Towards a unifying mechanism for ClpB/Hsp104-mediated protein disaggregation and prion propagation.

No abstract is available for this paper.

• Publication year

  2010

• Venue

  Biochemistry and cell biology = Biochimie et biologie cellulaire

• Publication date

  2010-01-11

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1139/o09-118PMID 20130680
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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  2007cited by this paper
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  2007cited by this paper
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  2005cited by this paper
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  2005cited by this paper
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  2004cited by this paper
• Evidence for an Unfolding/Threading Mechanism for Protein Disaggregation by Saccharomyces cerevisiae Hsp104*

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• Dominant gain-of-function mutations in Hsp104p reveal crucial roles for the middle region.

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• Role of the processing pore of the ClpX AAA+ ATPase in the recognition and engagement of specific protein substrates.

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