Cargando…
N-Terminal Coiled-Coil Structure of ATPase Subunits of 26S Proteasome Is Crucial for Proteasome Function
The proteasome is an essential proteolytic machine in eukaryotic cells, where it removes damaged proteins and regulates many cellular activities by degrading ubiquitinated proteins. Its heterohexameric AAA+ ATPase Rpt subunits play a central role in proteasome activity by the engagement of substrate...
Autores principales: | Inobe, Tomonao, Genmei, Reiko |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2015
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4514846/ https://www.ncbi.nlm.nih.gov/pubmed/26208326 http://dx.doi.org/10.1371/journal.pone.0134056 |
Ejemplares similares
-
Conformational switching in the coiled-coil domains of a proteasomal ATPase regulates substrate processing
por: Snoberger, Aaron, et al.
Publicado: (2018) -
Defining the geometry of the two-component proteasome degron
por: Inobe, Tomonao, et al.
Publicado: (2011) -
Substrate selection by the proteasome during degradation of protein complexes
por: Prakash, Sumit, et al.
Publicado: (2008) -
Genetic Alterations in Members of the Proteasome 26S Subunit, AAA-ATPase (PSMC) Gene Family in the Light of Proteasome Inhibitor Resistance in Multiple Myeloma
por: Haertle, Larissa, et al.
Publicado: (2023) -
N-Acyldopamine induces aggresome formation without proteasome inhibition and enhances protein aggregation via p62/SQSTM1 expression
por: Matsumoto, Gen, et al.
Publicado: (2018)