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UnknownImmunofluorescent detection of protein CoAlation in mammalian cells under oxidative stress.
Not available
S-EPMC11463958 | biostudies-literature
UnknownProtein CoAlation: a redox-regulated protein modification by coenzyme A in mammalian cells.
Not available
S-EPMC5509381 | biostudies-literature
UnknownProfiling the Site of Protein CoAlation and Coenzyme A Stabilization Interactions.
Not available
S-EPMC9312308 | biostudies-literature
UnknownProtein CoAlation is regulated by and integrated with growth factor signalling and the cellular antioxidant response.
Not available
S-EPMC12752523 | biostudies-literature
UnknownProtein CoAlation and antioxidant function of coenzyme A in prokaryotic cells.
Not available
S-EPMC5989533 | biostudies-literature
UnknownGlyceraldehyde-3-phosphate dehydrogenase from Citrobacter sp. S-77 is post-translationally modified by CoA (protein CoAlation) under oxidative stress.
Not available
S-EPMC6325607 | biostudies-literature
UnknownStaphylococcus aureus Small RNAs Possess Dephospho-CoA 5'-Caps, but No CoAlation Marks.
Not available
S-EPMC9326634 | biostudies-literature
ProteomicsBacillus subtilis YtpP and thioredoxin A are new players in the CoA-mediated defense mechanism against cellular stress
Coenzyme A is an important cellular metabolite critical for metabolic processes and the regulation of gene expression. The recent discovery of its antioxidant role has highlighted its protective function that leads to the formation of a mixed-disulfide bond with protein cysteines, termed protein CoA...
ORGANISM(S): Bacillus subtilis subsp. subtilis str. L170 
2023-05-10 | PXD041347 | Pride
Bacillus megaterium Coenzyme a Bacillus subtilis Antioxidant Oxidative stress Mixed-disulfide Protein coalation Protein decoalation 
UnknownExtensive Anti-CoA Immunostaining in Alzheimer's Disease and Covalent Modification of Tau by a Key Cellular Metabolite Coenzyme A.
Not available
S-EPMC8554225 | biostudies-literature
ProteomicsProtein CoAlation on TXNRD2 regulates mitochondrial thioredoxin system to protect against ferroptosis
Cystine-xCT transporter-Glutathione (GSH)-GPX4 axis is the canonical pathway to protect against ferroptosis. While not required for ferroptosis-inducing compounds (FINs) targeting GPX4, FINs targeting the xCT transporter require mitochondria and its lipid peroxidation to trigger ferroptosis. However...
ORGANISM(S): Homo sapiens (Human) 
2025-07-05 | PXD062566 | Pride
Proteomics Coa Txnrd2 
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