Probing the mechanism of inhibition of amyloid-β(1–42)–induced neurotoxicity by the chaperonin GroEL
Published 2018 View Full Article
- Home
- Publications
- Publication Search
- Publication Details
Title
Probing the mechanism of inhibition of amyloid-β(1–42)–induced neurotoxicity by the chaperonin GroEL
Authors
Keywords
-
Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 115, Issue 51, Pages E11924-E11932
Publisher
Proceedings of the National Academy of Sciences
Online
2018-12-04
DOI
10.1073/pnas.1817477115
References
Ask authors/readers for more resources
Related references
Note: Only part of the references are listed.- Chaperonin GroEL accelerates protofibril formation and decorates fibrils of the Het-s prion protein
- (2017) Marielle A. Wälti et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Oligomerization of the tetramerization domain of p53 probed by two- and three-color single-molecule FRET
- (2017) Hoi Sung Chung et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Sparse multidimensional iterative lineshape-enhanced (SMILE) reconstruction of both non-uniformly sampled and conventional NMR data
- (2016) Jinfa Ying et al. JOURNAL OF BIOMOLECULAR NMR
- Kinetic analysis reveals the diversity of microscopic mechanisms through which molecular chaperones suppress amyloid formation
- (2016) Paolo Arosio et al. Nature Communications
- Solution NMR Studies of Recombinant Aβ(1-42): From the Presence of a Micellar Entity to Residual β-Sheet Structure in the Soluble Species
- (2015) Marielle Aulikki Wälti et al. CHEMBIOCHEM
- Crystal structure of the human mitochondrial chaperonin symmetrical football complex
- (2015) Shahar Nisemblat et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- The cell biology of prion-like spread of protein aggregates: mechanisms and implication in neurodegeneration
- (2015) Maddalena Costanzo et al. BIOCHEMICAL JOURNAL
- Contribution of Specific Residues of the β-Solenoid Fold to HET-s Prion Function, Amyloid Structure and Stability
- (2014) Asen Daskalov et al. PLoS Pathogens
- Probing the transient dark state of substrate binding to GroEL by relaxation-based solution NMR
- (2013) D. S. Libich et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Measurement of 15N relaxation rates in perdeuterated proteins by TROSY-based methods
- (2012) Nils-Alexander Lakomek et al. JOURNAL OF BIOMOLECULAR NMR
- Atomic-resolution dynamics on the surface of amyloid-β protofibrils probed by solution NMR
- (2011) Nicolas L. Fawzi et al. NATURE
- Molecular chaperones in protein folding and proteostasis
- (2011) F. Ulrich Hartl et al. NATURE
- Kinetics of Amyloid β Monomer-to-Oligomer Exchange by NMR Relaxation
- (2010) Nicolas L. Fawzi et al. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
- Studying the effects of chaperones on amyloid fibril formation
- (2010) Hong Zhang et al. METHODS
- Early deficits in synaptic mitochondria in an Alzheimer's disease mouse model
- (2010) H. Du et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Biology of Amyloid: Structure, Function, and Regulation
- (2010) Jason Greenwald et al. STRUCTURE
- Experimental determination of upper bound for transition path times in protein folding from single-molecule photon-by-photon trajectories
- (2009) H. S. Chung et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Setting the chaperonin timer: The effects of K+ and substrate protein on ATP hydrolysis
- (2008) J. P. Grason et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Adapting Proteostasis for Disease Intervention
- (2008) William E. Balch et al. SCIENCE
Add your recorded webinar
Do you already have a recorded webinar? Grow your audience and get more views by easily listing your recording on Peeref.
Upload NowAsk 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