How many EF-Tu molecules participate in aminoacyl-tRNA binding and peptide bond formation in Escherichia coli translation?
about
A Steric Block in Translation Caused by the Antibiotic SpectinomycinStructural basis for hygromycin B inhibition of protein biosynthesisElongation factor Tu: a molecular switch in protein biosynthesis.GTP consumption of elongation factor Tu during translation of heteropolymeric mRNAs.Enacyloxin IIa, an inhibitor of protein biosynthesis that acts on elongation factor Tu and the ribosome.Two GTPs are consumed on EF-Tu per peptide bond in poly(Phe) synthesis, in spite of switching stoichiometry of the EF-Tu.aminoacyl-tRNA complex with temperature.Design and properties of efficient tRNA:EF-Tu FRET system for studies of ribosomal translation.tRNA-ribosome interactions.RNase II is important for A-site mRNA cleavage during ribosome pausing.A single amino acid substitution in elongation factor Tu disrupts interaction between the ternary complex and the ribosome.Solution of the ribosome riddle: how the ribosome selects the correct aminoacyl-tRNA out of 41 similar contestants.Isolation and stability of ternary complexes of elongation factor Tu, GTP and aminoacyl-tRNA.Pulvomycin-resistant mutants of E.coli elongation factor Tu.Antibiotic resistance mechanisms of mutant EF-Tu species in Escherichia coli.Elongation factor Tu, a GTPase triggered by codon recognition on the ribosome: mechanism and GTP consumption.Special peptidyl-tRNA molecules can promote translational frameshifting without slippage.Error-prone EF-Tu reduces in vivo enzyme activity and cellular growth rate.Streptococcus pneumoniae From Patients With Hemolytic Uremic Syndrome Binds Human Plasminogen via the Surface Protein PspC and Uses Plasmin to Damage Human Endothelial Cells.Mutants of EF-Tu defective in binding aminoacyl-tRNA.Phosphorylation of elongation factor Tu prevents ternary complex formation.Stoichiometry of the EF-Tu.GTP complex with aminoacyl-tRNA: ternary of quinternary?Purification and crystallization of the ternary complex of elongation factor Tu:GTP and Phe-tRNAPhe
P2860
Q27647153-9E5F2510-D6D9-4E18-90AC-5A9D5E223B11Q27650910-5981A082-A37C-46B6-B914-665A0004C5C5Q34399059-28881911-FBA3-49D0-A79C-420B2AEA5C39Q34554084-0AA5BE91-C7F2-4C86-9205-7D04E97039DCQ35850671-D3DA69A6-24FB-458D-84E8-5FB06B663CC0Q36731052-45441EEC-A31D-439C-BB87-74ECC535E4D3Q36778946-A43532BE-56A4-4D4C-A557-79A7031E9798Q36809234-B857BC81-FC42-4271-9D93-43FADF239279Q37365620-BDDF22BC-C05E-4663-8A46-F74BF6A55F89Q39895623-B146253E-D7E2-434F-809B-1EE177285633Q40491911-DD6CF0CA-B6CD-4121-A416-F15865899FC7Q40531147-5B0FDB09-1595-436F-8EEC-9EA8E3604455Q40793673-B3FCE817-5FEE-4231-BCC8-D41C596AAA83Q41043851-27CD0E3A-33C6-4BA2-8A0E-8AF4F1114549Q41043888-B1BBD88E-5295-4666-8531-EB48AD35C313Q41945785-73D868E0-3248-41A0-8D4E-2A8CBEEAAB7BQ45157987-32852F29-669A-47D2-97F7-575136F7CDB0Q47714965-B03E8830-0740-42D5-B6B5-CDFB5BDC14EDQ50139870-B1BFD56E-AA96-402B-9BBB-C6D705439EDFQ54008053-914A1658-752D-40D2-A0FF-D9E7844CD6DFQ54618748-BC4695D7-D5E9-469A-AFC4-5AD6596CA0FCQ57978207-A9C4DAC2-29AD-4BD3-9E36-DD39CBA875FC
P2860
How many EF-Tu molecules participate in aminoacyl-tRNA binding and peptide bond formation in Escherichia coli translation?
description
1990 nî lūn-bûn
@nan
1990 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1990 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1990年の論文
@ja
1990年論文
@yue
1990年論文
@zh-hant
1990年論文
@zh-hk
1990年論文
@zh-mo
1990年論文
@zh-tw
1990年论文
@wuu
name
How many EF-Tu molecules parti ...... Escherichia coli translation?
@ast
How many EF-Tu molecules parti ...... Escherichia coli translation?
@en
type
label
How many EF-Tu molecules parti ...... Escherichia coli translation?
@ast
How many EF-Tu molecules parti ...... Escherichia coli translation?
@en
prefLabel
How many EF-Tu molecules parti ...... Escherichia coli translation?
@ast
How many EF-Tu molecules parti ...... Escherichia coli translation?
@en
P2093
P1476
How many EF-Tu molecules parti ...... Escherichia coli translation?
@en
P2093
P304
P356
10.1016/0022-2836(90)90074-V
P407
P577
1990-02-01T00:00:00Z