Arginyltransferase is an ATP-independent self-regulating enzyme that forms distinct functional complexes in vivo (Q34540685)

2 August 2017

title

Arginyltransferase is an ATP-independent self-regulating enzyme that forms distinct functional complexes in vivo (English)

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2 August 2017

7

Yuri I Wolf

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2 August 2017

Junling Wang

1

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2 August 2017

Xuemei Han

2

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2 August 2017

Sougata Saha

3

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2 August 2017

Tao Xu

4

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2 August 2017

Reena Rai

5

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2 August 2017

Fangliang Zhang

6

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2 August 2017

Alexey Wolfson

8

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2 August 2017

John R Yates

9

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2 August 2017

Anna Kashina

10

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2 August 2017

publication date

1 January 2011

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2 August 2017

published in

Chemistry and Biology

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2 August 2017

volume

18

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2 August 2017

issue

1

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2 August 2017

page(s)

121-130

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describes a project that uses

2 August 2017

ImageQuant

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11 June 2022

https://www.ebi.ac.uk/europepmc/webservices/rest/PMC3031169/fullTextXML

inferred from PubMed Central ID database lookup

cites work

Arginylation-dependent neural crest cell migration is essential for mouse development

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3031169

Identification of N-terminally arginylated proteins and peptides by mass spectrometry

7 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3031169

Arginyltransferase regulates alpha cardiac actin function, myofibril formation and contractility during heart development

7 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3031169

Global analysis of posttranslational protein arginylation

7 July 2018

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3031169

Post-translational arginylation of calreticulin: a new isospecies of calreticulin component of stress granules

7 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3031169

Molecular dissection of arginyltransferases guided by similarity to bacterial peptidoglycan synthases

7 July 2018

1 reference

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Arginylation of beta-actin regulates actin cytoskeleton and cell motility

7 July 2018

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RGS4 and RGS5 are in vivo substrates of the N-end rule pathway

7 July 2018

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A novel form of neurotensin post-translationally modified by arginylation

7 July 2018

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Identification of mammalian arginyltransferases that modify a specific subset of protein substrates

7 July 2018

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An essential role of N-terminal arginylation in cardiovascular development

7 July 2018

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RGS4 is arginylated and degraded by the N-end rule pathway in vitro

7 July 2018

1 reference

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Alternative splicing results in differential expression, activity, and localization of the two forms of arginyl-tRNA-protein transferase, a component of the N-end rule pathway

7 July 2018

1 reference

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N-terminal arginylation of sciatic nerve and brain proteins following injury.

7 July 2018

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Enzymatic modification of proteins. II. Purification and properties of the arginyl transfer ribonucleic acid-protein transferase from rabbit liver cytoplasm

7 July 2018

1 reference

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In vivo half-life of a protein is a function of its amino-terminal residue

7 July 2018

1 reference

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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

7 July 2018

1 reference

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Cloning and functional analysis of the arginyl-tRNA-protein transferase gene ATE1 of Saccharomyces cerevisiae

7 July 2018

1 reference

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Amino-terminal arginylation of chromosomal proteins by arginyl-tRNA.

7 July 2018

1 reference

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High resolution two-dimensional electrophoresis of proteins

7 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3031169

Arginyltransferase, its specificity, putative substrates, bidirectional promoter, and splicing-derived isoforms

7 July 2018

1 reference

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A SOLUBLE AMINO ACID-INCORPORATING SYSTEM FROM RAT LIVER

27 October 2018

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12 December 2020

A soluble amino acid incorporating system

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12 December 2020

Incorporation of arginine by a soluble system from sheep thyroid

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12 December 2020

Arginyl-tRNA transferase activity as a marker of cellular aging in peripheral rat tissues

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12 December 2020

Post-translational addition of an arginine moiety to acidic NH2 termini of proteins is required for their recognition by ubiquitin-protein ligase

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12 December 2020

N-terminal arginylation of proteins in explants of injured sciatic nerves and embryonic brains of rats

1 reference

12 December 2020

10.1016/J.CHEMBIOL.2010.10.016

Identifiers

DOI

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2 August 2017

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2 August 2017

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