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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
MeSH Review

Protein Biosynthesis

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Disease relevance of Protein Biosynthesis


Psychiatry related information on Protein Biosynthesis


High impact information on Protein Biosynthesis

  • Their ability to bind S1 ribosomal protein suggests that poly(A) tracts may also play a role in mRNA translation [7].
  • Female flies must inhibit msl-2 mRNA translation for survival, and this inhibition is mediated by Sex-lethal (SXL) binding to sites in both the 5' and the 3' untranslated regions (UTRs) [8].
  • In response to IFN-gamma, GluProRS is phosphorylated and released from the MSC, binds the Cp 3'-untranslated region in an mRNP containing three additional proteins, and silences Cp mRNA translation [9].
  • Evidence for a pioneer round of mRNA translation: mRNAs subject to nonsense-mediated decay in mammalian cells are bound by CBP80 and CBP20 [10].
  • FMRP harbors three RNA binding domains, associates with polysomes, and is thought to regulate mRNA translation and/or localization, but the RNAs to which it binds are unknown [11].

Chemical compound and disease context of Protein Biosynthesis


Biological context of Protein Biosynthesis


Anatomical context of Protein Biosynthesis


Associations of Protein Biosynthesis with chemical compounds


Gene context of Protein Biosynthesis


Analytical, diagnostic and therapeutic context of Protein Biosynthesis


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  4. Flavivirus premembrane protein cleavage and spike heterodimer secretion require the function of the viral proteinase NS3. Lobigs, M. Proc. Natl. Acad. Sci. U.S.A. (1993) [Pubmed]
  5. FMRP interferes with the Rac1 pathway and controls actin cytoskeleton dynamics in murine fibroblasts. Castets, M., Schaeffer, C., Bechara, E., Schenck, A., Khandjian, E.W., Luche, S., Moine, H., Rabilloud, T., Mandel, J.L., Bardoni, B. Hum. Mol. Genet. (2005) [Pubmed]
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  8. A dual inhibitory mechanism restricts msl-2 mRNA translation for dosage compensation in Drosophila. Beckmann, K., Grskovic, M., Gebauer, F., Hentze, M.W. Cell (2005) [Pubmed]
  9. Noncanonical function of glutamyl-prolyl-tRNA synthetase: gene-specific silencing of translation. Sampath, P., Mazumder, B., Seshadri, V., Gerber, C.A., Chavatte, L., Kinter, M., Ting, S.M., Dignam, J.D., Kim, S., Driscoll, D.M., Fox, P.L. Cell (2004) [Pubmed]
  10. Evidence for a pioneer round of mRNA translation: mRNAs subject to nonsense-mediated decay in mammalian cells are bound by CBP80 and CBP20. Ishigaki, Y., Li, X., Serin, G., Maquat, L.E. Cell (2001) [Pubmed]
  11. Fragile X mental retardation protein targets G quartet mRNAs important for neuronal function. Darnell, J.C., Jensen, K.B., Jin, P., Brown, V., Warren, S.T., Darnell, R.B. Cell (2001) [Pubmed]
  12. 1-Phosphatidylinositol 4-phosphate 5-kinase (EC a proliferation- and malignancy-linked signal transduction enzyme. Singhal, R.L., Prajda, N., Yeh, Y.A., Weber, G. Cancer Res. (1994) [Pubmed]
  13. Tyrosinase-mediated inhibition of in vitro leucine incorporation into mouse melanoma by 4-isopropylcatechol. Sugano, H., Sugano, I., Jimbow, K., Fitzpatrick, T.B. Cancer Res. (1975) [Pubmed]
  14. Amino acid substitutions in protein biosynthesis. Poly(A)-directed polyphenylalanine synthesis. Pezzuto, J.M., Hecht, S.M. J. Biol. Chem. (1980) [Pubmed]
  15. Studies on the function of two adjacent N6,N6-dimethyladenosines near the 3' end of 16 S ribosomal RNA of Escherichia coli. II. The effect of the absence of the methyl groups on initiation of protein biosynthesis. Poldermans, B., Van Buul, C.P., Van Knippenberg, P.H. J. Biol. Chem. (1979) [Pubmed]
  16. Structure and function of the phenazine biosynthesis protein PhzF from Pseudomonas fluorescens 2-79. Parsons, J.F., Song, F., Parsons, L., Calabrese, K., Eisenstein, E., Ladner, J.E. Biochemistry (2004) [Pubmed]
  17. Block of HAC1 mRNA translation by long-range base pairing is released by cytoplasmic splicing upon induction of the unfolded protein response. Rüegsegger, U., Leber, J.H., Walter, P. Cell (2001) [Pubmed]
  18. Control of mRNA translation preserves endoplasmic reticulum function in beta cells and maintains glucose homeostasis. Scheuner, D., Mierde, D.V., Song, B., Flamez, D., Creemers, J.W., Tsukamoto, K., Ribick, M., Schuit, F.C., Kaufman, R.J. Nat. Med. (2005) [Pubmed]
  19. Microtubule-associated protein 1 light chain 3 is a fibronectin mRNA-binding protein linked to mRNA translation in lamb vascular smooth muscle cells. Zhou, B., Boudreau, N., Coulber, C., Hammarback, J., Rabinovitch, M. J. Clin. Invest. (1997) [Pubmed]
  20. Biosynthesis of nitric oxide activates iron regulatory factor in macrophages. Drapier, J.C., Hirling, H., Wietzerbin, J., Kaldy, P., Kühn, L.C. EMBO J. (1993) [Pubmed]
  21. Enacyloxin IIa, an inhibitor of protein biosynthesis that acts on elongation factor Tu and the ribosome. Cetin, R., Krab, I.M., Anborgh, P.H., Cool, R.H., Watanabe, T., Sugiyama, T., Izaki, K., Parmeggiani, A. EMBO J. (1996) [Pubmed]
  22. ABC1, a novel yeast nuclear gene has a dual function in mitochondria: it suppresses a cytochrome b mRNA translation defect and is essential for the electron transfer in the bc 1 complex. Bousquet, I., Dujardin, G., Slonimski, P.P. EMBO J. (1991) [Pubmed]
  23. Translation of bicistronic viral mRNA in transfected cells: regulation at the level of elongation. Fajardo, J.E., Shatkin, A.J. Proc. Natl. Acad. Sci. U.S.A. (1990) [Pubmed]
  24. The oligo(A) tail on histone mRNA plays an active role in translational silencing of histone mRNA during Xenopus oogenesis. Sánchez, R., Marzluff, W.F. Mol. Cell. Biol. (2004) [Pubmed]
  25. A link between diabetes and atherosclerosis: Glucose regulates expression of CD36 at the level of translation. Griffin, E., Re, A., Hamel, N., Fu, C., Bush, H., McCaffrey, T., Asch, A.S. Nat. Med. (2001) [Pubmed]
  26. Evidence for role of m7G5'-phosphate group in recognition of eukaryotic mRNA by initiation factor IF-M3. Shafritz, D.A., Weinstein, J.A., Safer, B., Merrick, W.C., Weber, L.A., Hickey, E.D., Baglioni, C. Nature (1976) [Pubmed]
  27. Interleukin 1 inhibits insulin secretion from isolated rat pancreatic islets by a process that requires gene transcription and mRNA translation. Hughes, J.H., Colca, J.R., Easom, R.A., Turk, J., McDaniel, M.L. J. Clin. Invest. (1990) [Pubmed]
  28. Human mitochondrial peptide deformylase, a new anticancer target of actinonin-based antibiotics. Lee, M.D., She, Y., Soskis, M.J., Borella, C.P., Gardner, J.R., Hayes, P.A., Dy, B.M., Heaney, M.L., Philips, M.R., Bornmann, W.G., Sirotnak, F.M., Scheinberg, D.A. J. Clin. Invest. (2004) [Pubmed]
  29. Control of preprogastrin messenger RNA translation by gastric acid in the rat. Bate, G.W., Varro, A., Dimaline, R., Dockray, G.J. Gastroenterology (1996) [Pubmed]
  30. Coupling of GCN4 mRNA translational activation with decreased rates of polypeptide chain initiation. Tzamarias, D., Roussou, I., Thireos, G. Cell (1989) [Pubmed]
  31. RNA binding and translational suppression by bicoid. Rivera-Pomar, R., Niessing, D., Schmidt-Ott, U., Gehring, W.J., Jäckle, H. Nature (1996) [Pubmed]
  32. A new yeast PUF family protein, Puf6p, represses ASH1 mRNA translation and is required for its localization. Gu, W., Deng, Y., Zenklusen, D., Singer, R.H. Genes Dev. (2004) [Pubmed]
  33. Regulated Pumilio-2 binding controls RINGO/Spy mRNA translation and CPEB activation. Padmanabhan, K., Richter, J.D. Genes Dev. (2006) [Pubmed]
  34. Chaperone hsp27 inhibits translation during heat shock by binding eIF4G and facilitating dissociation of cap-initiation complexes. Cuesta, R., Laroia, G., Schneider, R.J. Genes Dev. (2000) [Pubmed]
  35. Myf5 is a novel early axonal marker in the mouse brain and is subjected to post-transcriptional regulation in neurons. Daubas, P., Tajbakhsh, S., Hadchouel, J., Primig, M., Buckingham, M. Development (2000) [Pubmed]
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  38. Mass spectrometric identification of leucine zipper-like homodimer complexes of the autoantigen L7. Witte, S., Neumann, F., Krawinkel, U., Przybylski, M. J. Biol. Chem. (1996) [Pubmed]
  39. Antimicrobial characterization and interrelationships of dirithromycin and epidirithromycin. Kirst, H.A., Creemer, L.C., Paschal, J.W., Preston, D.A., Alborn, W.E., Counter, F.T., Amos, J.G., Clemens, R.L., Sullivan, K.A., Greene, J.M. Antimicrob. Agents Chemother. (1995) [Pubmed]
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