The ER stress sensor PERK luminal domain functions as a molecular chaperone to interact with misfolded proteins
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Title
The ER stress sensor PERK luminal domain functions as a molecular chaperone to interact with misfolded proteins
Authors
Keywords
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Journal
Acta Crystallographica Section D-Structural Biology
Volume 72, Issue 12, Pages 1290-1297
Publisher
International Union of Crystallography (IUCr)
Online
2016-11-30
DOI
10.1107/s2059798316018064
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- (2015) Scott A. Oakes et al. Annual Review of Pathology-Mechanisms of Disease
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- (2011) Daniel R. Southworth et al. MOLECULAR CELL
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- (2011) P. Walter et al. SCIENCE
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- PHENIX: a comprehensive Python-based system for macromolecular structure solution
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- (2009) W. P. Cheng et al. EUROPEAN JOURNAL OF CLINICAL INVESTIGATION
- Substrate binding site flexibility of the small heat shock protein molecular chaperones
- (2009) N. Jaya et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
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- (2008) InKi Kim et al. JOURNAL OF BIOLOGICAL CHEMISTRY
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