Directed mutagenesis identifies amino acid residues involved in elongation factor Tu binding to yeast Phe-tRNAPhe.
about
Elongation Factor Tu Prevents Misediting of Gly-tRNA(Gly) Caused by the Design Behind the Chiral Proofreading Site of D-Aminoacyl-tRNA DeacylaseThe determination of tRNALeu recognition nucleotides for Escherichia coli L/F transferaseConserved discrimination against misacylated tRNAs by two mesophilic elongation factor Tu orthologsLabeled EF-Tus for rapid kinetic studies of pretranslocation complex formationTuning the affinity of aminoacyl-tRNA to elongation factor Tu for optimal decodingFunctional consequences of T-stem mutations in E. coli tRNAThrUGU in vitro and in vivo.Initiation factor eIF2γ promotes eIF2-GTP-Met-tRNAi(Met) ternary complex binding to the 40S ribosome.Is the sequence-specific binding of aminoacyl-tRNAs by EF-Tu universal among bacteria?Histidine 66 in Escherichia coli elongation factor tu selectively stabilizes aminoacyl-tRNAs.Saccharomyces cerevisiae Eukaryotic Elongation Factor 1A (eEF1A) Is Methylated at Lys-390 by a METTL21-Like Methyltransferase.The 51-63 base pair of tRNA confers specificity for binding by EF-TuElongation factor Ts directly facilitates the formation and disassembly of the Escherichia coli elongation factor Tu·GTP·aminoacyl-tRNA ternary complex.Mechanism and Regulation of Protein Synthesis in Saccharomyces cerevisiae.Lack of discrimination against non-proteinogenic amino acid norvaline by elongation factor Tu from Escherichia coli.Understanding the sequence specificity of tRNA binding to elongation factor Tu using tRNA mutagenesis.Outwitting EF-Tu and the ribosome: translation with d-amino acids.Modulation of individual steps in group I intron catalysis by a peripheral metal ion.The interface between Escherichia coli elongation factor Tu and aminoacyl-tRNA.Role of D-aminoacyl-tRNA deacylase beyond chiral proofreading as a cellular defense against glycine mischarging by AlaRS.A discriminator code-based DTD surveillance ensures faithful glycine delivery for protein biosynthesis in bacteria
P2860
Q28552401-322380B7-8557-4848-A977-FA264F55EEFAQ33929029-5DCA430D-2D22-4100-B4C0-29B16FA70182Q33961608-C63FFC3A-9FA8-41D7-9979-2B33F2BD6506Q34361127-55E16638-041F-45FB-8366-D68D604B3F2AQ34750390-7CFDCB50-D691-4298-BBCB-00FCFFFD2504Q34985799-065A26DF-1D99-4894-A9E5-FC4440076E12Q35534370-B9D6234A-3B77-4447-907B-624C79F81869Q35617298-810B2022-D66D-4620-A5C3-AFC944979FD5Q35668805-E4B9A704-4790-4F22-976C-2E6E09D8E448Q35675772-48A690CD-CC67-476B-8B89-8A8F7A992573Q35794689-562EAB48-C024-451B-B7A5-4E5032C0A0DFQ36832738-3E4554EF-29E4-4970-B3EF-2C7FED0FEAEDQ36875727-41191D19-F968-42AA-8422-84871F2CF9AAQ36910679-A5B0FEAC-F373-45C6-A925-8FFAFF350B77Q37425352-4265E1D6-898D-46BE-9775-829E5E68D9E4Q41127564-B88CE216-44CA-4BF1-BFE3-E025018DA97AQ41749632-E788571B-DFFE-497E-B7B1-FAE3E380C513Q42123631-F2D458E3-717D-463D-B6BE-37A0A2A8D84AQ42290156-4FA8DE03-AA3B-4B1B-AD83-41350FE1E6FFQ56530058-E9B97D9B-4B44-4CD1-A160-0743BD92CA06
P2860
Directed mutagenesis identifies amino acid residues involved in elongation factor Tu binding to yeast Phe-tRNAPhe.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年学术文章
@wuu
2007年学术文章
@zh
2007年学术文章
@zh-cn
2007年学术文章
@zh-hans
2007年学术文章
@zh-my
2007年学术文章
@zh-sg
2007年學術文章
@yue
2007年學術文章
@zh-hant
name
Directed mutagenesis identifie ...... binding to yeast Phe-tRNAPhe.
@en
Directed mutagenesis identifie ...... binding to yeast Phe-tRNAPhe.
@nl
type
label
Directed mutagenesis identifie ...... binding to yeast Phe-tRNAPhe.
@en
Directed mutagenesis identifie ...... binding to yeast Phe-tRNAPhe.
@nl
prefLabel
Directed mutagenesis identifie ...... binding to yeast Phe-tRNAPhe.
@en
Directed mutagenesis identifie ...... binding to yeast Phe-tRNAPhe.
@nl
P2860
P1476
Directed mutagenesis identifie ...... binding to yeast Phe-tRNAPhe.
@en
P2093
Lee E Sanderson
Olke C Uhlenbeck
P2860
P304
P356
10.1016/J.JMB.2007.01.075
P407
P577
2007-02-06T00:00:00Z