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- Currently displaying 861 - 880 of 1200 publications
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
(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 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)
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
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)
A high power-density, mediator-free, microfluidic biophotovoltaic device for cyanobacterial cells
Advanced Energy Materials
(2015)
5
(doi: 10.1002/aenm.201401299)
Kinetics of protein aggregation
EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS
(2015)
44
S98
SICM-Based Nanodelivery System for Local TRPV1 Stimulation
Biophysical Journal
(2015)
108
332a
(doi: 10.1016/j.bpj.2014.11.1808)
Biophysical approaches for the study of interactions between molecular chaperones and protein aggregates.
Chemical communications (Cambridge, England)
(2015)
51
14425
(doi: 10.1039/c5cc03689e)
Crucial role of non-specific interactions in amyloid nucleation
EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS
(2015)
44
S161
New insights into the mechanism of amyloid formation by alpha-synuclein
EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS
(2015)
44
S100
A microfluidic platform for quantitative measurements of effective protein charges and single ion binding in solution.
Phys Chem Chem Phys
(2015)
17
12161
(doi: 10.1039/c5cp00746a)
On the lag phase in amyloid fibril formation.
Phys Chem Chem Phys
(2015)
17
7606
(doi: 10.1039/c4cp05563b)
Lipid vesicles trigger α-synuclein aggregation by stimulating primary nucleation
Nature Chemical Biology
(2015)
11
229
(doi: 10.1038/nchembio.1750)