Journal article
Polypeptide transfer from Hsp40 to Hsp70 molecular chaperones
Trends in biochemical sciences (Amsterdam. Regular ed.), Vol.34(5), pp.230-233
05/2009
DOI: 10.1016/j.tibs.2008.12.009
PMCID: PMC4437460
PMID: 19359181
Abstract
Heat shock protein 40 (Hsp40) co-chaperones assist in cellular protein folding and degradation through the binding and delivery of non-native proteins to heat shock protein 70 (Hsp70). The mechanism for substrate transfer from Hsp40s to Hsp70 is unknown. Two recent studies provide new details that shed light on novel mechanisms for substrate recognition by Hsp40s and a common mechanism for polypeptide transfer to Hsp70.
Details
- Title: Subtitle
- Polypeptide transfer from Hsp40 to Hsp70 molecular chaperones
- Creators
- Daniel W Summers - Department of Cell and Developmental Biology, University of North Carolina at Chapel Hill, NC 27599-7090, USAPeter M DouglasCarlos H I RamosDouglas M Cyr
- Resource Type
- Journal article
- Publication Details
- Trends in biochemical sciences (Amsterdam. Regular ed.), Vol.34(5), pp.230-233
- DOI
- 10.1016/j.tibs.2008.12.009
- PMID
- 19359181
- PMCID
- PMC4437460
- NLM abbreviation
- Trends Biochem Sci
- ISSN
- 0968-0004
- eISSN
- 1362-4326
- Publisher
- England
- Grant note
- 5 T32 GM008581-09 / NIGMS NIH HHS R03 TW007437 / FIC NIH HHS T32 GM008581 / NIGMS NIH HHS R01 GM067785 / NIGMS NIH HHS 5 R01 GM067785-06 / NIGMS NIH HHS R01 GM056981 / NIGMS NIH HHS
- Language
- English
- Date published
- 05/2009
- Academic Unit
- Iowa Neuroscience Institute; Biology
- Record Identifier
- 9983991939602771
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