Amino acid and protein specificity of protein fatty acylation in
C. elegans
branched-chain fatty acids
click chemistry
protein lipidation
proteomics
Journal
Proceedings of the National Academy of Sciences of the United States of America
ISSN: 1091-6490
Titre abrégé: Proc Natl Acad Sci U S A
Pays: United States
ID NLM: 7505876
Informations de publication
Date de publication:
30 Jan 2024
30 Jan 2024
Historique:
medline:
22
1
2024
pubmed:
22
1
2024
entrez:
22
1
2024
Statut:
ppublish
Résumé
Protein lipidation plays critical roles in regulating protein function and localization. However, the chemical diversity and specificity of fatty acyl group utilization have not been investigated using untargeted approaches, and it is unclear to what extent structures and biosynthetic origins of
Identifiants
pubmed: 38252833
doi: 10.1073/pnas.2307515121
doi:
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
e2307515121Subventions
Organisme : NIGMS NIH HHS
ID : R35 GM131877
Pays : United States
Organisme : NCI NIH HHS
ID : R01 CA240529
Pays : United States
Déclaration de conflit d'intérêts
Competing interests statement:H.L. is a founder of, consultant, and a stockholder for Sedec Therapeutics. F.C.S. is a founder of, consultant, and a stockholder for Ascribe Bioscience and Holoclara Inc.