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- Currently displaying 1201 - 1220 of 2453 publications
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.
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.
Nat Commun
(2016)
7
10948
(doi: 10.1038/ncomms10948)
Identification and Structural Characterization of an Intermediate in the Folding of the Measles Virus X Domain*
The 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
Journal of the American Chemical Society
(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.
The Journal of Physical Chemistry B
(2016)
120
2087
(doi: 10.1021/acs.jpcb.5b09663)
A structural ensemble of a ribosome-nascent chain complex during cotranslational protein folding
Nature Structural & 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)
Oligomers of Heat-Shock Proteins: Structures That Don’t Imply Function
PLoS Comput Biol
(2016)
12
e1004756
(doi: 10.1371/journal.pcbi.1004756)
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
(2016)
113
e1206
(doi: 10.1073/pnas.1524128113)
Consistent Treatment of Hydrophobicity in Protein Lattice Models Accounts for Cold Denaturation
Physical review letters
(2016)
116
078101
Construction of homogeneous antibody-drug conjugates using site-selective protein chemistry.
Chemical Science
(2016)
7
2954
(doi: 10.1039/c6sc00170j)
Oligomers of heat-shock proteins: Structures that don't imply function
(2016)
(doi: 10.48550/arxiv.1508.07924)
An anticancer drug suppresses the primary nucleation reaction that initiates the production of the toxic Aβ42 aggregates linked with Alzheimer's disease
Science advances
(2016)
2
e1501244
(doi: 10.1126/sciadv.1501244)
Single-Molecule Imaging of Individual Amyloid Protein Aggregates in Human Biofluids
ACS Chem Neurosci
(2016)
7
399
(doi: 10.1021/acschemneuro.5b00324)