Cargando…
Uncoupling of p97 ATPase activity has a dominant negative effect on protein extraction
p97 is a highly abundant, homohexameric AAA+ ATPase that performs a variety of essential cellular functions. Characterized as a ubiquitin-selective chaperone, p97 recognizes proteins conjugated to K48-linked polyubiquitin chains and promotes their removal from chromatin and other molecular complexes...
Autores principales: | Rycenga, Halley B., Wolfe, Kelly B., Yeh, Elizabeth S., Long, David T. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2019
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6637110/ https://www.ncbi.nlm.nih.gov/pubmed/31316150 http://dx.doi.org/10.1038/s41598-019-46949-4 |
Ejemplares similares
-
Toward an understanding of the Cdc48/p97 ATPase
por: Bodnar, Nicholas, et al.
Publicado: (2017) -
The AAA+ ATPase p97, a cellular multitool
por: Stach, Lasse, et al.
Publicado: (2017) -
The Role of the N-Domain in the ATPase Activity of the Mammalian AAA ATPase p97/VCP
por: Niwa, Hajime, et al.
Publicado: (2012) -
P97/VCP ATPase inhibitors can rescue p97 mutation-linked motor neuron degeneration
por: Wang, F, et al.
Publicado: (2022) -
Optimization of Phenyl Indole Inhibitors of the AAA+
ATPase p97
por: LaPorte, Matthew G., et al.
Publicado: (2018)