Discovery of Small-Molecule Autophagy Inhibitors by Disrupting the Protein-Protein Interactions Involving Autophagy-Related 5.
Autophagy
/ drug effects
Autophagy-Related Protein 12
/ antagonists & inhibitors
Autophagy-Related Protein 5
/ antagonists & inhibitors
Autophagy-Related Proteins
/ antagonists & inhibitors
Microtubule-Associated Proteins
/ metabolism
Models, Molecular
Protein Conformation
Multiprotein Complexes
/ antagonists & inhibitors
Antineoplastic Agents
/ chemistry
Humans
Animals
Journal
Journal of medicinal chemistry
ISSN: 1520-4804
Titre abrégé: J Med Chem
Pays: United States
ID NLM: 9716531
Informations de publication
Date de publication:
23 02 2023
23 02 2023
Historique:
pubmed:
8
2
2023
medline:
25
2
2023
entrez:
7
2
2023
Statut:
ppublish
Résumé
One possible strategy for modulating autophagy is to disrupt the critical protein-protein interactions (PPIs) formed during this process. Our attention is on the autophagy-related 12 (ATG12)-autophagy-related 5 (ATG5)-autophagy-related 16-like 1 (ATG16L1) heterotrimer complex, which is responsible for ATG8 translocation from ATG3 to phosphatidylethanolamine. In this work, we discovered a compound with an (
Identifiants
pubmed: 36749313
doi: 10.1021/acs.jmedchem.2c01233
doi:
Substances chimiques
Autophagy-Related Protein 12
0
Autophagy-Related Protein 5
0
Autophagy-Related Proteins
0
Microtubule-Associated Proteins
0
ATG16L1 protein, human
0
Multiprotein Complexes
0
Antineoplastic Agents
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM