Tips on using this search form
- All search terms are case-insensitive
- If you specify more than one search option (e.g. you search for both "Authors" and "Paper title") then the publications returned will be those that match all of your search terms
- To reset the search form, click here
- Currently displaying 1241 - 1260 of 2489 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.
Nature communications
(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
J Am Chem Soc
(2016)
138
3966
(doi: 10.1021/jacs.5b13577)
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
Sci Rep
(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 Part B
(2016)
120
2087
(doi: 10.1021/acs.jpcb.5b09663)
Alpha-Synuclein Oligomers Interact with Metal Ions to Induce Oxidative Stress and Neuronal Death in Parkinson's Disease.
Antioxidants and Redox Signaling
(2016)
24
376
(doi: 10.1089/ars.2015.6343)
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)
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 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)
Structural Studies of the Oligomerization Process of Human Cystatin C Variants
Biophysical Journal
(2016)
110
26A
(doi: 10.1016/j.bpj.2015.11.205)
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)
Consistent Treatment of Hydrophobicity in Protein Lattice Models Accounts for Cold Denaturation.
Phys Rev Lett
(2016)
116
078101
Combining Single-Molecule Techniques with Microfluidics for Protein Analysis
Biophysical Journal
(2016)
110
195a
(doi: 10.1016/j.bpj.2015.11.1086)
Oligomers of heat-shock proteins: Structures that don't imply function
(2016)
(doi: 10.48550/arxiv.1508.07924)