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- Currently displaying 841 - 860 of 1199 publications
The length distribution of frangible biofilaments.
Journal of Chemical Physics
(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
(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)
Oligomers of heat-shock proteins: Structures that don't imply function
(2015)
(doi: 10.48550/arxiv.1508.07924)
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)
Dynamics of protein aggregation and oligomer formation governed by secondary nucleation
J Chem Phys
(2015)
143
054901
(doi: 10.1063/1.4927655)
Force generation by the growth of amyloid aggregates
Proc Natl Acad Sci U S A
(2015)
112
9524
(doi: 10.1073/pnas.1417326112)
Molecular Rotors Provide Insights into Microscopic Structural Changes During Protein Aggregation.
The 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 and Disease
(2015)
6
e1820
(doi: 10.1038/cddis.2015.166)
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-CuII 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)
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 α-synuclein fibril formation.
Proc Natl Acad Sci U S A
(2015)
112
e1994
(doi: 10.1073/pnas.1421204112)
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.)
On-demand delivery of single DNA molecules using nanopipets
ACS nano
(2015)
9
3587
(doi: 10.1021/acsnano.5b00911)
