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UnknownDynamic acylome reveals metabolite driven modifications in Syntrophomonas wolfei.
Not available
S-EPMC9676460 | biostudies-literature
UnknownLoss of the mitochondrial phosphate carrier SLC25A3 induces remodeling of the cardiac mitochondrial protein acylome.
Not available
S-EPMC8461815 | biostudies-literature
UnknownActivity-Based Acylome Profiling with <i>N</i>-(Cyanomethyl)-<i>N</i>-(phenylsulfonyl)amides for Targeted Lysine Acylation and Post-Translational Control of Protein Function in Cells.
Not available
S-EPMC11899832 | biostudies-literature
ProteomicsDynamic acylome reveals metabolite driven modifications in Syntrophomonas wolfei
Syntrophomonas wolfei is an anaerobic syntrophic microbe that degrades short-chain fatty acids to acetate, hydrogen, and/or formate. This thermodynamically unfavorable process proceeds through a series of reactive acyl-Coenzyme A species (RACS). In other prokaryotic and eukaryotic systems, the produ...
ORGANISM(S): Syntrophomonas Wolfei Subsp. Wolfei Str. Goettingen (ncbitaxon:335541) Syntrophomonas Wolfei Subsp. Methylbutyratica (ncbitaxon:378794) 
2022-06-25 | MSV000089730 | MassIVE
ProteomicsPrecision Chemistry and Activity-Based Proteomics for Posttranslational Control of Protein Function
Lysine acylations are ubiquitous and structurally diverse posttranslational modifications that vastly expand the functional heterogeneity of the human proteome. Hence, the targeted acylation of lysine residues has emerged as a strategic approach to exert biomimetic control over protein function. How...
ORGANISM(S): Homo sapiens (Human) 
2025-05-06 | PXD051414 | Pride
Retinoid metabolism. Posttranslational modifications Lysine conjugation Protein-rna interactions Chemoproteomics Activity-based protein profiling N-(cyanomethyl)-n-(phenylsulfonyl)amides 
ProteomicsDynamic acylome reveals metabolite driven modifications in Syntrophomonas wolfei
Syntrophomonas wolfei is an anaerobic syntrophic microbe that degrades short-chain fatty acids to acetate, hydrogen, and/or formate. This thermodynamically unfavorable process proceeds through a series of reactive acyl-Coenzyme A species (RACS). In other prokaryotic and eukaryotic systems, the produ...
ORGANISM(S): Syntrophomonas Wolfei 
PXD036088 | panorama
UnknownMetabolic alkene labeling and in vitro detection of histone acylation via the aqueous oxidative Heck reaction.
Not available
S-EPMC4871226 | biostudies-literature
UnknownQuantitative analysis of protein lipidation and acyl-CoAs reveals substrate preferences of the S-acylation machinery.
Not available
S-EPMC11322976 | biostudies-literature
ProteomicsBioorthogonal Click Chemistry for Antibody-Free Profiling of Acetylation, Propionylation, and Butyrylation in Pseudomonas aeruginosa and Methicillin-Resistant Staphylococcus aureus
Lysine acylation is a post-translational modification (PTM) conserved in all domains of life and is essential for regulating diverse biological processes. Traditional methods for investigating acylation rely on anti-acyl-lysine-antibodies, which are costly, time-consuming, and often exhibit variable...
ORGANISM(S): Pseudomonas aeruginosa (strain UCBPP-PA14) Staphylococcus aureus 
2026-06-11 | PXD072564 | Pride
Butyrylation Propionylation Posttranslational modifications Acetylation Bacterial acylation 
ProteomicsAn atlas of Arabidopsis protein S-Acylation reveals its widespread role in plant cell organisation of and function.
S-acylation is the addition of a fatty acid to a cysteine residue of a protein. While this modification may profoundly alter protein behaviour, its effects on the function of plant proteins remains poorly characterised, largely as a result to the lack of basic information regarding which proteins ar...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2022-06-26 | PXD031348 | Pride
Acylome Arabidopsis Cellulose synthesis 
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