Proteolytic stability and aggregation in a key metabolic enzyme of bacteria.
lac operon
protein aggregation
protein degradation
ssrA
β-galactosidase
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:
07 May 2024
07 May 2024
Historique:
medline:
29
4
2024
pubmed:
29
4
2024
entrez:
29
4
2024
Statut:
ppublish
Résumé
Proteins that are kinetically stable are thought to be less prone to both aggregation and proteolysis. We demonstrate that the classical
Identifiants
pubmed: 38683989
doi: 10.1073/pnas.2301458121
doi:
Substances chimiques
beta-Galactosidase
EC 3.2.1.23
Escherichia coli Proteins
0
Protein Aggregates
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Pagination
e2301458121Subventions
Organisme : HHS | NIH | National Institute of General Medical Sciences (NIGMS)
ID : R01GM120231
Organisme : HHS | NIH | National Institute of General Medical Sciences (NIGMS)
ID : R01GM148703
Déclaration de conflit d'intérêts
Competing interests statement:The authors declare no competing interest.