Structural and kinetic bases for the recognition of tRNATyr by tyrosyl-tRNA synthetase.
about
Genetic code in evolution: switching species-specific aminoacylation with a peptide transplant.2.9 Å crystal structure of ligand-free tryptophanyl-tRNA synthetase: Domain movements fragment the adenine nucleotide binding siteClass I tyrosyl-tRNA synthetase has a class II mode of cognate tRNA recognitionCyclodipeptide synthases, a family of class-I aminoacyl-tRNA synthetase-like enzymes involved in non-ribosomal peptide synthesisHuman tyrosyl-tRNA synthetase shares amino acid sequence homology with a putative cytokineInteraction between the acceptor end of tRNA and the T box stimulates antitermination in the Bacillus subtilis tyrS gene: a new role for the discriminator baseNucleotides that determine Escherichia coli tRNA(Arg) and tRNA(Lys) acceptor identities revealed by analyses of mutant opal and amber suppressor tRNAs.tRNA requirements for glyQS antitermination: a new twist on tRNA.Genetic selection for active E.coli amber tRNA(Asn) exclusively led to glutamine inserting suppressors.Two conformations of a crystalline human tRNA synthetase-tRNA complex: implications for protein synthesis.Role of the extra G-C pair at the end of the acceptor stem of tRNA(His) in aminoacylation.Overproduction of tyrosyl-tRNA synthetase is toxic to Escherichia coli: a genetic analysisStructural similarities in glutaminyl- and methionyl-tRNA synthetases suggest a common overall orientation of tRNA bindingtRNA-directed transcription antitermination.The mitochondrial tyrosyl-tRNA synthetase of Podospora anserina is a bifunctional enzyme active in protein synthesis and RNA splicing.Macromolecular recognition through electrostatic repulsion.
P2860
Q24532926-E639E2D9-A406-4521-8D35-57A3575EE702Q27621756-AF2938BA-41F2-4C51-A08C-E53DC701CB32Q27639341-7F0D7452-84E7-476D-98D4-4352EF51EF93Q27666851-BC836AE8-4C09-40C8-941B-0FBFAB8C6696Q28118703-3E86AA5E-8EEE-4150-BE9B-7E37B531B30BQ28245821-5F5072E1-419E-4E20-A9A3-DC9077CEAD0FQ33912761-E281D1BE-3186-46B7-B4F8-A5D95EC37257Q34365308-CF6F27D2-D1CD-4203-9088-A184D357AA2EQ34740394-3B19DCA7-0C3A-440B-91BC-656F5C877E63Q34766900-333C2B91-D5CD-49CF-929A-58C469DE3AEAQ35948701-D5E801D9-38DF-46C5-BB5C-7B1828B0E906Q36257319-F903D187-090E-4B63-9C48-65823FA76EACQ37467882-F9D03F2D-7718-4B96-AD34-198AA8CA0D7CQ40395522-77737059-0EB5-4B10-9FF2-B80587B2384CQ40653743-585F6689-31AB-4B45-9AF7-FEBEE511E686Q40807138-4C7541D3-EADD-4F9D-B115-DAE7FB9121C4
P2860
Structural and kinetic bases for the recognition of tRNATyr by tyrosyl-tRNA synthetase.
description
1989 nî lūn-bûn
@nan
1989 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1989 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1989年の論文
@ja
1989年論文
@yue
1989年論文
@zh-hant
1989年論文
@zh-hk
1989年論文
@zh-mo
1989年論文
@zh-tw
1989年论文
@wuu
name
Structural and kinetic bases for the recognition of tRNATyr by tyrosyl-tRNA synthetase.
@ast
Structural and kinetic bases for the recognition of tRNATyr by tyrosyl-tRNA synthetase.
@en
Structural and kinetic bases for the recognition of tRNATyr by tyrosyl-tRNA synthetase.
@nl
type
label
Structural and kinetic bases for the recognition of tRNATyr by tyrosyl-tRNA synthetase.
@ast
Structural and kinetic bases for the recognition of tRNATyr by tyrosyl-tRNA synthetase.
@en
Structural and kinetic bases for the recognition of tRNATyr by tyrosyl-tRNA synthetase.
@nl
prefLabel
Structural and kinetic bases for the recognition of tRNATyr by tyrosyl-tRNA synthetase.
@ast
Structural and kinetic bases for the recognition of tRNATyr by tyrosyl-tRNA synthetase.
@en
Structural and kinetic bases for the recognition of tRNATyr by tyrosyl-tRNA synthetase.
@nl
P1476
Structural and kinetic bases for the recognition of tRNATyr by tyrosyl-tRNA synthetase.
@en
P2093
Bedouelle H
P304
P356
10.1016/0022-2836(89)90317-3
P407
P577
1989-02-01T00:00:00Z