Proteolytic stability and aggregation in a key metabolic enzyme of bacteria.


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
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

e2301458121

Subventions

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.

Auteurs

Dan Pollack (D)

Department of Biology, Center for Genomics and Systems Biology, New York University, New York, NY 10003.

Takashi Nozoe (T)

Department of Basic Science, Graduate School of Arts and Sciences, The University of Tokyo, Tokyo 153-8902, Japan.
Research Center for Complex Systems Biology, The University of Tokyo, Tokyo 153-8902, Japan.
Universal Biology Institute, The University of Tokyo, Tokyo 113-0033, Japan.

Edo Kussell (E)

Department of Biology, Center for Genomics and Systems Biology, New York University, New York, NY 10003.
Department of Physics, New York University, New York, NY 10003.

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Classifications MeSH