Partially Unfolded Forms of the Prion Protein Populated under Misfolding-promoting Conditions
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Title
Partially Unfolded Forms of the Prion Protein Populated under Misfolding-promoting Conditions
Authors
Keywords
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Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 290, Issue 42, Pages 25227-25240
Publisher
American Society for Biochemistry & Molecular Biology (ASBMB)
Online
2015-09-03
DOI
10.1074/jbc.m115.677575
References
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Note: Only part of the references are listed.- Structural Effects of Multiple Pathogenic Mutations Suggest a Model for the Initiation of Misfolding of the Prion Protein
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- (2012) John J. Skinner et al. PROTEIN SCIENCE
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- Prion disease susceptibility is affected by -structure folding propensity and local side-chain interactions in PrP
- (2010) M. Q. Khan et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Prion hypothesis: the end of the controversy?
- (2010) Claudio Soto TRENDS IN BIOCHEMICAL SCIENCES
- Prion Proteins with Pathogenic and Protective Mutations Show Similar Structure and Dynamics
- (2009) Sung-Hun Bae et al. BIOCHEMISTRY
- Folding kinetics of the human prion protein probed by temperature jump
- (2009) T. Hart et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
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