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  • amino
  • Among them, a set of RNA sequences, referred to as flexizymes (Fxs), discovered in our laboratory are able to charge amino acids onto tRNAs. (nih.gov)
  • The 5′-leader ribozyme recognizes a specific amino acid and self-charges to the 3′-end of RNA. (nih.gov)
  • Gene
  • TRY-GTA11-1 (Transfer RNA-Tyr (GTA) 11-1) is an RNA Gene, and is affiliated with the non-coding RNA class. (genecards.org)
  • Morpholinos are synthetic oligonucleotides that can be used to inhibit nuclear RNA splicing or mRNA translation and are the common gene inhibition reagent in Xenopus as neither siRNA or miRNA have yet been shown to reproducibly function in frog embryos. (wikipedia.org)
  • cell
  • Pillé and colleagues previously found that blocking RhoC expression by short interfering RNA significantly inhibited cell proliferation of breast tumor cells in vitro as well as tumor growth in an animal model ( 12 ). (aacrjournals.org)
  • Experiment: Gurdon used a technique known as nuclear transfer to replace the killed-off nucleus of a frog (Xenopus) egg with a nucleus from a mature cell (intestinal epithelial). (wikipedia.org)
  • Structure
  • The NH2-terminal structure of the membrane-binding domain is CH3(CH2)12-CO-Gly-Ala-Gln-Leu-Ser-Thr-Leu-Gly-His-Met-Val-Leu-Phe-Pro-Val-Trp-Phe-Leu-Tyr-Ser-Leu-Leu-Met-Lys. (wikipedia.org)
  • Entry
  • Now EC 3.4.11.2, membrane alanyl aminopeptidase EC 3.4.13.7: Glu-Glu dipeptidase EC 3.4.13.8: Transferred entry: Pro-X dipeptidase. (wikipedia.org)
  • Now EC 3.4.13.18, cytosol nonspecific dipeptidase EC 3.4.13.9: X-Pro dipeptidase EC 3.4.13.10: Transferred entry: β-aspartyldipeptidase. (wikipedia.org)
  • Now EC 3.4.19.5, β-aspartyl-peptidase EC 3.4.13.11: Transferred entry: dipeptidase. (wikipedia.org)
  • Now EC 3.4.13.19, membrane dipeptidase EC 3.4.13.12: Met-X dipeptidase EC 3.4.13.13: Transferred entry: homocarnosinase. (wikipedia.org)
  • Now EC 3.4.13.3, X-His dipeptidase EC 3.4.13.14: Deleted entry: γ-glutamyldipeptidase EC 3.4.13.15: Transferred entry: N2-β-alanylarginine dipeptidase. (wikipedia.org)
  • Now EC 3.4.19.1, acylaminoacyl-peptidase EC 3.4.14.4: dipeptidyl-peptidase III EC 3.4.14.5: dipeptidyl-peptidase IV EC 3.4.14.6: dipeptidyl-dipeptidase EC 3.4.14.7: Deleted entry: tetralysine endopeptidase EC 3.4.14.8: Transferred entry: tripeptidyl peptidase. (wikipedia.org)
  • Now EC 3.4.14.10, tripeptidyl-peptidase II EC 3.4.14.9: tripeptidyl-peptidase I EC 3.4.14.10: tripeptidyl-peptidase II EC 3.4.14.11: Xaa-Pro dipeptidyl-peptidase EC 3.4.14.12: Xaa-Xaa-Pro tripeptidyl-peptidase EC 3.4.15.1: peptidyl-dipeptidase A EC 3.4.15.2: Transferred entry: pepdidyl carboxyamidase. (wikipedia.org)
  • Now EC 3.4.19.2, peptidyl-glycinamidase EC 3.4.15.3: Transferred entry: dipeptidyl carboxypeptidase. (wikipedia.org)
  • Now EC 3.4.15.5, peptidyl-dipeptidase Dcp EC 3.4.15.4: Peptidyl-dipeptidase B EC 3.4.15.5: Peptidyl-dipeptidase Dcp EC 3.4.15.6: cyanophycinase EC 3.4.16.1: Transferred entry: serine carboxypeptidase. (wikipedia.org)
  • Now included with EC 3.4.16.5, carboxypeptidase C EC 3.4.16.4: serine-type D-Ala-D-Ala carboxypeptidase EC 3.4.16.5: carboxypeptidase c EC 3.4.16.6: carboxypeptidase D EC 3.4.17.1: carboxypeptidase A EC 3.4.17.2: carboxypeptidase B EC 3.4.17.3: lysine carboxypeptidase EC 3.4.17.4: Gly-X carboxypeptidase EC 3.4.17.5: Deleted entry: aspartate carboxypeptidase EC 3.4.17.6: alanine carboxypeptidase EC 3.4.17.7: Transferred entry: acylmuramoyl-alanine carboxypeptidase. (wikipedia.org)
  • Now EC 3.4.21.34 (plasma kallikrein) and EC 3.4.21.35 (tissue kallikrein) EC 3.4.21.9: enteropeptidase EC 3.4.21.10: acrosin EC 3.4.21.11: Transferred entry: elastase. (wikipedia.org)
  • Now EC 3.4.21.37, leukocyte elastase EC 3.4.21.12: alpha-lytic endopeptidase EC 3.4.21.13: Transferred entry: Phaseolus proteinase. (wikipedia.org)
  • Now EC 3.4.16.6, carboxypeptidase D EC 3.4.21.14: Transferred entry: now EC 3.4.21.67 endopeptidase So EC 3.4.21.15: Transferred entry: Aspergillus alkaline proteinase. (wikipedia.org)
  • Now EC 3.4.21.74, venombin A EC 3.4.21.29: Transferred entry: Bothrops atrox serine proteinase. (wikipedia.org)
  • Now EC 3.4.21.74, venombin A EC 3.4.21.30: Transferred entry: Crotalus adamanteus serine proteinase. (wikipedia.org)
  • Now EC 3.4.21.74, venombin A EC 3.4.21.31: Transferred entry: urokinase. (wikipedia.org)
  • Tyrosine
  • Tyrosine-tRNA ligase (EC 6.1.1.1), also known as tyrosyl-tRNA synthetase (symbol YARS), is an enzyme that catalyzes the chemical reaction ATP + L-tyrosine + tRNA(Tyr) ⇌ {\displaystyle \rightleftharpoons } AMP + diphosphate + L-tyrosyl-tRNA(Tyr) The three substrates of this enzyme are ATP, L-tyrosine, and a tyrosine-specific transfer RNA [tRNA(Tyr) or tRNATyr], whereas its three products are AMP, diphosphate, and L-tyrosyl-tRNA(Tyr). (wikipedia.org)
  • Mutagenesis experiments have shown that the flexibility of the peptide that links the α-ACB and S4-like domains is responsible for the disorder of the latter in the structure and that elements of sequence in this linker peptide are essential for the binding of tRNA(Tyr) by YARS and its aminoacylation with tyrosine. (wikipedia.org)
  • The crystal structure of the complex between YARS from Methanococcus jannaschii, tRNA(Tyr) and L-tyrosine has been solved at 1.95 Å resolution. (wikipedia.org)
  • They contain the well-known classical receptor (a) and non-receptor PTPs (b), which are strictly tyrosine-specific, and the DSPs (c) which target Ser/Thr as well as Tyr and are the most diverse in terms of substrate specificity. (wikipedia.org)
  • The water molecule is held in place by hydrogen bonding from the hydroxyl group of a nearby tyrosine residue (Tyr-194). (wikipedia.org)
  • residues
  • Proteins are phosphorylated predominantly on Ser, Thr and Tyr residues, which account for 79.3, 16.9 and 3.8% respectively of the phosphoproteome, at least in mammals. (wikipedia.org)
  • During Hg2+ transfer to the catalytic active site from the C terminus cysteine residues, a trigonal planar intermediate is formed stabilized by hydrogen bonding of a water molecule to the thiolates. (wikipedia.org)
  • inhibit
  • Another experimental approach using antisense RNA to inhibit gene expression led to the identification of some 150 essential genes in Staphylococcus aureus ( 5 ). (pnas.org)
  • Morpholinos are synthetic oligonucleotides that can be used to inhibit nuclear RNA splicing or mRNA translation and are the common gene inhibition reagent in Xenopus as neither siRNA or miRNA have yet been shown to reproducibly function in frog embryos. (wikipedia.org)
  • genes
  • Finally, the use of antisense RNA is limited to the genes for which an adequate expression of the inhibitory RNA can be obtained in the organism under study. (pnas.org)
  • protein
  • We showed that a single base substitution from A to G at position 836 in the coding sequence of Oryza sativa beta-1,6-N-acetylglucosaminyl transferase ( OsGCNT ), effectively mutating Tyr to Cys at position 279 in the translated protein sequence, was responsible for the spotted-leaf phenotype as it could be rescued by functional complementation. (biomedcentral.com)
  • The protein Tyr phosphatase (PTP) super-family forms the second group, and the aspartate-based protein phosphatases the third. (wikipedia.org)