is conjectured to help direct site-specific 2'-O-methylation of substrate RNAs. | Small nucleolar RNA snR64 |
c_7vqnmnvi06e2 | In molecular biology, snoR9 is a non-coding RNA (ncRNA) which functions in the biogenesis (modification) of other small nuclear RNAs (snRNAs). It is known as a small nucleolar RNA (snoRNA) and also often referred to as a 'guide RNA'. R9 is a member of the C/D box class of snoRNAs which contain the conserved sequence mo... | Small nucleolar RNA snoR9 plant |
c_a1594uz0bior | In molecular biology, snoRNA HBII-210 belongs to the C/D family of snoRNAs. It is the human orthologue of the mouse MBII-210 and is predicted to guide the 2'O-ribose methylation of large 28S rRNA on residue G4464. | Small nucleolar RNA SNORD69 |
c_84e9djyehxd8 | In molecular biology, snoRNA HBII-239 belongs to the family of C/D snoRNAs. It is the human orthologue of the mouse MBII-239 described and is predicted to guide 2'O-ribose methylation of 5.8S rRNA on residue U14. | Small nucleolar RNA SNORD71 |
c_nhzhdf731ucu | In molecular biology, snoRNA HBII-289 belongs to the family of C/D snoRNAs. It is the human orthologue of the mouse MBII-289 and has no identified RNA target. | Small nucleolar RNA SNORD89 |
c_hesfpel6hg46 | In molecular biology, snoRNA SNORD70 (HBII-234) is a non-coding RNA that belongs to the C/D family of snoRNAs. It is the human orthologue of the mouse MBII-234 and is predicted to guide 2'O-ribose methylation of the small 18S rRNA on position A512. It is hosted, together with HBII-95, by the core C/D box snoRNA protein... | Small nucleolar RNA SNORD70 |
c_8wrz79a4w3y2 | In molecular biology, snoRNA SNORD90 (HBII-295) is a non-coding RNA that belongs to the family of C/D snoRNAs. Initially described as HBII-295 this RNA has now been called SNORD70 by the HUGO Gene Nomenclature Committee. It is the human orthologue of the mouse MBII-295 and has no identified RNA target. | Small nucleolar RNA SNORD90 |
c_rh5glylqoodv | This RNA is expressed from an intron of the MNAB/OR1K1 gene. There is evidence that SNORD90 is involved in guiding N6-methyladenosine (m6A) modifications onto target RNA transcripts. Specifically, SNORD90 has been shown to increase m6A levels on neuregulin 3 (NRG3) leading to its down-regulation through recognition by ... | Small nucleolar RNA SNORD90 |
c_5by0255y7gqf | In molecular biology, snoRNA U101 (also known as SNORD101) is a non-coding RNA (ncRNA) molecule which functions in the modification of other small nuclear RNAs (snRNAs). This type of modifying RNA is usually located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a smal... | Small nucleolar RNA SNORD101 |
c_dgvziog49jxk | snoRNA U101 belongs to the C/D box class of snoRNAs which contain the conserved sequence motifs known as the C box (UGAUGA) and the D box (CUGA). Most of the members of the box C/D family function in directing site-specific 2'-O-methylation of substrate RNAs.U101 was identified by computational screening of the introns... | Small nucleolar RNA SNORD101 |
c_7ewxvafgi9so | In molecular biology, snoRNA U102 (also known as SNORD102) is a non-coding RNA (ncRNA) molecule which functions in the modification of other small nuclear RNAs (snRNAs). This type of modifying RNA is usually located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a smal... | Small nucleolar RNA SNORD102 |
c_7hssr6nwi6xz | snoRNA U102 belongs to the C/D box class of snoRNAs which contain the conserved sequence motifs known as the C box (UGAUGA) and the D box (CUGA). Most of the members of the box C/D family function in directing site-specific 2'-O-methylation of substrate RNAs.U102 was identified by computational screening of the introns... | Small nucleolar RNA SNORD102 |
c_cufkjvy2ma61 | In molecular biology, snoRNA U103 (also known as SNORD103) is a non-coding RNA (ncRNA) molecule which functions in the modification of other small nuclear RNAs (snRNAs). This type of modifying RNA is usually located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a smal... | Small nucleolar RNA SNORD103 |
c_026qx6c5ubxy | snoRNA U103 belongs to the C/D box class of snoRNAs which contain the conserved sequence motifs known as the C box (UGAUGA) and the D box (CUGA). Most of the members of the box C/D family function in directing site-specific 2'-O-methylation of substrate RNAs.U103 was identified by computational screening of the introns... | Small nucleolar RNA SNORD103 |
c_7okgcwl3ubfi | In molecular biology, snoRNA U16 (also known as SNORD16) is a non-coding RNA (ncRNA) molecule which functions in the modification of other small nuclear RNAs (snRNAs). This type of modifying RNA is usually located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small ... | Small nucleolar RNA SNORD16 |
c_as5rho13t0m1 | snoRNA U16 belongs to the C/D box class of snoRNAs which contain the conserved sequence motifs known as the C box (UGAUGA) and the D box (CUGA). Most of the members of the box C/D family function in directing site-specific 2'-O-methylation of substrate RNAs.U16 is predicted to guide the 2'O-ribose methylation of 18S ri... | Small nucleolar RNA SNORD16 |
c_df92af33abyu | In molecular biology, snoRNA U20 (also known as SNORD20) is a non-coding RNA (ncRNA) molecule which functions in the modification of other small nuclear RNAs (snRNAs). This type of modifying RNA is usually located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small ... | Small nucleolar RNA SNORD20 |
c_1mvbwhljzcbl | snoRNA U20 belongs to the C/D box class of snoRNAs which contain the conserved sequence motifs known as the C box (UGAUGA) and the D box (CUGA). Most of the members of the box C/D family function in directing site-specific 2'-O-methylation of substrate RNAs.U20 is encoded in intron 11 of the nucleolin gene in human, mo... | Small nucleolar RNA SNORD20 |
c_zpmytc6tgf61 | In molecular biology, snoRNA U22 (also known as SNORD22) is a non-coding RNA (ncRNA) molecule which functions in the modification of other small nuclear RNAs (snRNAs). This type of modifying RNA is usually located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small ... | Small nucleolar RNA SNORD22 |
c_gwn1sbssl5ho | U22 belongs to the C/D box class of snoRNAs which contain the conserved sequence motifs known as the C box (UGAUGA) and the D box (CUGA). Most of the members of the box C/D family function in directing site-specific 2'-O-methylation of substrate RNAs.In the human genome snoRNA U22 is encoded along with seven other snoR... | Small nucleolar RNA SNORD22 |
c_t2d9hyljqctu | In molecular biology, snoRNA U25 (also known as SNORD25) is a non-coding RNA (ncRNA) molecule which functions in the biogenesis (modification) of other small nuclear RNAs (snRNAs). This type of modifying RNA is located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a s... | Small nucleolar RNA SNORD25 |
c_bg6f28nyzid2 | Most of the members of the box C/D family function in directing site-specific 2'-O-methylation of substrate RNAs.U25 is found in gene clusters in plants and within the U22 snoRNA host gene (UHG) in mammals. U25 is thought to as a 2'-O-ribose methylation guide for ribosomal RNA. This RNA has also been named snoRNA R73 i... | Small nucleolar RNA SNORD25 |
c_ei3jlndul61n | In molecular biology, snoRNA U32 (also known as SNORD32) is a non-coding RNA (ncRNA) molecule which functions in the modification of other small nuclear RNAs (snRNAs). This type of modifying RNA is usually located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small ... | Small nucleolar RNA SNORD32 |
c_0snbfdz0zi8p | snoRNA U32 belongs to the C/D box class of snoRNAs which contain the conserved sequence motifs known as the C box (UGAUGA) and the D box (CUGA). Most of the members of the box C/D family function in directing site-specific 2'-O-methylation of substrate RNAs.U32 is encoded within intron 2 of the ribosomal protein L13 ge... | Small nucleolar RNA SNORD32 |
c_lvq5fcbtzihe | In molecular biology, snoRNA U34 (also known as SNORD34) is a non-coding RNA (ncRNA) molecule which functions in the modification of other small nuclear RNAs (snRNAs). This type of modifying RNA is usually located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small ... | Small nucleolar RNA SNORD34 |
c_ej9ofyhf3q1j | snoRNA U34 belongs to the C/D box class of snoRNAs which contain the conserved sequence motifs known as the C box (UGAUGA) and the D box (CUGA). Most of the members of the box C/D family function in directing site-specific 2'-O-methylation of substrate RNAs.snoRNA U34 was initially characterised by a computational scre... | Small nucleolar RNA SNORD34 |
c_p15xb1sr31wu | In molecular biology, snoRNA U35 (also known as SNORD35) is a non-coding RNA (ncRNA) molecule which functions in the modification of other small nuclear RNAs (snRNAs). This type of modifying RNA is usually located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small ... | Small nucleolar RNA SNORD35 |
c_wqaqg53z0xxf | snoRNA U35 belongs to the C/D box class of snoRNAs which contain the conserved sequence motifs known as the C box (UGAUGA) and the D box (CUGA). Most of the members of the box C/D family function in directing site-specific 2'-O-methylation of substrate RNAs.U35 is encoded in intron 6 of ribosomal protein L13A and intro... | Small nucleolar RNA SNORD35 |
c_5h75jzrgmqqa | In molecular biology, snoRNA U36 (also known as SNORD36) is a non-coding RNA (ncRNA) molecule which functions in the biogenesis (modification) of other small nuclear RNAs (snRNAs). This type of modifying RNA is located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a s... | Small nucleolar RNA SNORD36 |
c_ovhx0w9ri8p1 | Most of the members of the box C/D family function in directing site-specific 2'-O-methylation of substrate RNAs.U36 is encoded within the intron of ribosomal protein rpL7a, and has two regions of complementarity to 18S and 28S ribosomal RNA. This complementarity suggests that U36 acts as a 2'-O-ribose methylation guid... | Small nucleolar RNA SNORD36 |
c_u53egcupv5gz | In molecular biology, snoRNA U38 (also known as SNORD38) is a non-coding RNA (ncRNA) molecule which functions in the modification of other small nuclear RNAs (snRNAs). This type of modifying RNA is usually located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small ... | Small nucleolar RNA SNORD38 |
c_siif1x3p0qto | Most of the members of the box C/D family function in directing site-specific 2'-O-methylation of substrate RNAs.U38 is located in introns 4 and 5 of ribosomal protein S8 in human and in the homologous genes in mouse and cow. U38 is predicted to guides the methylation of 2'-O-ribose residues in 28S ribosomal RNA (rRNA)... | Small nucleolar RNA SNORD38 |
c_v8zevgeakmh3 | In molecular biology, snoRNA U39 (also known as SNORD39) is a non-coding RNA (ncRNA) molecule which functions in the modification of other small nuclear RNAs (snRNAs). This type of modifying RNA is usually located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small ... | Small nucleolar RNA SNORD39 |
c_ynsu1wjowb0z | In molecular biology, snoRNA U41 (also known as SNORD41) belongs to the C/D box class of snoRNAs. It is predicted to guide 2'O-ribose methylation of the large 28S rRNA on residue U4276. | Small nucleolar RNA SNORD41 |
c_ibzxo3g1qbbl | In molecular biology, snoRNA U42 (also known as SNORD42) is a non-coding RNA (ncRNA) molecule which functions in the modification of other small nuclear RNAs (snRNAs). This type of modifying RNA is usually located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small ... | Small nucleolar RNA SNORD42 |
c_syuix2vp6zhd | Most of the members of the box C/D family function in directing site-specific 2'-O-methylation of substrate RNAs.In the human genome there are two closely related copies of U42 (called U42A and U42B) both located within the introns of the ribosomal protein L23a (RPL23a) gene. Both snoRNAs are predicted to guide the sit... | Small nucleolar RNA SNORD42 |
c_2fmmtc7ghz10 | In molecular biology, snoRNA U43 (also known as SNORD43) is a non-coding RNA (ncRNA) molecule which functions in the modification of other small nuclear RNAs (snRNAs). This type of modifying RNA is usually located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small ... | Small nucleolar RNA SNORD43 |
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