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- Currently displaying 1141 - 1160 of 2455 publications
Electrostatically-guided inhibition of Curli amyloid nucleation by the CsgC-like family of chaperones.
Sci Rep
(2016)
6
24656
(doi: 10.1038/srep24656)
Structural characterization of the interaction of α-synuclein nascent chains with the ribosomal surface and trigger factor
Proceedings of the National Academy of Sciences
(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$β$42 peptide and its variants
(2016)
(doi: 10.1039/C7SC00215G)
A general reaction network unifies the aggregation behaviour of the A$\beta$42 peptide and its variants
(2016)
(doi: 10.48550/arxiv.1604.00828)
Analysis of the length distribution of amyloid fibrils by centrifugal sedimentation.
Analytical biochemistry
(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)
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)
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)
Nanoscopic insights into seeding mechanisms and toxicity of α-synuclein species in neurons.
Proceedings of the National Academy of Sciences of the United States of America
(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.
Anal Chem
(2016)
88
3488
(doi: 10.1021/acs.analchem.5b02930)
An Environmentally Sensitive Fluorescent Dye as a Multidimensional Probe of Amyloid Formation
The Journal of Physical Chemistry B
(2016)
120
2087
(doi: 10.1021/acs.jpcb.5b09663)
Oligomers of Heat-Shock Proteins: Structures That Don't Imply Function
Plos Computational Biology
(2016)
12
e1004756
(doi: 10.1371/journal.pcbi.1004756)
A structural ensemble of a ribosome–nascent chain complex during cotranslational protein folding
Nature Structural and Molecular Biology
(2016)
23
278
(doi: 10.1038/nsmb.3182)
A Fragment-Based Method of Creating Small-Molecule Libraries to Target the Aggregation of Intrinsically Disordered Proteins
ACS Combinatorial Science
(2016)
18
144
(doi: 10.1021/acscombsci.5b00129)
Molecular Recognition by Templated Folding of an Intrinsically Disordered Protein.
Scientific reports
(2016)
6
21994
(doi: 10.1038/srep21994)
Kinetic model of the aggregation of alpha-synuclein provides insights into prion-like spreading.
Proceedings of the National Academy of Sciences of the United States of America
(2016)
113
E1206
(doi: 10.1073/pnas.1524128113)