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- Currently displaying 901 - 920 of 1256 publications
The length distribution of frangible biofilaments.
J Chem Phys
(2015)
143
164901
(doi: 10.1063/1.4933230)
Particle-based simulations of steady-state mass transport at high Péclet numbers
(2015)
(doi: 10.48550/arxiv.1510.05126)
The 2015 super-resolution microscopy roadmap
Journal of Physics D Applied Physics
(2015)
48
443001
Latent analysis of unmodified biomolecules and their complexes in solution with attomole detection sensitivity.
Nature chemistry
(2015)
7
802
(doi: 10.1038/nchem.2344)
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
Fast flow microfluidics and single-molecule fluorescence for the rapid characterization of α-synuclein oligomers.
Analytical chemistry
(2015)
87
8818
(doi: 10.1021/acs.analchem.5b01811)
Force generation by the growth of amyloid aggregates
Proc Natl Acad Sci U S A
(2015)
112
9524
(doi: 10.1073/pnas.1417326112)
Dynamics of protein aggregation and oligomer formation governed by secondary nucleation.
The Journal of Chemical Physics
(2015)
143
054901
(doi: 10.1063/1.4927655)
Molecular Rotors Provide Insights into Microscopic Structural Changes During Protein Aggregation.
Journal of Physical Chemistry B
(2015)
119
10170
(doi: 10.1021/acs.jpcb.5b05099)
Aggregated α-synuclein and complex I deficiency: exploration of their relationship in differentiated neurons.
Cell Death Dis
(2015)
6
e1820
(doi: 10.1038/cddis.2015.166)
Rapid sizing of proteins in complex solutions
EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS
(2015)
44
S49
Lipid vesicles trigger α-synuclein aggregation by stimulating primary nucleation
EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS
(2015)
44
S101
New insights into the mechanism of amyloid formation by alpha-synuclein
EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS
(2015)
44
S100
Kinetics of protein aggregation
EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS
(2015)
44
S98
Crucial role of non-specific interactions in amyloid nucleation
EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS
(2015)
44
S161
Intracellular oligomeric amyloid-beta rapidly regulates GluA1 subunit of AMPA receptor in the hippocampus
Scientific reports
(2015)
5
10934
(doi: 10.1038/srep10934)
Enzymatically Active Microgels from Self-Assembling Protein Nanofibrils for Microflow Chemistry
ACS Nano
(2015)
9
5772
(doi: 10.1021/acsnano.5b00061)
Neuronal Cx3cr1 Deficiency Protects against Amyloid β-Induced Neurotoxicity
PloS one
(2015)
10
e0127730
(doi: 10.1371/journal.pone.0127730)
Aggregation-Prone Amyloid-β⋅Cu(II) Species Formed on the Millisecond Timescale under Mildly Acidic Conditions.
ChemBioChem
(2015)
16
1293
(doi: 10.1002/cbic.201500080)
The Aβ40 and Aβ42 peptides self-assemble into separate homomolecular fibrils in binary mixtures but cross-react during primary nucleation
Chemical science
(2015)
6
4215
(doi: 10.1039/c4sc02517b)
