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- Currently displaying 801 - 820 of 1199 publications
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.
Biophysical journal
(2016)
110
1957
(doi: 10.1016/j.bpj.2016.03.038)
Self-assembly of MPG1, a hydrophobin protein from the rice blast fungus that forms functional amyloid coatings, occurs by a surface-driven mechanism.
Scientific Reports
(2016)
6
25288
(doi: 10.1038/srep25288)
PSD95 nanoclusters are postsynaptic building blocks in hippocampus circuits.
Sci Rep
(2016)
6
24626
(doi: 10.1038/srep24626)
Electrostatically-guided inhibition of Curli amyloid nucleation by the CsgC-like family of chaperones.
Sci Rep
(2016)
6
24656
(doi: 10.1038/srep24656)
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 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)
Initiation of T cell signaling by CD45 segregation at 'close contacts'.
Nat Immunol
(2016)
17
574
(doi: 10.1038/ni.3392)
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)
Oligomers of Heat-Shock Proteins: Structures That Don't Imply Function.
PLOS Computational Biology
(2016)
12
e1004756
(doi: 10.1371/journal.pcbi.1004756)
A Fragment-Based Method of Creating Small-Molecule Libraries to Target the Aggregation of Intrinsically Disordered Proteins.
ACS Comb Sci
(2016)
18
144
(doi: 10.1021/acscombsci.5b00129)
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)
Single-Molecule Imaging of Individual Amyloid Protein Aggregates in Human Biofluids.
ACS Chem Neurosci
(2016)
7
399
(doi: 10.1021/acschemneuro.5b00324)