(Q31154963)

29 June 2017

title

Aspartyl-tRNA synthetase requires a conserved proline in the anticodon-binding loop for tRNA(Asn) recognition in vivo (English)

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29 June 2017

5

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author name string

Liang Feng

1

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29 June 2017

Jing Yuan

2

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29 June 2017

Helen Toogood

3

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29 June 2017

Debra Tumbula-Hansen

4

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29 June 2017

language of work or name

English

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publication date

21 March 2005

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Journal of Biological Chemistry

29 June 2017

number of pages

4

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based on heuristic

inferred from page(s)

published in

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29 June 2017

volume

280

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29 June 2017

issue

21

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29 June 2017

page(s)

20638-20641

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29 June 2017

cites work

Aminoacyl-tRNA synthesis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M500874200

Enzyme structure with two catalytic sites for double-sieve selection of substrate

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M500874200

Insights into editing from an ile-tRNA synthetase structure with tRNAile and mupirocin

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M500874200

Thermus thermophilus: a link in evolution of the tRNA-dependent amino acid amidation pathways

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M500874200

Glutamyl-tRNA(Gln) amidotransferase in Deinococcus radiodurans may be confined to asparagine biosynthesis

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M500874200

Non-discriminating and discriminating aspartyl-tRNA synthetases differ in the anticodon-binding domain

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M500874200

Evolutionary divergence of the archaeal aspartyl-tRNA synthetases into discriminating and nondiscriminating forms

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M500874200

Expanding tRNA recognition of a tRNA synthetase by a single amino acid change

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M500874200

Identity elements for specific aminoacylation of yeast tRNA(Asp) by cognate aspartyl-tRNA synthetase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M500874200

Identity of prokaryotic and eukaryotic tRNA(Asp) for aminoacylation by aspartyl-tRNA synthetase from Thermus thermophilus

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M500874200

Anticodon recognition in evolution: switching tRNA specificity of an aminoacyl-tRNA synthetase by site-directed peptide transplantation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M500874200

Cysteinyl-tRNA formation: the last puzzle of aminoacyl-tRNA synthesis.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M500874200

Location of a mutation in the aspartyl-tRNA synthetase gene of Escherichia coli K12.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M500874200

Transfer RNA-dependent amino acid biosynthesis: an essential route to asparagine formation

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M500874200

Ribozyme processed tRNA transcripts with unfriendly internal promoter for T7 RNA polymerase: production and activity

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M500874200

Protein synthesis in Escherichia coli with mischarged tRNA.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M500874200

Twenty-first aminoacyl-tRNA synthetase-suppressor tRNA pairs for possible use in site-specific incorporation of amino acid analogues into proteins in eukaryotes and in eubacteria

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M500874200

The crystal structure of asparaginyl-tRNA synthetase from Thermus thermophilus and its complexes with ATP and asparaginyl-adenylate: the mechanism of discrimination between asparagine and aspartic acid

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M500874200

21 January 2018

Identifiers

DOI

10.1074/JBC.M500874200

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29 June 2017

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