Genetic dissection of protein-protein interactions in multi-tRNA synthetase complex (Q24673361): Difference between revisions

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Revision as of 01:08, 24 December 2021 (restore) Trilotat (talk | contribs) 2,485,496 edits ‎Created claim: ADS bibcode (P819): 1999PNAS...96.4488R, #quickstatements; #temporary_batch_1640298805744 Tag: quickstatements [2.0] ← Older edit		Revision as of 04:06, 23 August 2023 (restore) undo Emijrpbot (talk | contribs) Bots 72,185,996 edits ‎Changed label, description and/or aliases in bn, fa, ur: BOT - Adding descriptions (3 languages): bn, fa, ur Newer edit →
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			১৯৯৯-এ প্রকাশিত বৈজ্ঞানিক নিবন্ধ
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			مقالهٔ علمی
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			سائنسی مضمون

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Revision as of 04:06, 23 August 2023

scientific article

Language	Label	Description	Also known as
English	Genetic dissection of protein-protein interactions in multi-tRNA synthetase complex	scientific article

Statements

instance of

scholarly article

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title

Genetic dissection of protein-protein interactions in multi-tRNA synthetase complex (English)

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main subject

protein-protein interaction

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based on heuristic

inferred from title

author name string

S B Rho

series ordinal

1

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M J Kim

series ordinal

2

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J S Lee

series ordinal

3

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W Seol

series ordinal

4

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H Motegi

series ordinal

5

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S Kim

series ordinal

6

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K Shiba

series ordinal

7

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language of work or name

English

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publication date

13 April 1999

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published in

Proceedings of the National Academy of Sciences of the United States of America

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volume

96

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issue

8

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page(s)

4488-93

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cites work

Human asparaginyl-tRNA synthetase: molecular cloning and the inference of the evolutionary history of Asx-tRNA synthetase family

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A multifunctional repeated motif is present in human bifunctional tRNA synthetase

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The p43 component of the mammalian multi-synthetase complex is likely to be the precursor of the endothelial monocyte-activating polypeptide II cytokine

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Interaction between human tRNA synthetases involves repeated sequence elements

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Expression of human aspartyl-tRNA synthetase in Escherichia coli. Functional analysis of the N-terminal putative amphiphilic helix

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7 April 2017

Cdi1, a human G1 and S phase protein phosphatase that associates with Cdk2

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Evolution of the Glx-tRNA synthetase family: the glutaminyl enzyme as a case of horizontal gene transfer

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Human cytoplasmic isoleucyl-tRNA synthetase: selective divergence of the anticodon-binding domain and acquisition of a new structural unit

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Isolation, structure and expression of mammalian genes for histidyl-tRNA synthetase

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Predicting coiled coils from protein sequences

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A conserved domain within Arc1p delivers tRNA to aminoacyl-tRNA synthetases

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Cloning of a human cDNA encoding a protein with high homology to yeast methionyl-tRNA synthetase

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7 April 2017

Cloning and characterization of cDNA encoding a human arginyl-tRNA synthetase

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7 April 2017

Human lysyl-tRNA synthetase accepts nucleotide 73 variants and rescues Escherichia coli double-defective mutant

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Macromolecular assemblage of aminoacyl-tRNA synthetases: identification of protein-protein interactions and characterization of a core protein

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The p18 component of the multisynthetase complex shares a protein motif with the beta and gamma subunits of eukaryotic elongation factor 1

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PubMed Central

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7 April 2017

Mammalian valyl-tRNA synthetase forms a complex with the first elongation factor

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Valyl-tRNA synthetase from rabbit liver. I. Purification as a heterotypic complex in association with elongation factor 1

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7 April 2017

The primary structure of human glutaminyl-tRNA synthetase. A highly conserved core, amino acid repeat regions, and homologies with translation elongation factors

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7 April 2017

Cloning and nucleotide sequence of the structural gene encoding for human tryptophanyl-tRNA synthetase

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7 April 2017

Structural analysis of the high molecular mass aminoacyl-tRNA synthetase complex. Effects of neutral salts and detergents

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PubMed Central

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7 April 2017

Structural relationships and the classification of aminoacyl-tRNA synthetases

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PubMed Central

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7 April 2017

A workbench for multiple alignment construction and analysis

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PubMed Central

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7 April 2017

Rescuing an essential enzyme-RNA complex with a non-essential appended domain

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PubMed Central

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The yeast protein Arc1p binds to tRNA and functions as a cofactor for the methionyl- and glutamyl-tRNA synthetases

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PubMed Central

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Mammalian aminoacyl-tRNA synthetases.

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PubMed Central

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The aminoacyl-tRNA synthetase family: modules at work

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PubMed Central

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28 September 2017

Aminoacyl-tRNA synthetases from higher eukaryotes.

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PubMed Central

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28 September 2017

Mechanisms of the transfer of aminoacyl-tRNA from aminoacyl-tRNA synthetase to the elongation factor 1 alpha

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PubMed Central

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28 September 2017

Aminoacyl tRNA synthetases: general scheme of structure-function relationships in the polypeptides and recognition of transfer RNAs

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PubMed Central

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28 September 2017

cDNA sequence, predicted primary structure, and evolving amphiphilic helix of human aspartyl-tRNA synthetase

1 reference

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PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=16359

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28 September 2017

Aminoacyl-tRNA synthetase family from prokaryotes and eukaryotes: structural domains and their implications

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PubMed Central

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=16359

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28 September 2017

The multienzyme complex containing nine aminoacyl-tRNA synthetases is ubiquitous from Drosophila to mammals

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PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=16359

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28 September 2017

Structural analysis of the multienzyme aminoacyl-tRNA synthetase complex: a three-domain model based on reversible chemical crosslinking

1 reference

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PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=16359

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30 May 2018

Modification of methionyl-tRNA synthetase by proteolytic cleavage and properties of the trypsin-modified enzyme.

1 reference

stated in

PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=16359

retrieved

30 May 2018

Isolation and electron microscopic characterization of the high molecular mass aminoacyl-tRNA synthetase complex from murine erythroleukemia cells.

1 reference

stated in

PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=16359

retrieved

30 May 2018

Engineering mammalian aspartyl-tRNA synthetase to probe structural features mediating its association with the multisynthetase complex

1 reference

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PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=16359

retrieved

30 May 2018

Macromolecular Complexes of Aminoacyl-tRNA Synthetases from Eukaryotes. 1.Extensive Purification and Characterization of the High-Molecular-Weight Complex(es) of Seven Aminoacyl-tRNA Synthetases from Sheep Liver

1 reference

stated in

PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=16359

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30 May 2018

Disassembly and gross structure of particulate aminoacyl-tRNA synthetases from rat liver. Isolation and the structural relationship of synthetase complexes

1 reference

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PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=16359

retrieved

30 May 2018

Cloning and analysis of a cDNA encoding mammalian arginyl-tRNA synthetase, a component of the multisynthetase complex with a hydrophobic N-terminal extension

1 reference

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PubMed Central

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=16359

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28 November 2018

The NH2-terminal extension of rat liver arginyl-tRNA synthetase is responsible for its hydrophobic properties

1 reference

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/10200289

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Antheprot: An interactive graphics software for analyzing protein structures from sequences

1 reference

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/10200289

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Evidence for similar structural organization of the multienzyme aminoacyl-tRNA synthetase complex in vivo and in vitro

1 reference

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/10200289

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Macromolecular complexes from sheep and rabbit containing seven aminoacyl-tRNA synthetases. II. Structural characterization of the polypeptide components and immunological identification of the methionyl-tRNA synthetase subunit

1 reference

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/10200289

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Perturbation of the aminoacyl-tRNA synthetase complex by salts and detergents. Importance of hydrophobic interactions and possible involvement of lipids

1 reference

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/10200289

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Modular arrangement of functional domains along the sequence of an aminoacyl tRNA synthetase

1 reference

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/10200289

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

A complex from cultured Chinese hamster ovary cells containing nine aminoacyl-tRNA synthetases. Thermolabile leucyl-tRNA synthetase from the tsH1 mutant cell line is an integral component of this complex

1 reference

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/10200289

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Leucyl-tRNA and lysyl-tRNA synthetases, derived from the high-Mr complex of sheep liver, are hydrophobic proteins

1 reference

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/10200289

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Expression of the aminoacyl-tRNA synthetase complex in cultured Chinese hamster ovary cells. Specific depression of the methionyl-tRNA synthetase component upon methionine restriction

1 reference

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/10200289

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Aspartyl-tRNA synthetase from rat: in vitro functional analysis of its assembly into the multisynthetase complex

1 reference

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/10200289

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

The two-hybrid system: an assay for protein-protein interactions

1 reference

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/10200289

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Characterization of a novel N-terminal peptide in human aspartyl-tRNA synthetase. Roles in the transfer of aminoacyl-tRNA from aminoacyl-tRNA synthetase to the elongation factor 1 alpha

1 reference

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/10200289

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Modular design of components of the operational RNA code for alanine in evolution

1 reference

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/10200289

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

DOI

10.1073/PNAS.96.8.4488

0 references

ADS bibcode

1999PNAS...96.4488R

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PMC publication ID

16359

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PubMed publication ID

10200289

0 references

ResearchGate publication ID

13098509

0 references

 

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