Protein Quality Control: Chaperones Culling Corrupt Conformations

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dc.contributor.authorMcClellan, Amie J.
dc.contributor.authorTam, Stephen
dc.contributor.authorKaganovich, Daniel
dc.contributor.authorFrydman, Judith
dc.date.accessioned2016-10-28T19:43:38Z
dc.date.available2016-10-28T19:43:38Z
dc.date.issued2005-08
dc.description.abstractAchieving the correct balance between folding and degradation of misfolded proteins is critical for cell viability. The importance of defining the mechanisms and factors that mediate cytoplasmic quality control is underscored by the growing list of diseases associated with protein misfolding and aggregation. Molecular chaperones assist protein folding and also facilitate degradation of misfolded polypeptides by the ubiquitin–proteasome system. Here we discuss emerging links between folding and degradation machineries and highlight challenges for future research.en_US
dc.identifier.citationNature Cell Biology. Aug2005, Vol. 7 Issue 8, p736-741. 6p. DOI: 10.1038/ncb0805-736en_US
dc.identifier.urihttp://hdl.handle.net/11209/10522
dc.language.isoenen_US
dc.publisherNature Publishing Groupen_US
dc.subjectProteinsen_US
dc.subjectCytoplasmen_US
dc.subjectProtoplasmen_US
dc.subjectMolecular chaperonesen_US
dc.subjectPeptide hormonesen_US
dc.subjectUbiquitinen_US
dc.subjectProteins -- Analysisen_US
dc.titleProtein Quality Control: Chaperones Culling Corrupt Conformationsen_US
dc.typeArticleen_US

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