Cargando…
Recent structural insights into the mechanism of ClpP protease regulation by AAA+ chaperones and small molecules
ClpP is a highly conserved serine protease that is a critical enzyme in maintaining protein homeostasis and is an important drug target in pathogenic bacteria and various cancers. In its functional form, ClpP is a self-compartmentalizing protease composed of two stacked heptameric rings that allow p...
Autores principales: | Mabanglo, Mark F., Houry, Walid A. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Society for Biochemistry and Molecular Biology
2022
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9035409/ https://www.ncbi.nlm.nih.gov/pubmed/35245501 http://dx.doi.org/10.1016/j.jbc.2022.101781 |
Ejemplares similares
-
Cellular functions of the ClpP protease impacting bacterial virulence
por: Aljghami, Mazen E., et al.
Publicado: (2022) -
Structure, function, and substrates of Clp AAA+ protease systems in cyanobacteria, plastids, and apicoplasts: A comparative analysis
por: Bouchnak, Imen, et al.
Publicado: (2021) -
ClpP protease activation results from the reorganization of the electrostatic interaction networks at the entrance pores
por: Mabanglo, Mark F., et al.
Publicado: (2019) -
ClpP Protease, a Promising Antimicrobial Target
por: Moreno-Cinos, Carlos, et al.
Publicado: (2019) -
Insights to the Assembly of a Functionally Active
Leptospiral ClpP1P2 Protease Complex along with Its ATPase Chaperone
ClpX
por: Dhara, Anusua, et al.
Publicado: (2019)