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- Currently displaying 741 - 760 of 1109 publications
A mechanistic model of tau amyloid aggregation based on direct observation of oligomers
Nature Communications
(2015)
6
7025
(doi: 10.1038/ncomms8025)
Preventing peptide and protein misbehavior.
Proceedings of the National Academy of Sciences of the United States of America
(2015)
112
5267
(doi: 10.1073/pnas.1505170112)
Structural characterization of toxic oligomers that are kinetically trapped during alpha-synuclein fibril formation
Proceedings of the National Academy of Sciences
(2015)
112
E1994
(doi: 10.1073/pnas.1421204112.)
Structural characterization of toxic oligomers that are kinetically trapped during α-synuclein fibril formation.
Proceedings of the National Academy of Sciences of the United States of America
(2015)
112
E1994
(doi: 10.1073/pnas.1421204112)
On-Demand Delivery of Single DNA Molecules Using Nanopipets
ACS nano
(2015)
9
3587
(doi: 10.1021/acsnano.5b00911)
Lipid peroxidation is essential for α-synuclein-induced cell death
Journal of Neurochemistry
(2015)
133
582
(doi: 10.1111/jnc.13024)
A molecular chaperone breaks the catalytic cycle that generates toxic Aβ oligomers
Nature Structural and Molecular Biology
(2015)
22
207
(doi: 10.1038/nsmb.2971)
Lipid peroxidation is essential for α-synuclein-induced cell death
Journal of neurochemistry
(2015)
133
582
(doi: 10.1111/jnc.13024)
A molecular chaperone breaks the catalytic cycle that generates toxic Aβ oligomers
Nature structural & molecular biology
(2015)
22
207
(doi: 10.1038/nsmb.2971)
Lipid vesicles trigger α-synuclein aggregation by stimulating primary nucleation.
Nature chemical biology
(2015)
11
229
(doi: 10.1038/nchembio.1750)
Single-Molecule FRET Reveals Hidden Complexity in a Protein Energy Landscape
Structure
(2015)
23
190
(doi: 10.1016/j.str.2014.10.023)
On the lag phase in amyloid fibril formation
Phys Chem Chem Phys
(2015)
17
7606
(doi: 10.1039/c4cp05563b)
Sizing and interactions of proteins under native conditions from microfluidic diffusion measurements: application to molecular chaperones and single-step immunoassay
PROTEIN SCIENCE
(2015)
24
3
New insights into the mechanism of amyloid formation by alpha-synuclein
EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS
(2015)
44
S100
Virtual-'Light-Sheet' Single-Molecule Localisation Microscopy Enables Quantitative Optical Sectioning for Super-Resolution Imaging
PloS one
(2015)
10
e0125438
(doi: 10.1371/journal.pone.0125438)
Lipid vesicles trigger α-synuclein aggregation by stimulating primary nucleation
EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS
(2015)
44
S101
Biophysical approaches for the study of interactions between molecular chaperones and protein aggregates.
Chemical communications (Cambridge, England)
(2015)
51
14425
(doi: 10.1039/c5cc03689e)
A microfluidic platform for quantitative measurements of effective protein charges and single ion binding in solution
Physical Chemistry Chemical Physics
(2015)
17
12161
(doi: 10.1039/c5cp00746a)