Existence of two forms of rat liver arginyl-tRNA synthetase suggests channeling of aminoacyl-tRNA for protein synthesis (Q33578233)

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English	Existence of two forms of rat liver arginyl-tRNA synthetase suggests channeling of aminoacyl-tRNA for protein synthesis	scientific article

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scholarly article

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Europe PubMed Central

PubMed publication ID

2187187

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28 July 2017

title

Existence of two forms of rat liver arginyl-tRNA synthetase suggests channeling of aminoacyl-tRNA for protein synthesis (English)

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PubMed publication ID

2187187

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28 July 2017

author name string

P Sivaram

series ordinal

1

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Europe PubMed Central

PubMed publication ID

2187187

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28 July 2017

M P Deutscher

series ordinal

2

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PubMed publication ID

2187187

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28 July 2017

language of work or name

English

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publication date

1 May 1990

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Europe PubMed Central

PubMed publication ID

2187187

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28 July 2017

number of pages

5

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published in

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

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Europe PubMed Central

PubMed publication ID

2187187

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28 July 2017

volume

87

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Europe PubMed Central

PubMed publication ID

2187187

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28 July 2017

issue

10

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Europe PubMed Central

PubMed publication ID

2187187

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28 July 2017

page(s)

3665-3669

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Europe PubMed Central

PubMed publication ID

2187187

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28 July 2017

cites work

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Preferential utilization of exogenously supplied leucine for protein synthesis in estradiol-induced and uninduced cockerel liver explants

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Analysis of the specific radioactivity of valine isolated from aminoacyl-transfer ribonucleic acid of rat liver

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Cytochalasin releases mRNA from the cytoskeletal framework and inhibits protein synthesis

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A basic NH2-terminal extension of rat liver arginyl-tRNA synthetase required for its association with high molecular weight complexes.

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The yeast VAS1 gene encodes both mitochondrial and cytoplasmic valyl-tRNA synthetases

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Purification and characterization of arginyl-tRNA-protein transferase from rabbit reticulocytes. Its involvement in post-translational modification and degradation of acidic NH2 termini substrates of the ubiquitin pathway

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Ubiquitin-mediated pathways for intracellular proteolysis

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

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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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Universality and structure of the N-end rule

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Interaction of aminoacyl-tRNA synthetases with ribosomes and ribosomal subunits

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Relationship of the pool of intracellular valine to protein synthesis and degradation in cultured cells.

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All factors required for protein synthesis are retained on heparin bound to Sepharose

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Characterization of postribosomal aminoacyl-tRNA synthetases in cultured Chinese hamster ovary cells

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

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Posttranslational NH2-Terminal Aminoacylation

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Purification of a low molecular weight form of rat liver arginyl-tRNA synthetase.

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31 October 2018

Methionyl-tRNA Synthetase from Sheep Mammary Gland. Purification of a Fully Active Monomeric Enzyme Derived from High-Molecular-Weight Complexes by Controlled Proteolysis

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Evidence for in vivo compartmentation of phenylalanyl-tRNA ligase in amphibian oocytes

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https://pubmed.ncbi.nlm.nih.gov/2187187

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Seven mammalian aminoacyl-tRNA synthetases associated within the same complex are functionally independent

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/2187187

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Molecular weights of mitochondrial and cytoplasmic aminoacyl-tRNA synthetases of beef liver and their complexes

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/2187187

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12 December 2020

based on heuristic

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

1 reference

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/2187187

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Multiple forms of arginyl- and lysyl-tRNA synthetases in rat liver: a re-evaluation

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/2187187

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Transfer RNA is required for conjugation of ubiquitin to selective substrates of the ubiquitin- and ATP-dependent proteolytic system

1 reference

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/2187187

retrieved

12 December 2020

based on heuristic

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Structural organization of the multienzyme complex of mammalian aminoacyl-tRNA synthetases

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/2187187

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

A role for lipids in the functional and structural properties of the rat liver aminoacyl-tRNA synthetase complex

1 reference

stated in

PubMed

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https://pubmed.ncbi.nlm.nih.gov/2187187

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12 December 2020

based on heuristic

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A novel role for aminoacyl-tRNA synthetases in the regulation of polypeptide chain initiation

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/2187187

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12 December 2020

based on heuristic

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The chicken progesterone receptor A and B isoforms are products of an alternate translation initiation event

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/2187187

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12 December 2020

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A SOLUBLE AMINO ACID-INCORPORATING SYSTEM FROM RAT LIVER

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/2187187

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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

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/2187187

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Complex of aminoacyl-transfer RNA synthetases

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/2187187

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Reactions at the 3' terminus of transfer ribonucleic acid. 3. Catalytic properties of two purified rabbit liver transfer ribonucleic acid nucleotidyl transferases

1 reference

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/2187187

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Binding of aminoacyl transfer ribonucleic acid synthetases to ribosomes from rabbit reticulocytes

1 reference

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/2187187

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Isolation and partial characterization of an aminoacyl-tRNA synthetase complex from rabbit reticulocytes

1 reference

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/2187187

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

DOI

10.1073/PNAS.87.10.3665

1 reference

stated in

Europe PubMed Central

PubMed publication ID

2187187

retrieved

28 July 2017

ADS bibcode

1990PNAS...87.3665S

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PMC publication ID

53963

1 reference

stated in

Europe PubMed Central

PubMed publication ID

2187187

retrieved

28 July 2017

PubMed publication ID

2187187

1 reference

stated in

Europe PubMed Central

PubMed publication ID

2187187

retrieved

28 July 2017

ResearchGate publication ID

20969243

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