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- Currently displaying 681 - 700 of 1104 publications
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'
– 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 Computational Biology
(2016)
12,
e1004756
(doi: 10.1371/journal.pcbi.1004756)
Consistent Treatment of Hydrophobicity in Protein Lattice Models Accounts for Cold Denaturation.
– Physical review letters
(2016)
116,
078101
Kinetic model of the aggregation of alpha-synuclein provides insights into prion-like spreading
– Proc Natl Acad Sci U S A
(2016)
113,
e1206
(doi: 10.1073/pnas.1524128113)
Neuroscience: An anticancer drug suppresses the primary nucleation reaction that initiates the production of the toxic Ab42 aggregates linked with Alzheimer's disease
– Sci Adv
(2016)
2,
e1501244
(doi: 10.1126/sciadv.1501244)
Single-Molecule Imaging of Individual Amyloid Protein Aggregates in Human Biofluids.
– ACS Chemical Neuroscience
(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)
Combining Single-Molecule Techniques with Microfluidics for Protein Analysis
– Biophysical Journal
(2016)
110,
195a
(doi: 10.1016/j.bpj.2015.11.1086)
Improved Photo Physical Properties of mEos3 for Single Molecule Tracking
– Biophysical Journal
(2016)
110,
485A
(doi: 10.1016/j.bpj.2015.11.2596)