The requirement for Cdc48/p97 in nuclear protein quality control degradation depends on the substrate and correlates with substrate insolubility

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The requirement for Cdc48/p97 in nuclear protein quality control degradation depends on the substrate and correlates with substrate insolubility is …
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scholarly articleQ13442814

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P356DOI10.1242/JCS.141838
P932PMC publication ID4004975
P698PubMed publication ID24569878
P5875ResearchGate publication ID260381110

P50authorRichard G GardnerQ38329148
P2093author name stringPamela S Gallagher
Sarah V Clowes Candadai
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Substrate recognition in nuclear protein quality control degradation is governed by exposed hydrophobicity that correlates with aggregation and insolubility.Q36647227
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The three-dimensional structure of a glutathione S-transferase from the mu gene class. Structural analysis of the binary complex of isoenzyme 3-3 and glutathione at 2.2-A resolutionQ38325077
Role of the ubiquitin-selective CDC48(UFD1/NPL4 )chaperone (segregase) in ERAD of OLE1 and other substratesQ39646650
Reversible Ponceau staining as a loading control alternative to actin in Western blotsQ39731848
Characterization of the aggregation-prevention activity of p97/valosin-containing proteinQ40043585
The ubiquitin-selective chaperone CDC-48/p97 links myosin assembly to human myopathyQ40157250
P4510describes a project that usesImageJQ1659584
P433issuePt 9
P407language of work or nameEnglishQ1860
P921main subjectcell biologyQ7141
quality controlQ827792
P304page(s)1980-91
P577publication date2014-05-01
P1433published inJournal of Cell ScienceQ1524177
P1476titleThe requirement for Cdc48/p97 in nuclear protein quality control degradation depends on the substrate and correlates with substrate insolubility
P478volume127