Cryo-EM structure of a human prion fibril with a hydrophobic, protease-resistant core
Published 2020 View Full Article
- Home
- Publications
- Publication Search
- Publication Details
Title
Cryo-EM structure of a human prion fibril with a hydrophobic, protease-resistant core
Authors
Keywords
-
Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 27, Issue 5, Pages 417-423
Publisher
Springer Science and Business Media LLC
Online
2020-04-14
DOI
10.1038/s41594-020-0403-y
References
Ask authors/readers for more resources
Related references
Note: Only part of the references are listed.- Structural features distinguishing infectious ex vivo mammalian prions from non-infectious fibrillar assemblies generated in vitro
- (2019) Cassandra Terry et al. Scientific Reports
- Cryo-EM fibril structures from systemic AA amyloidosis reveal the species complementarity of pathological amyloids
- (2019) Falk Liberta et al. Nature Communications
- Novel tau filament fold in chronic traumatic encephalopathy encloses hydrophobic molecules
- (2019) Benjamin Falcon et al. NATURE
- Protein-Solvent Interfaces in Human Y145Stop Prion Protein Amyloid Fibrils Probed by Paramagnetic Solid-State NMR Spectroscopy
- (2018) Darryl Aucoin et al. JOURNAL OF STRUCTURAL BIOLOGY
- Sub-ångström cryo-EM structure of a prion protofibril reveals a polar clasp
- (2018) Marcus Gallagher-Jones et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Sub-ångström cryo-EM structure of a prion protofibril reveals a polar clasp
- (2018) Marcus Gallagher-Jones et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Structural basis for the complete resistance of the human prion protein mutant G127V to prion disease
- (2018) Zhen Zheng et al. Scientific Reports
- Structural attributes of mammalian prion infectivity: Insights from studies with synthetic prions
- (2018) Qiuye Li et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Structural Studies of Amyloid Fibrils by Paramagnetic Solid-State Nuclear Magnetic Resonance Spectroscopy
- (2018) Theint Theint et al. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
- New tools for automated high-resolution cryo-EM structure determination in RELION-3
- (2018) Jasenko Zivanov et al. eLife
- High-throughput screening and scale-up of cocrystals using resonant acoustic mixing
- (2017) Karthik Nagapudi et al. INTERNATIONAL JOURNAL OF PHARMACEUTICS
- Cryo-EM structures of tau filaments from Alzheimer’s disease
- (2017) Anthony W. P. Fitzpatrick et al. NATURE
- MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy
- (2017) Shawn Q Zheng et al. NATURE METHODS
- A bacterial global regulator forms a prion
- (2017) Andy H. Yuan et al. SCIENCE
- Toward the Atomic Structure of PrP Sc
- (2017) Jose A. Rodriguez et al. Cold Spring Harbor Perspectives in Biology
- Species-dependent structural polymorphism of Y145Stop prion protein amyloid revealed by solid-state NMR spectroscopy
- (2017) Theint Theint et al. Nature Communications
- Prion strains in mammals: Different conformations leading to disease
- (2017) Rodrigo Morales PLoS Pathogens
- Gctf: Real-time CTF determination and correction
- (2016) Kai Zhang JOURNAL OF STRUCTURAL BIOLOGY
- Amyloid fibrils from the N-terminal prion protein fragment are infectious
- (2016) Jin-Kyu Choi et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Ex vivomammalian prions are formed of paired double helical prion protein fibrils
- (2016) Cassandra Terry et al. Open Biology
- The Structural Architecture of an Infectious Mammalian Prion Using Electron Cryomicroscopy
- (2016) Ester Vázquez-Fernández et al. PLoS Pathogens
- Structural Studies of Truncated Forms of the Prion Protein PrP
- (2015) William Wan et al. BIOPHYSICAL JOURNAL
- A naturally occurring variant of the human prion protein completely prevents prion disease
- (2015) Emmanuel A. Asante et al. NATURE
- De novo generation of infectious prions with bacterially expressed recombinant prion protein
- (2013) Zhihong Zhang et al. FASEB JOURNAL
- Electron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM
- (2013) Xueming Li et al. NATURE METHODS
- Inherited Prion Disease A117V Is Not Simply a Proteinopathy but Produces Prions Transmissible to Transgenic Mice Expressing Homologous Prion Protein
- (2013) Emmanuel A. Asante et al. PLoS Pathogens
- High-resolution structure of infectious prion protein: the final frontier
- (2012) Rodrigo Diaz-Espinoza et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- REFMAC5 for the refinement of macromolecular crystal structures
- (2011) Garib N. Murshudov et al. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
- XDS
- (2010) Wolfgang Kabsch ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
- Features and development ofCoot
- (2010) P. Emsley et al. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
- PHENIX: a comprehensive Python-based system for macromolecular structure solution
- (2010) Paul D. Adams et al. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
- The hydrophobic core region governs mutant prion protein aggregation and intracellular retention
- (2010) Emiliano Biasini et al. BIOCHEMICAL JOURNAL
- PyRosetta: a script-based interface for implementing molecular modeling algorithms using Rosetta
- (2010) S. Chaudhury et al. BIOINFORMATICS
- Prion Diseases and Their Biochemical Mechanisms†
- (2009) Nathan J. Cobb et al. BIOCHEMISTRY
- Natural and synthetic prion structure from X-ray fiber diffraction
- (2009) H. Wille et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Core Structure of Amyloid Fibrils Formed by Residues 106–126 of the Human Prion Protein
- (2009) Patrick Walsh et al. STRUCTURE
- Ultrastructures and strain comparison of under-glycosylated scrapie prion fibrils
- (2008) Valerie L. Sim et al. NEUROBIOLOGY OF AGING
- Amyloid Fibrils of the HET-s(218-289) Prion Form a Solenoid with a Triangular Hydrophobic Core
- (2008) C. Wasmer et al. SCIENCE
Publish scientific posters with Peeref
Peeref publishes scientific posters from all research disciplines. Our Diamond Open Access policy means free access to content and no publication fees for authors.
Learn MoreAsk a Question. Answer a Question.
Quickly pose questions to the entire community. Debate answers and get clarity on the most important issues facing researchers.
Get Started