Common Mode of Remodeling AAA ATPases p97/CDC48 by Their Disassembling Cofactors ASPL/PUX1.
Sign Up to like & getrecommendations! Published in 2019 at "Structure"
DOI: 10.1016/j.str.2019.10.001
Abstract: The hexameric ring structure of the type II AAA+ ATPases is considered as stable and permanent. Recently, the UBX domain-containing cofactors Arabidopsis thaliana PUX1 and human alveolar soft part sarcoma locus (ASPL) were reported to… read more here.
Keywords: ubx domain; mode remodeling; common mode; pux1 ... See more keywords
AAA-ATPases in Protein Degradation
Sign Up to like & getrecommendations! Published in 2017 at "Frontiers in Molecular Biosciences"
DOI: 10.3389/fmolb.2017.00042
Abstract: Proteolytic machineries containing multisubunit protease complexes and AAA-ATPases play a key role in protein quality control and the regulation of protein homeostasis. In these protein degradation machineries, the proteolytically active sites are formed by either… read more here.
Keywords: aaa atpases; aaa; protein degradation; protease ... See more keywords
Shaping the Nascent Ribosome: AAA-ATPases in Eukaryotic Ribosome Biogenesis
Sign Up to like & getrecommendations! Published in 2019 at "Biomolecules"
DOI: 10.3390/biom9110715
Abstract: AAA-ATPases are molecular engines evolutionarily optimized for the remodeling of proteins and macromolecular assemblies. Three AAA-ATPases are currently known to be involved in the remodeling of the eukaryotic ribosome, a megadalton range ribonucleoprotein complex responsible… read more here.
Keywords: aaa atpases; ribosome; eukaryotic ribosome; ribosome biogenesis ... See more keywords