About: The effect of mutations in EF-Tu on its affinity for tRNA as measured by two novel and independent methods of general applicability

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About: The effect of mutations in EF-Tu on its affinity for tRNA as measured by two novel and independent methods of general applicability Goto Sponge NotDistinct Permalink

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scientific article published on 01 January 2000

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rdf:type	Item
description	wetenschappelijk artikel (nl) wüsseschaftlicher Artikel, wo im Johr 2000 veröffentlicht worden isch (gsw) наукова стаття, опублікована в січні 2000 (uk) article scientifique publié en 2000 (fr) im Jahr 2000 veröffentlichter wissenschaftlicher Artikel (de) artículu científicu espublizáu en xineru de 2000 (ast) articolo scientifico (pubblicato il 2000) (it) artikull shkencor i botuar më 01 janar 2000 (sq) scientific article published on 01 January 2000 (en)
publication date	wds:Q73385508-623AFFBF-F75E-4CEC-A615-F4F84FC3490C
publication date	2000-01-01 00:00:00Z (xsd:dateTime)
cites work	wds:Q73385508-11867091-B5A2-4743-BEF3-2CEDED4BDF60 wds:Q73385508-1571434E-225E-45FB-BED7-A75F191CBA71 wds:Q73385508-17B2CD00-6489-4728-B315-9D3DC669A5FE wds:Q73385508-22E2800E-9AA3-4E8B-B1E1-EAA9EE966601 wds:Q73385508-30DCDB52-4B40-42CF-BB87-3BA4099372AD wds:Q73385508-3426D08F-2C6D-4D4B-B129-79860661165F wds:Q73385508-38114C24-060E-4B25-A947-6AFCD84BF657 wds:Q73385508-3CB16397-2569-4BEF-9C9C-78C54E3F9646 wds:Q73385508-41DC5338-AB28-41BE-B362-B290CA4D9D12 wds:Q73385508-43FBD735-168C-4C2C-B920-15A3F753947E wds:Q73385508-54CC79A8-4200-4A1F-A1E9-16C21DC6927B wds:Q73385508-55FF4A03-0F69-4B43-9313-B0047D271C5A wds:Q73385508-57C2E938-A7B7-4D7A-BD6E-717892043FE3 wds:Q73385508-5B0735E0-F45D-495F-864B-621AAFC538B4 wds:Q73385508-7C100280-2DD8-42AC-8AB9-5AE7FD796CBE wds:Q73385508-82E7CA66-EFEA-4F48-9F5E-A4D27391CFAC wds:Q73385508-8DF9576E-DA25-4997-B9FC-FF08957B10D2 wds:Q73385508-99DDD406-1DCA-46AA-9112-6235C24BE1DE wds:Q73385508-AAFE4628-25D9-4683-8D43-A74CE4239B2C wds:Q73385508-C843D5F3-85D8-475E-951A-54570565FA50 wds:Q73385508-D988F315-015D-4039-A61E-24FB1AEF17D6 wds:Q73385508-DB8BB89E-6948-48ED-A94A-8AC05311DF85 wds:Q73385508-F10E7328-4018-4EA0-8581-1CB252BE97C8 wds:Q73385508-FC3557F7-3476-4E13-A6A4-CD2AAA473AED
cites work	Kinetic studies of Escherichia coli elongation factor Tu-guanosine 5'-triphosphate-aminoacyl-tRNA complexes Crystal structure of the ternary complex of Phe-tRNAPhe, EF-Tu, and a GTP analog Ternary Complex Formation between Elongation Factor Tu, GTP and Aminoacyl-tRNA: an Equilibrium Study An Algorithm for Least-Squares Estimation of Nonlinear Parameters Crystal structure of active elongation factor Tu reveals major domain rearrangements Direct determination of the association constant between elongation factor Tu X GTP and aminoacyl-tRNA using fluorescence. Divergent effects of fluoroaluminates on the peptide chain elongation factors EF-Tu and EF-G as members of the GTPase superfamily. Aminoacyl transfer ribonucleic acid binding site of the bacterial elongation factor Tu A second tRNA binding site on elongation factor Tu is induced while the factor is bound to the ribosome Discrimination between aminoacyl groups on su+ 7 tRNA by elongation factor Tu Antibiotic resistance mechanisms of mutant EF-Tu species in Escherichia coli Identification of a histidine residue near the aminoacyl transfer ribonucleic acid binding site of elongation factor Tu. Escherichia coli elongation-factor-Tu mutants with decreased affinity for aminoacyl-tRNA. The determination of binding parameters from protection experiments. A quantitative assay for ternary complex formation of elongation factor Tu, GTP, and aminoacyl-tRNA. The complex formation between Escherichia coli aminoacyl-tRNA, elongation factor Tu and GTP. The effect of the side-chain of the amino acid linked to tRNA Isolation and functional analysis of histidine-tagged elongation factor Tu Pulvomycin-resistant mutants of E.coli elongation factor Tu. Mutants of EF-Tu defective in binding aminoacyl-tRNA. Fluorescence characterization of the interaction of various transfer RNA species with elongation factor Tu.GTP: evidence for a new functional role for elongation factor Tu in protein biosynthesis. Interaction of elongation factor Tu from Escherichia coli with aminoacyl-tRNA carrying a fluorescent reporter group on the 3' terminus. Interaction of aminoacyl-tRNA with bacterial elongation factor Tu: GTP complex: effects of the amino group of amino acid esterified to tRNA, the amino acid side chain, and tRNA structure Substitution of Arg230 and Arg233 in Escherichia coli elongation factor Tu strongly enhances its pulvomycin resistance Translational activities of EF-Tu [G222D] which cannot be reconciled with the classical scheme of the polypeptide chain elongation cycle. A growth-defective kirromycin-resistant EF-Tu Escherichia coli mutant and a spontaneously evolved suppression of the defect.
author name string	wds:Q73385508-39E0F45B-40A1-4CE8-BC7A-133E2832EC50 wds:Q73385508-B12F4EAE-833A-43BF-8FF2-7F864ED100CB wds:Q73385508-B88336A3-7D47-4FE4-B12E-C68F85FCABA1 wds:Q73385508-C6897FE5-DB06-4983-A8D1-B063F9550003
author name string	B Kraal A P Potapov E L Vorstenbosch J M de Graaf
rdfs:label	The effect of mutations in EF-Tu on its affinity for tRNA as measured by two novel and independent methods of general applicability (en) The effect of mutations in EF-Tu on its affinity for tRNA as measured by two novel and independent methods of general applicability (nl) The effect of mutations in EF-Tu on its affinity for tRNA as measured by two novel and independent methods of general applicability (sq)
skos:prefLabel	The effect of mutations in EF-Tu on its affinity for tRNA as measured by two novel and independent methods of general applicability (en) The effect of mutations in EF-Tu on its affinity for tRNA as measured by two novel and independent methods of general applicability (nl) The effect of mutations in EF-Tu on its affinity for tRNA as measured by two novel and independent methods of general applicability (sq)
name	The effect of mutations in EF-Tu on its affinity for tRNA as measured by two novel and independent methods of general applicability (en) The effect of mutations in EF-Tu on its affinity for tRNA as measured by two novel and independent methods of general applicability (nl) The effect of mutations in EF-Tu on its affinity for tRNA as measured by two novel and independent methods of general applicability (sq)
title	wds:Q73385508-EC5C77CB-F5B2-4D38-8EF6-3EE398F1CC7C
title	The effect of mutations in EF-Tu on its affinity for tRNA as measured by two novel and independent methods of general applicability (en)
page(s)	wds:Q73385508-C1D6D05C-D4E6-4965-A5E9-CFB5959E1067
page(s)	1-14
instance of	wds:Q73385508-0151F562-DE29-4CB0-B80C-C9E5CA523609
instance of	scholarly article
PubMed ID	wds:Q73385508-6AAD0D6E-7DA7-4021-ABC9-8EEA26527C1D
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/10647810
PubMed ID	10647810
published in	wds:Q73385508-5F0DB481-CF59-4C9C-B732-DDECDDFF9903
published in	Journal of Proteomics
issue	wds:Q73385508-52B28DC6-CBFE-4974-B202-4958C63A54E4
volume	wds:Q73385508-96C5CD97-9AFB-4375-8A5E-110F90A28955
issue	1-2
volume	42
DOI	wds:Q73385508-0F0C82D3-112C-4C63-8DEF-1FBA52398D64
DOI	http://dx.doi.org/10.1016/S0165-022X(99)00032-9
DOI	10.1016/S0165-022X(99)00032-9
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q73385508
is cites work of	RNA-dependent lipid remodeling by bacterial multiple peptide resistance factors A signal relay between ribosomal protein S12 and elongation factor EF-Tu during decoding of mRNA. Tuning the affinity of aminoacyl-tRNA to elongation factor Tu for optimal decoding Phenylalanyl-tRNA synthetase editing defects result in efficient mistranslation of phenylalanine codons as tyrosine.

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