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ATE1 gene

Known as: ARGINYLTRANSFERASE 1, ATE1 
National Institutes of Health

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Related topics

1 relation
Arginyltransferase

Papers overview

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Highly Cited
2014
Highly Cited
2014
Arginyltransferase ATE1 catalyzes midchain arginylation of proteins at side chain carboxylates in vivo.
2014
2014
Loss of ATE1-mediated arginylation leads to impaired platelet myosin phosphorylation, clot retraction, and in vivo thrombosis formation
Protein arginylation by arginyl–transfer RNA protein transferase (ATE1) is emerging as a regulator protein function that is… 
2012
2012
Small molecule inhibitors of arginyltransferase regulate arginylation-dependent protein degradation, cell motility, and angiogenesis.
2012
2012
Arginylation regulates myofibrils to maintain heart function and prevent dilated cardiomyopathy.
Highly Cited
2011
Highly Cited
2011
Arginyltransferase is an ATP-independent self-regulating enzyme that forms distinct functional complexes in vivo.
Highly Cited
2009
Highly Cited
2009
Ablation of Arginylation in the Mouse N-End Rule Pathway: Loss of Fat, Higher Metabolic Rate, Damaged Spermatogenesis, and Neurological Perturbations
In the N-end rule pathway of protein degradation, the destabilizing activity of N-terminal Asp, Glu or (oxidized) Cys residues… 
2006
2006
Molecular dissection of arginyltransferases guided by similarity to bacterial peptidoglycan synthases
Post‐translational protein arginylation is essential for cardiovascular development and angiogenesis in mice and is mediated by… 
Highly Cited
2005
Highly Cited
2005
RGS4 and RGS5 are in vivo substrates of the N-end rule pathway.
The ATE1-encoded Arg-transferase mediates conjugation of Arg to N-terminal Asp, Glu, and Cys of certain eukaryotic proteins… 
Highly Cited
1999
Highly Cited
1999
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
ABSTRACT The N-end rule relates the in vivo half-life of a protein to the identity of its N-terminal residue. The underlying… 
Highly Cited
1990
Highly Cited
1990
Cloning and functional analysis of the arginyl-tRNA-protein transferase gene ATE1 of Saccharomyces cerevisiae.
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