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dc.contributor.authorBarthelme, Dominik
dc.contributor.authorSauer, Robert T.
dc.date.accessioned2018-07-09T14:39:42Z
dc.date.available2018-07-09T14:39:42Z
dc.date.issued2015-12
dc.date.submitted2015-11
dc.identifier.issn0022-2836
dc.identifier.issn1089-8638
dc.identifier.urihttp://hdl.handle.net/1721.1/116854
dc.description.abstractThe AAA + Cdc48 ATPase (alias p97 or VCP) is a key player in multiple ubiquitin-dependent cell signaling, degradation, and quality control pathways. Central to these broad biological functions is the ability of Cdc48 to interact with a large number of adaptor proteins and to remodel macromolecular proteins and their complexes. Different models have been proposed to explain how Cdc48 might couple ATP hydrolysis to forcible unfolding, dissociation, or remodeling of cellular clients. In this review, we provide an overview of possible mechanisms for substrate unfolding/remodeling by this conserved and essential AAA + protein machine and their adaption and possible biological function throughout evolution. Keywords: AAA + machine; protein remodeling; human diseaseen_US
dc.description.sponsorshipNational Institutes of Health (U.S.) (Grant AI-16892)en_US
dc.publisherElsevieren_US
dc.relation.isversionofhttp://dx.doi.org/10.1016/J.JMB.2015.11.015en_US
dc.rightsCreative Commons Attribution-NonCommercial-NoDerivs Licenseen_US
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/en_US
dc.sourcePMCen_US
dc.titleOrigin and Functional Evolution of the Cdc48/p97/VCP AAA+ Protein Unfolding and Remodeling Machineen_US
dc.typeArticleen_US
dc.identifier.citationBarthelme, Dominik and Robert T. Sauer. “Origin and Functional Evolution of the Cdc48/p97/VCP AAA+ Protein Unfolding and Remodeling Machine.” Journal of Molecular Biology 428, 9 (May 2016): 1861–1869 © 2015 Elsevier Ltden_US
dc.contributor.departmentMassachusetts Institute of Technology. Department of Biologyen_US
dc.contributor.mitauthorBarthelme, Dominik
dc.contributor.mitauthorSauer, Robert T.
dc.relation.journalJournal of Molecular Biologyen_US
dc.eprint.versionAuthor's final manuscripten_US
dc.type.urihttp://purl.org/eprint/type/JournalArticleen_US
eprint.statushttp://purl.org/eprint/status/PeerRevieweden_US
dc.date.updated2018-07-09T12:52:52Z
dspace.orderedauthorsBarthelme, Dominik; Sauer, Robert T.en_US
dspace.embargo.termsNen_US
dc.identifier.orcidhttps://orcid.org/0000-0002-1719-5399
dspace.mitauthor.errortrue
mit.licensePUBLISHER_CCen_US


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