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- Currently displaying 1141 - 1160 of 2399 publications
Ca2+ is a key factor in α-synuclein-induced neurotoxicity.
Development (Cambridge, England)
(2016)
143
e1.1
(doi: 10.1242/dev.139345)
Amyloid fibrils as building blocks for natural and artificial functional materials
Advanced materials (Deerfield Beach, Fla.)
(2016)
28
6546
(doi: 10.1002/adma.201505961)
A Microfluidic Platform for Real-Time Detection and Quantification of Protein-Ligand Interactions.
Biophys J
(2016)
110
1957
(doi: 10.1016/j.bpj.2016.03.038)
Rational design of mutations that change the aggregation rate of a protein while maintaining its native structure and stability
Scientific Reports
(2016)
6
25559
(doi: 10.1038/srep25559)
Self-assembly of MPG1, a hydrophobin protein from the rice blast fungus that forms functional amyloid coatings, occurs by a surface-driven mechanism
Sci Rep
(2016)
6
25288
(doi: 10.1038/srep25288)
Electrostatically-guided inhibition of Curli amyloid nucleation by the CsgC-like family of chaperones
Scientific Reports
(2016)
6
24656
(doi: 10.1038/srep24656)
Structural characterization of the interaction of α-synuclein nascent chains with the ribosomal surface and trigger factor.
Proc Natl Acad Sci U S A
(2016)
113
5012
(doi: 10.1073/pnas.1519124113)
The S/T-Rich Motif in the DNAJB6 Chaperone Delays Polyglutamine Aggregation and the Onset of Disease in a Mouse Model.
Molecular Cell
(2016)
62
272
(doi: 10.1016/j.molcel.2016.03.017)
A transcriptional signature of Alzheimer's disease is associated with a metastable subproteome at risk for aggregation.
Proceedings of the National Academy of Sciences of the United States of America
(2016)
113
4753
(doi: 10.1073/pnas.1516604113)
A general reaction network unifies the aggregation behaviour of the A$\beta$42 peptide and its variants
(2016)
(doi: 10.48550/arxiv.1604.00828)
A general reaction network unifies the aggregation behaviour of the A$β$42 peptide and its variants
(2016)
(doi: 10.1039/C7SC00215G)
Analysis of the length distribution of amyloid fibrils by centrifugal sedimentation
Anal Biochem
(2016)
504
7
(doi: 10.1016/j.ab.2016.03.015)
Kinetic analysis reveals the diversity of microscopic mechanisms through which molecular chaperones suppress amyloid formation
Nature Communications
(2016)
7
10948
(doi: 10.1038/ncomms10948)
Identification and structural characterization of an intermediate in the folding of the measles virus X domain
Journal of Biological Chemistry
(2016)
291
10886
(doi: 10.1074/jbc.M116.721126)
Amyloid‑β and α‑Synuclein Decrease the Level of Metal-Catalyzed Reactive Oxygen Species by Radical Scavenging and Redox Silencing
J Am Chem Soc
(2016)
138
3966
(doi: 10.1021/jacs.5b13577)
Nanoscopic insights into seeding mechanisms and toxicity of α-synuclein species in neurons.
Proc Natl Acad Sci U S A
(2016)
113
3815
(doi: 10.1073/pnas.1516546113)
Quantitative thermophoretic study of disease-related protein aggregates
Scientific reports
(2016)
6
22829
(doi: 10.1038/srep22829)
Ca2+ is a key factor in α-synuclein-induced neurotoxicity.
Journal of Cell Science
(2016)
129
1792
(doi: 10.1242/jcs.180737)
Microfluidic Diffusion Viscometer for Rapid Analysis of Complex Solutions.
Analytical Chemistry
(2016)
88
3488
(doi: 10.1021/acs.analchem.5b02930)
An Environmentally Sensitive Fluorescent Dye as a Multidimensional Probe of Amyloid Formation
J Phys Chem B
(2016)
120
2087
(doi: 10.1021/acs.jpcb.5b09663)
