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  One domain fits all: Using disordered regions to sequester misfolded proteins.

Boczek, E., & Alberti, S. (2018). One domain fits all: Using disordered regions to sequester misfolded proteins. The Journal of cell biology, 217(4), 1173-1175. doi:10.1083/jcb.201803015.

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Item Permalink: https://hdl.handle.net/21.11116/0000-0003-F5AD-6 Version Permalink: https://hdl.handle.net/21.11116/0000-0003-F5AE-5
Genre: Journal Article

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 Creators:
Boczek, Edgar1, Author           
Alberti, Simon1, Author           
Affiliations:
1Max Planck Institute for Molecular Cell Biology and Genetics, Max Planck Society, ou_2340692              

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 Abstract: Small heat shock proteins (sHsps) are adenosine triphosphate-independent chaperones that protect cells from misfolded proteins. In this issue, Grousl et al. (2018.J. Cell Biol.https://doi.org/10.1083/jcb.201708116) show that the yeast sHsp Hsp42 uses a prion-like intrinsically disordered domain to bind and sequester misfolded proteins in protein deposition sites.

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 Dates: 2018-04-02
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: DOI: 10.1083/jcb.201803015
Other: cbg-7099
PMID: 29523584
 Degree: -

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Title: The Journal of cell biology
  Other : J Cell Biol
Source Genre: Journal
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Publ. Info: -
Pages: - Volume / Issue: 217 (4) Sequence Number: - Start / End Page: 1173 - 1175 Identifier: -