Substrate specificity and catalysis by the editing active site of Alanyl-tRNA synthetase from Escherichia coli.
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Elongation Factor Tu Prevents Misediting of Gly-tRNA(Gly) Caused by the Design Behind the Chiral Proofreading Site of D-Aminoacyl-tRNA DeacylaseCharacterization of aminoacyl-tRNA synthetase stability and substrate interaction by differential scanning fluorimetry.Kinetic partitioning between synthetic and editing pathways in class I aminoacyl-tRNA synthetases occurs at both pre-transfer and post-transfer hydrolytic stepsBiallelic IARS Mutations Cause Growth Retardation with Prenatal Onset, Intellectual Disability, Muscular Hypotonia, and Infantile Hepatopathy.Role of D-aminoacyl-tRNA deacylase beyond chiral proofreading as a cellular defense against glycine mischarging by AlaRS.
P2860
Substrate specificity and catalysis by the editing active site of Alanyl-tRNA synthetase from Escherichia coli.
description
2011 nî lūn-bûn
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2011年の論文
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2011年論文
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2011年論文
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2011年論文
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2011年論文
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2011年論文
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2011年论文
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2011年论文
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2011年论文
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name
Substrate specificity and cata ...... thetase from Escherichia coli.
@en
Substrate specificity and cata ...... thetase from Escherichia coli.
@nl
type
label
Substrate specificity and cata ...... thetase from Escherichia coli.
@en
Substrate specificity and cata ...... thetase from Escherichia coli.
@nl
prefLabel
Substrate specificity and cata ...... thetase from Escherichia coli.
@en
Substrate specificity and cata ...... thetase from Escherichia coli.
@nl
P2093
P2860
P356
P1433
P1476
Substrate specificity and cata ...... thetase from Escherichia coli.
@en
P2093
Adam C Mirando
Astrid Lague
Christopher S Francklyn
Gregory J Smith
Susan Robey-Bond
Zvi Pasman
P2860
P304
P356
10.1021/BI1013535
P407
P577
2011-01-31T00:00:00Z