Molecular mechanisms of protein aggregation from global fitting of kinetic models
Published 2016 View Full Article
- Home
- Publications
- Publication Search
- Publication Details
Title
Molecular mechanisms of protein aggregation from global fitting of kinetic models
Authors
Keywords
-
Journal
Nature Protocols
Volume 11, Issue 2, Pages 252-272
Publisher
Springer Nature
Online
2016-01-08
DOI
10.1038/nprot.2016.010
References
Ask authors/readers for more resources
Related references
Note: Only part of the references are listed.- A molecular chaperone breaks the catalytic cycle that generates toxic Aβ oligomers
- (2015) Samuel I A Cohen et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- The physical basis of protein misfolding disorders
- (2015) Tuomas P. J. Knowles et al. PHYSICS TODAY
- Preventing peptide and protein misbehavior: Fig. 1.
- (2015) Paolo Arosio et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Zinc as chaperone-mimicking agent for retardation of amyloid β peptide fibril formation
- (2015) Axel Abelein et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- A molecular chaperone breaks the catalytic cycle that generates toxic Aβ oligomers
- (2015) Samuel I A Cohen et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Role of filament annealing in the kinetics and thermodynamics of nucleated polymerization
- (2014) Thomas C. T. Michaels et al. JOURNAL OF CHEMICAL PHYSICS
- Differences in nucleation behavior underlie the contrasting aggregation kinetics of the Aβ40 and Aβ42 peptides
- (2014) Georg Meisl et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Chemical kinetics for drug discovery to combat protein aggregation diseases
- (2014) Paolo Arosio et al. TRENDS IN PHARMACOLOGICAL SCIENCES
- Quantification of the Concentration of Aβ42 Propagons during the Lag Phase by an Amyloid Chain Reaction Assay
- (2013) Paolo Arosio et al. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
- Proliferation of amyloid- 42 aggregates occurs through a secondary nucleation mechanism
- (2013) S. I. A. Cohen et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Role of Aromatic Side Chains in Amyloid β-Protein Aggregation
- (2012) Risto Cukalevski et al. ACS Chemical Neuroscience
- Direct Observation of the Interconversion of Normal and Toxic Forms of α-Synuclein
- (2012) Nunilo Cremades et al. CELL
- From Macroscopic Measurements to Microscopic Mechanisms of Protein Aggregation
- (2012) Samuel I.A. Cohen et al. JOURNAL OF MOLECULAR BIOLOGY
- Nucleated polymerization with secondary pathways. II. Determination of self-consistent solutions to growth processes described by non-linear master equations
- (2011) Samuel I. A. Cohen et al. JOURNAL OF CHEMICAL PHYSICS
- Nucleated polymerization with secondary pathways. I. Time evolution of the principal moments
- (2011) Samuel I. A. Cohen et al. JOURNAL OF CHEMICAL PHYSICS
- Protein aggregation diseases: pathogenicity and therapeutic perspectives
- (2010) Adriano Aguzzi et al. NATURE REVIEWS DRUG DISCOVERY
- Amyloid β-Protein Aggregation Produces Highly Reproducible Kinetic Data and Occurs by a Two-Phase Process
- (2009) Erik Hellstrand et al. ACS Chemical Neuroscience
- A facile method for expression and purification of the Alzheimer’s disease-associated amyloid β-peptide
- (2009) Dominic M. Walsh et al. FEBS Journal
- The Recombinant Amyloid-β Peptide Aβ1–42 Aggregates Faster and Is More Neurotoxic than Synthetic Aβ1–42
- (2009) Verena H. Finder et al. JOURNAL OF MOLECULAR BIOLOGY
- Amyloid seeds formed by cellular uptake, concentration, and aggregation of the amyloid-beta peptide
- (2009) X. Hu et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- An Analytical Solution to the Kinetics of Breakable Filament Assembly
- (2009) T. P. J. Knowles et al. SCIENCE
Find the ideal target journal for your manuscript
Explore over 38,000 international journals covering a vast array of academic fields.
SearchAsk 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