A prion-like domain in Hsp42 drives chaperone-facilitated aggregation of misfolded proteins
Author:
Affiliation:
1. Zentrum für Molekulare Biologie der Universität Heidelberg (ZMBH), DKFZ-ZMBH Alliance, Heidelberg, Germany
2. Deutsches Krebsforschungszentrum (DKFZ), Heidelberg, Germany
Abstract
Funder
Universität Heidelberg
Verband der Chemischen Industrie
Boehringer Ingelheim Fonds
Deutsche Forschungsgemeinschaft
Publisher
Rockefeller University Press
Subject
Cell Biology
Link
http://rupress.org/jcb/article-pdf/217/4/1269/1376833/jcb_201708116.pdf
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3. The N-terminal arm of small heat shock proteins is important for both chaperone activity and substrate specificity;Basha;J. Biol. Chem.,2006
4. Cellular strategies of protein quality control;Chen;Cold Spring Harb. Perspect. Biol.,2011
5. Systemic control of protein synthesis through sequestration of translation and ribosome biogenesis factors during severe heat stress;Cherkasov;FEBS Lett.,2015
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