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Co-Translational Protein Modification

Known as: co-translational modification, cotranslational modification, cotranslational protein modification 
The process of covalently altering one or more amino acids in a protein after translation has begun but before the protein has been released from the… Expand
National Institutes of Health

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Amino Acid Modification, Co-Translational

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
2016
2016
N-terminal acetylation promotes synaptonemal complex assembly in C. elegans.
N-terminal acetylation of the first two amino acids on proteins is a prevalent cotranslational modification. Despite its… Expand
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2014
2014
Arrest defective 1 regulates the oxidative stress response in human cells and mice by acetylating methionine sulfoxide reductase A
Methionine sulfoxide reductase A (MSRA) protects proteins from oxidation, and also helps remove reactive oxygen species (ROS) by… Expand
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2012
2012
Tyrosine Phosphorylation of the BRI1 Receptor Kinase Occurs via a Post-Translational Modification and is Activated by the Juxtamembrane Domain
In metazoans, receptor kinases control many essential processes related to growth and development and response to the environment… Expand
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2005
2005
Cloning, expression, characterization, and crystallization of a glutaminyl cyclase from human bone marrow: a single zinc metalloenzyme.
Glutaminyl cyclase (QC) catalyzes the N-terminal pyroglutamate formation of numerous hormones and peptides from their glutaminyl… Expand
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Highly Cited
1998
Highly Cited
1998
An ERp60-like protein from the filarial parasite Dirofilaria immitis has both transglutaminase and protein disulfide isomerase activity.
Transglutaminases (TGases; EC 2.3.2.13) are a family of enzymes that catalyze calcium-dependent covalent cross-linking of… Expand
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Highly Cited
1997
Highly Cited
1997
Autophosphorylation of the catalytic subunit of cAMP-dependent protein kinase in Escherichia coli.
When the catalytic (rC) subunit of cAMP-dependent protein kinase (cAPK) is expressed in Escherichia coli, it is… Expand
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Highly Cited
1996
Highly Cited
1996
A role for N-myristoylation in protein targeting: NADH-cytochrome b5 reductase requires myristic acid for association with outer mitochondrial but not ER membranes
N-myristoylation is a cotranslational modification involved in protein- protein interactions as well as in anchoring polypeptides… Expand
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1994
1994
Temperature-sensitive lesions in the capsid proteins of the rotavirus mutants tsF and tsG that affect virion assembly.
The SA11 rotavirus mutants tsF and tsG contain temperature sensitive (ts) lesions in the capsid proteins VP2 and VP6… Expand
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Highly Cited
1994
Highly Cited
1994
Identification of covalently bound amino-terminal myristic acid in endothelial nitric oxide synthase.
  • J. Liu, W. Sessa
  • The Journal of biological chemistry
  • 1994
    • Corpus ID: 23110258
Endothelial nitric oxide synthase (eNOS) is unique among the nitric oxide synthase family of proteins due to the presence of an N… Expand
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1992
1992
Autophosphorylation of the catalytic subunit of cAMP-dependent protein kinase.
The catalytic subunit of cAMP-dependent protein kinase contains two stable phosphorylation sites, Thr-197 and Ser-338 (Shoji, S… Expand
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