id stringlengths 14 14 | text stringlengths 9 3.55k | source stringlengths 1 250 |
|---|---|---|
c_qttx4a0l9myn | In molecular biology mir-153 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | Mir-153 microRNA precursor family |
c_3t9jdee7sa7q | In molecular biology mir-190 microRNA is a short RNA molecule. MicroRNAs function is to regulate the expression levels of other genes by several mechanisms. | Mir-190 microRNA precursor family |
c_nnhonya7lgyj | In molecular biology mir-198 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | Mir-198 microRNA precursor family |
c_dwnddwolc5jq | In molecular biology mir-202 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. The pre-miR-202 in the mouse genome is located fully within an exon, whereas in human it lies across a splice junction. This implies that human miR-202 is exposed to ... | Mir-202 microRNA precursor family |
c_o06rm2irrv7f | In molecular biology mir-216 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | Mir-216 microRNA precursor family |
c_9evwkn2pjsol | In molecular biology mir-23 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | Mir-23 microRNA precursor family |
c_jlkpjg69f61n | In molecular biology mir-241 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | Mir-241 microRNA precursor family |
c_09ibseqka7oi | In molecular biology mir-275 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | Mir-275 microRNA precursor family |
c_5plwmjic0c8e | In molecular biology mir-277 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | Mir-277 microRNA precursor family |
c_yxo0khzcvi4u | In molecular biology mir-278 microRNA is a short RNA molecule belonging to a class of molecules referred to as microRNAs. These function to regulate the expression levels of other genes by several mechanisms, primarily binding to their target at its 3'UTR. | Mir-278 microRNA precursor family |
c_3qp56a2oyfq5 | In molecular biology mir-299 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | Mir-299 microRNA precursor family |
c_z0hz0bjepf25 | In molecular biology mir-301 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | Mir-301 microRNA precursor family |
c_71qcxhn15chu | In molecular biology mir-305 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | Mir-305 microRNA precursor family |
c_vnt503kx9r2y | In molecular biology mir-322 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | Mir-322 microRNA precursor family |
c_mzro2qj7y9rf | In molecular biology mir-326 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | Mir-326 microRNA precursor family |
c_vty8vti45w60 | In molecular biology mir-330 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | Mir-330 microRNA precursor family |
c_tgdw6al8584l | In molecular biology mir-331 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | Mir-331 microRNA precursor family |
c_315vn1culsqd | In molecular biology mir-345 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | Mir-345 microRNA precursor family |
c_071ggfsvm67r | In molecular biology mir-346 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | Mir-346 microRNA precursor family |
c_hhzwf1g5bp7v | In molecular biology mir-350 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | Mir-350 microRNA precursor family |
c_wssmvl78nfpn | In molecular biology mir-361 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. For example, miR-361-5p might act as a suppressor in triple-negative breast cancer (TNBC) by targeting RQCD1 to inhibit the EGFR/PI3K/Akt signaling pathway. | Mir-361 microRNA precursor family |
c_kmvxlvgaccir | In molecular biology mir-363 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | Mir-363 microRNA precursor family |
c_awid2qjpgj6n | In molecular biology mir-365 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | Mir-365 microRNA precursor family |
c_suklnrhvb33r | In molecular biology mir-370 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. This microRNA, mir-370-3p, has been shown to play a role in heart failure. The upregulation of mir-370-3p in the sinus node leads to downregulation of the pacemaker i... | Mir-370 microRNA precursor family |
c_brepbg5a4oc7 | In molecular biology mir-374 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | Mir-374 microRNA precursor family |
c_bjrmjmolnkw6 | In molecular biology mir-383 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | Mir-383 microRNA precursor family |
c_qvlq9weuuzon | In molecular biology mir-384 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | Mir-384 microRNA precursor family |
c_my3gv6dtuhb8 | In molecular biology mir-390 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | Mir-390 microRNA precursor family |
c_zjrsneq9t8s7 | In molecular biology mir-396 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | Mir-396 microRNA precursor family |
c_jq7qid8p5thk | In molecular biology mir-397 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | Mir-397 microRNA precursor family |
c_16glm15ytfdx | In molecular biology mir-398 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | Mir-398 microRNA precursor family |
c_iqo0ajor2aak | In molecular biology mir-430 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | Mir-430 microRNA precursor family |
c_zdlk8wrthwap | In molecular biology mir-455 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | Mir-455 microRNA precursor family |
c_9i0ezmx8g4f4 | In molecular biology mir-5 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. mir-5 has been implicated in regulation of VEGF in an experiment where a plasmid containing a cluster of mir-5, mir-10 and mir-7 was shown to down-regulate VEGF by 75%.... | Mir-5 microRNA precursor family |
c_if8famlifkby | In molecular biology mir-535 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | Mir-535 microRNA precursor family |
c_n719bs47gvty | In molecular biology mir-542 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | Mir-542 microRNA precursor family |
c_co716kd9ndeu | In molecular biology mir-589 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | Mir-589 microRNA precursor family |
c_epz7dtyln8k1 | In molecular biology mir-598 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | Mir-598 microRNA precursor family |
c_qirgzmfdrvvs | In molecular biology mir-625 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. Many microRNAs play important roles in cancer development and progression. | Mir-625 microRNA precursor family |
c_5be59cwhek53 | In molecular biology mir-632 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | Mir-632 microRNA precursor family |
c_if3xio87g7mu | In molecular biology mir-636 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | Mir-636 microRNA precursor family |
c_lregwtq2znne | In molecular biology mir-661 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | Mir-661 microRNA precursor family |
c_89j3ts062mpx | In molecular biology mir-663 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | Mir-663 microRNA precursor family |
c_29m12qyuesuz | In molecular biology mir-71 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | Mir-71 microRNA precursor family |
c_8bc0mf8iavop | In molecular biology mir-711 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | Mir-711 microRNA precursor family |
c_j67yzdazk80q | In molecular biology mir-84 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | Mir-84 microRNA precursor family |
c_emqjcqlz4bb4 | In molecular biology mir-885 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | Mir-885 microRNA precursor family |
c_sbqjcbkueud0 | In molecular biology short linear motifs (SLiMs), linear motifs or minimotifs are short stretches of protein sequence that mediate protein–protein interaction.The first definition was given by Tim Hunt: "The sequences of many proteins contain short, conserved motifs that are involved in recognition and targeting activi... | Short linear motif |
c_j4toiyg3qe4a | In molecular biology the B-box-type zinc finger domain is a short protein domain of around 40 amino acid residues in length. B-box zinc fingers can be divided into two groups, where types 1 and 2 B-box domains differ in their consensus sequence and in the spacing of the 7-8 zinc-binding residues. Several proteins conta... | B-box zinc finger |
c_xb5ke8nf2o3o | In molecular biology the BED-type zinc finger domain is a protein domain which was named after the Drosophila proteins BEAF and DREF, is found in one or more copies in cellular regulatory factors and transposases from plants, animals and fungi. The BED finger is an about 50 to 60 amino acid residues domain that contain... | BED zinc finger |
c_poxths2gn6mv | In molecular biology the Bacterial Microcompartment (BMC) domain is a protein domain found in a variety of shell proteins, including CsoS1A, CsoS1B and CsoS1C of Thiobacillus neapolitanus (Halothiobacillus neapolitanus) and their orthologs from other bacteria. These shell proteins form the polyhedral structure of the c... | BMC domain |
c_356sp9ei6o44 | The majority of the shell proteins consist of a single BMC domain in each subunit, forming a hexameric structure that assembles to form the flat facets of the polyhedral shell. To date, two shell proteins were found to consist a tandem BMC domains, of which forms a trimeric structure, giving a pseudo-hexameric appearan... | BMC domain |
c_63m8aha55a4y | In molecular biology the DHHC domain is a protein domain that acts as an enzyme, which adds a palmitoyl chemical group to proteins in order to anchor them to cell membranes. The DHHC domain was discovered in 1999 and named after a conserved sequence motif found in its protein sequence. Roth and colleagues showed that t... | DHHC domain |
c_678k4ffwhl38 | In mammals twenty three members of this family have been identified and their substrate specificities investigated. Some members of the family such as ZDHHC3 and ZDHHC7 enhance palmitoylation of proteins such as PSD-95, SNAP-25, GAP43, Gαs. Others such as ZDHHC9 showed specificity only toward the H-Ras protein. However... | DHHC domain |
c_8hkre8gi7yp3 | In molecular biology the DM domain is a protein domain first discovered in the doublesex proteins of Drosophila melanogaster and is also seen in C. elegans and mammalian proteins. In D. melanogaster the doublesex gene controls somatic sexual differentiation by producing alternatively spliced mRNAs encoding related sex-... | DM domain |
c_ekzk1e2p59bj | In molecular biology the FGGY carbohydrate kinase family is a family of evolutionarily related carbohydrate kinase enzymes. These enzymes include L-fuculokinase EC 2.7.1.51 (gene fucK); gluconokinase EC 2.7.1.12 (gene gntK); glycerol kinase EC 2.7.1.30 (gene glpK); xylulokinase EC 2.7.1.17 (gene xylB); D-ribulose kinas... | FGGY carbohydrate kinase family |
c_svv1t7ejc5q5 | These enzymes consist of two domains. The N-terminal and C-terminal domains both adopt a ribonuclease H-like fold and are structurally related to each other. == References == | FGGY carbohydrate kinase family |
c_9gsg5qsr1mh6 | In molecular biology the FYVE zinc finger domain is named after the four cysteine-rich proteins: Fab 1 (yeast orthologue of PIKfyve), YOTB, Vac 1 (vesicle transport protein), and EEA1, in which it has been found. FYVE domains bind phosphatidylinositol 3-phosphate, in a way dependent on its metal ion coordination and ba... | FYVE domain |
c_hzut3jf5fnzh | In molecular biology the L-like lectin domain is a protein domain found in lectins which are similar to the leguminous plant lectins. Lectins are structurally diverse proteins that bind to specific carbohydrates. This family includes the VIP36 and ERGIC-53 lectins. Although proteins containing this domain were original... | L-type lectin domain |
c_94ll0wrsva43 | It was identified as a calcium-dependent, mannose-specific lectin. Its dysfunction has been associated with combined factors V and VIII deficiency, suggesting an important and substrate-specific role for ERGIC-53 in the glycoprotein-secreting pathway.The L-like lectin domain has an overall globular shape composed of a ... | L-type lectin domain |
c_cbjpl75xh2sa | In molecular biology the LysM domain is a protein domain found in a wide variety of extracellular proteins and receptors. The LysM domain is named after the Lysin Motif which was the original name given to the sequence motif identified in bacterial proteins. The region was originally identified as a C-terminal repeat f... | LysM domain |
c_glwqncfq6hhm | LysM domains are also found in plant receptors, including NFP, the receptor for Nod factor which is necessary for the root nodule symbiosis between legumes and symbiotic bacteria. The LysM domain is typically between 44 and 65 amino acid residues in length. The structure of the LysM domain showed that it is composed of... | LysM domain |
c_3nbklg3zdp9b | In molecular biology the MIZ-type zinc finger domain is a zinc finger-containing protein with homology to the yeast protein, Nfi-1. Miz1 is a sequence specific DNA binding protein that can function as a positive-acting transcription factor. Miz1 binds to the homeobox protein Msx2, enhancing the specific DNA-binding abi... | MIZ zinc finger |
c_1skk7z2ppy7h | The name MIZ is derived from Msx-interacting-zinc finger. The crystal structure of S. cerevisiae sumo e3 ligase siz1 containing this domain has been solved. == References == | MIZ zinc finger |
c_b3erj9snqzcf | In molecular biology the MYND-type zinc finger domain is a conserved protein domain. The MYND domain (myeloid, Nervy, and DEAF-1) is present in a large group of proteins that includes RP-8 (PDCD2), Nervy, and predicted proteins from Drosophila, mammals, Caenorhabditis elegans, yeast, and plants. The MYND domain consist... | MYND zinc finger |
c_l609jwu8j4gn | Mutating conserved cysteine residues in the DEAF-1 MYND domain does not abolish DNA binding, which suggests that the MYND domain might be involved in protein-protein interactions. Indeed, the MYND domain of ETO/MTG8 interacts directly with the N-CoR and SMRT co-repressors. Aberrant recruitment of co-repressor complexes... | MYND zinc finger |
c_bxm34wgjpb7e | ETO has been shown to be a co-repressor recruited by the promyelocytic leukemia zinc finger (PLZF) protein. A divergent MYND domain present in the adenovirus E1A binding protein BS69 was also shown to interact with N-CoR and mediate transcriptional repression. The current evidence suggests that the MYND motif in mammal... | MYND zinc finger |
c_649pkaiztnpy | In molecular biology the PIN domain is a protein domain that is about 130 amino acids in length. PIN domains function as nuclease enzymes that cleave single stranded RNA in a sequence- or structure-dependent manner.PIN domains contain four nearly invariant acidic residues. Crystal structures show these residues cluster... | PIN domain |
c_c72t4rjkj2va | The majority of PIN-domain proteins found in prokaryotes are the toxic components of toxin-antitoxin operons. These loci provide a control mechanism that helps free-living prokaryotes cope with nutritional stress. == References == | PIN domain |
c_wbz8rpspi3bh | 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 or LH2 (Lipoxygenase homology) domain. The known structure of pancreatic lipase shows this domain binds to procolipase Pfam... | PLAT domain |
c_y055urh6h6g5 | In molecular biology the SPR domain is a protein domain found in the Sprouty (Spry) and Spred (Sprouty related EVH1 domain) proteins. These have been identified as inhibitors of the Ras/mitogen-activated protein kinase (MAPK) cascade, a pathway crucial for developmental processes initiated by activation of various rece... | SPR domain |
c_1u1yvw1wbs77 | In molecular biology the SeqA protein is found in bacteria and archaea. The function of this protein is highly important in DNA replication. The protein negatively regulates the initiation of DNA replication at the origin of replication, in Escherichia coli, OriC. | SeqA protein |
c_f91mlsjs4n15 | Additionally the protein plays a further role in sequestration. The importance of this protein is vital, without its help in DNA replication, cell division and other crucial processes could not occur. This protein domain is thought to be part of a much larger protein complex which includes other proteins such as SeqB. | SeqA protein |
c_bpmjbtz847l4 | In molecular biology the ZZ-type zinc finger domain is a type of protein domain that was named because of its ability to bind two zinc ions. These domains contain 4-6 Cys residues that participate in zinc binding (plus additional Ser/His residues), including a Cys-X2-Cys motif found in other zinc finger domains. These ... | ZZ zinc finger |
c_jda1kep8f9ke | ZZ-type zinc finger domains are found in: Transcription factors P300 and CBP. Plant proteins involved in light responses, such as Hrb1. E3 ubiquitin ligases MEX and MIB2 (EC). | ZZ zinc finger |
c_2i9l1gyz9aa1 | Dystrophin and its homologuesSingle copies of the ZZ zinc finger occur in the transcriptional adaptor/coactivator proteins P300, in cAMP response element-binding protein (CREB)-binding protein (CBP) and ADA2. CBP provides several binding sites for transcriptional coactivators. The site of interaction with the tumour su... | ZZ zinc finger |
c_0zeyy2h02jzg | The ZZ-type zinc finger of CBP contains two twisted anti-parallel beta-sheets and a short alpha-helix, and binds two zinc ions. One zinc ion is coordinated by four cysteine residues via 2 Cys-X2-Cys motifs, and the third zinc ion via a third Cys-X-Cys motif and a His-X-His motif. The first zinc cluster is strictly cons... | ZZ zinc finger |
c_vz23pjo3q580 | In Arabidopsis thaliana (Mouse-ear cress), the hypersensitive to red and blue 1 (Hrb1) protein, which regulating both red and blue light responses, contains a ZZ-type zinc finger domain.ZZ-type zinc finger domains have also been identified in the testis-specific E3 ubiquitin ligase MEX that promotes death receptor-indu... | ZZ zinc finger |
c_gynv4bei11mm | In addition, the Cys-rich domains of dystrophin, utrophin and an 87kDa post-synaptic protein contain a ZZ-type zinc finger with high sequence identity to P300/CBP ZZ-type zinc fingers. In dystrophin and utrophin, the ZZ-type zinc finger lies between a WW domain (flanked by and EF hand) and the C-terminal coiled-coil do... | ZZ zinc finger |
c_03lryzv1ewnr | Dystrophin and its autosomal homologue utrophin interact with beta-dystroglycan via their C-terminal regions, which are composed of a WW domain, an EF hand domain, and a ZZ-type zinc finger domain. The WW domain is the primary site of interaction between dystrophin or utrophin and dystroglycan, while the EF hand and ZZ... | ZZ zinc finger |
c_t3ze5u3k2ejp | In molecular biology the fructosamine kinase family is a family of enzymes. This family includes eukaryotic fructosamine-3-kinase enzymes which may initiate a process leading to the deglycation of fructoselysine and of glycated proteins and in the phosphorylation of 1-deoxy-1-morpholinofructose, fructoselysine, fructos... | Fructosamine kinase family |
c_skknepd87b3z | Ketosamine-3-kinases (KT3K) catalyse the phosphorylation of the ketosamine moiety of glycated proteins. The instability of a phosphorylated ketosamine leads to its degradation, and KT3K is thus thought to be involved in protein repair.The function of the prokaryotic members of this group has not been established. Howev... | Fructosamine kinase family |
c_qehehooguwba | First, they are similar to characterised FN3K from mouse and human. Second, the Escherichia coli members are found in close proximity on the genome to fructose-6-phosphate kinase (PfkB). Last, FN3K activity has been found in the blue-green algae Anacystis montana indicating such activity-directly demonstrated in eukary... | Fructosamine kinase family |
c_2o57378l7x8b | In molecular biology the nematode Her-1 protein is a protein which adopts an all-helical structure with two subdomains: amino acids 19-80 comprise a left-handed three-helix bundle with an overhand connection between the second and third helices, whilst amino acids 81-164 comprise a left-handed anti-parallel four-helix ... | Nematode Her-1 |
c_c2o9wg74fkq0 | In molecular biology the orange carotenoid N-terminal domain is a protein domain found predominantly at the N-terminus of the Orange carotenoid protein (OCP), and is involved in non-covalent binding of a carotenoid chromophore. It is unique for being present in soluble proteins, whereas the vast majority of domains cap... | Orange carotenoid N-terminal domain |
c_6uhrv196feah | The domain adopts an alpha-helical structure consisting of two four-helix bundles.Orange carotenoid-binding proteins (OCP) were first identified in cyanobacterial species, where they occur associated with phycobilisome in the cellular thylakoid membrane. These proteins function in photoprotection, and are essential for... | Orange carotenoid N-terminal domain |
c_syl2h2ev1lov | In full-length OCP, the NPQ activity is regulated by photoactivation by strong blue-green light. OCP seems to act as a homodimer, and binds one molecule of 3'-hydroxyechinenone (a ketocarotenoid) and one chloride ion per subunit. The carotenoid binding site is lined with a striking number of methionine residues. | Orange carotenoid N-terminal domain |
c_5hlvizhwgucc | The N-terminal domain of OCP is usually accompanied by a C-terminal domain which belongs to the NTF2 superfamily and helps bind the carotenoid. OCP can be proteolytically cleaved into a red form (RCP), which lacks 15 residues from the N-terminus and approximately 150 residues from the C terminus. This domain is implica... | Orange carotenoid N-terminal domain |
c_heb3sc0qqklf | In molecular biology the protein SSI is a Subtilisin inhibitor-like which stands for Streptomyces subtilisin inhibitor. This is a protease inhibitor. These are often synthesised as part of a larger precursor protein, either as a prepropeptide. The function of this protein domain is to prevent access of the substrate to... | SSI protease inhibitor |
c_wfarv47jsh98 | In molecular biology the protein domain S-adenosylmethionine synthetase N terminal domain is found at the N-terminal of the enzyme. | S-Adenosylmethionine synthetase enzyme |
c_9voft4bzrsu6 | In molecular biology the protein domain, Siah interacting protein N-terminal domain is found at the N-terminal of the protein, Siah interacting protein (SIP). It has a helical hairpin structure with a hydrophobic core which is further stabilised by an arrangement of side chains contributed by the two amphipathic helice... | Siah interacting protein N-terminal domain |
c_j6az3s8v69fi | In molecular biology the small pathogenicity island RNA X (alias RsaOR) gene is a bacterial non-coding RNA. It was discovered in a large-scale analysis of Staphylococcus aureus. SprX was shown to influence antibiotic resistance of the bacteria to Vancomycin and Teicoplanin glycopeptides, which are used to treat MRSA in... | SprX small RNA |
c_0h73r8t404f5 | In molecular biology there are a number of neurogenic proteins referred to as mastermind-like proteins (MAMLs) of which this domain is the N-terminal region. Mastermind-like proteins act as critical transcriptional co-activators for Notch signaling.The N-terminal domain of MAML proteins, MAML1, MAML2, MAML3, is a polyp... | MamL-1 domain |
c_bkfbt65dmdd7 | The C-terminal region is required for transcriptional activation. Notch receptors are cleaved upon ligand engagement and the intracellular domain of Notch shuttles to the nucleus. MAMLs form a functional DNA-binding complex with the cleaved Notch receptor and the transcription factor CSL, thereby regulating transcripti... | MamL-1 domain |
c_mov69fetc8wk | MAML proteins may also play roles as key transcriptional co-activators in other signal transduction pathways as well, including: muscle differentiation and myopathies (MEF2C), tumour suppressor pathway (p53) and colon carcinoma survival (beta-catenin). MAML proteins could mediate cross-talk among the various signaling ... | MamL-1 domain |
c_ijlbtpizhr3l | In molecular biology this protein domain, refers to UbiD, which is found in prokaryotes, archaea and fungi, with two members in Archaeoglobus fulgidus. They are related to UbiD, a 3-octaprenyl-4-hydroxybenzoate carboxy-lyase from Escherichia coli that is involved in ubiquinone biosynthesis. The member from Helicobacter... | UbiD protein domain |
c_upf2ntt72qy8 | In molecular biology, "formylglycine-generating enzyme" (sometimes annotated as formylglycine-generating sulfatase enzyme) is the name of the FGE protein domain, whether or not the protein is catalytically active. Both prokaryotic and eukaryotic homologs of FGE possess highly conserved active sites — including the cata... | Formylglycine-generating enzyme |
c_ittrh74xbn6a | In molecular biology, 2'-5'-oligoadenylate synthetase (2-5A synthetase) is an enzyme (EC 2.7.7.84) that reacts to interferon signal. It is an antiviral enzyme that counteracts viral attack by degrading RNAs, both viral and host. The enzyme uses ATP in 2'-specific nucleotidyl transfer reactions to synthesize 2'-5'-oligo... | 2'-5'-oligoadenylate synthase |
c_pvzzlswbtjd5 | In molecular biology, ADF-H domain (actin-depolymerising factor homology domain) is an approximately 150 amino acid motif that is present in three phylogenetically distinct classes of eukaryotic actin-binding proteins. ADF/cofilins, which include ADF, cofilin, destrin, actophorin, coactosin, depactin and glia maturatio... | ADF-H domain |
c_q7l8e5ddd9gh | ADF/cofilins bind ADP-actin with higher affinity than ATP-actin and inhibit the spontaneous nucleotide exchange on actin monomers Twinfilins, which are actin monomer-binding proteins that are composed of two ADF-H domains Abp1/Drebrins, which are relatively large proteins composed of an N-terminal ADF-H domain followed... | ADF-H domain |
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