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- Currently displaying 841 - 860 of 1233 publications
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)
Initiation of T cell signaling by CD45 segregation at 'close contacts'.
Nature immunology
(2016)
17
574
(doi: 10.1038/ni.3392)
Ca2+ is a key factor in α-synuclein-induced neurotoxicity
Journal of cell science
(2016)
129
1792
(doi: 10.1242/jcs.180737)
Quantitative thermophoretic study of disease-related protein aggregates
Scientific Reports
(2016)
6
22829
(doi: 10.1038/srep22829)
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 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)
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
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)
Oligomers of heat-shock proteins: Structures that don't imply function
(2016)
(doi: 10.48550/arxiv.1508.07924)
Single-Molecule Imaging of Individual Amyloid Protein Aggregates in Human Biofluids
ACS Chem Neurosci
(2016)
7
399
(doi: 10.1021/acschemneuro.5b00324)
Automated Ex Situ Assays of Amyloid Formation on a Microfluidic Platform.
Biophys J
(2016)
110
555
(doi: 10.1016/j.bpj.2015.11.3523)
Improved Photo Physical Properties of mEos3 for Single Molecule Tracking
Biophysical Journal
(2016)
110
485a
(doi: 10.1016/j.bpj.2015.11.2596)
Alpha-Synuclein Oligomers Interact with Metal Ions to Induce Oxidative Stress and Neuronal Death in Parkinson's Disease.
Antioxid Redox Signal
(2016)
24
376
(doi: 10.1089/ars.2015.6343)
Spearhead Nanometric Field-Effect Transistor Sensors for Single-Cell Analysis
ACS nano
(2016)
10
3214
(doi: 10.1021/acsnano.5b05211)
Combining Single-Molecule Techniques with Microfluidics for Protein Analysis
Biophysical Journal
(2016)
110
195A
(doi: 10.1016/j.bpj.2015.11.1086)
3D Super-Resolution Imaging of Unperturbed Cells
Biophysical Journal
(2016)
110
485A
(doi: 10.1016/j.bpj.2015.11.2595)