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 921 - 940 of 1276 publications
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
Anal Chem
(2015)
87
8818
(doi: 10.1021/acs.analchem.5b01811)
Force generation by the growth of amyloid aggregates
Proceedings of the National Academy of Sciences
(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.
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 Dis
(2015)
6
e1820
(doi: 10.1038/cddis.2015.166)
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
New insights into the mechanism of amyloid formation by alpha-synuclein
EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS
(2015)
44
S100
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
Intracellular oligomeric amyloid-beta rapidly regulates GluA1 subunit of AMPA receptor in the hippocampus.
Sci Rep
(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⋅CuII Species Formed on the Millisecond Timescale under Mildly Acidic Conditions
Chembiochem : a European journal of chemical biology
(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.
Proc Natl Acad Sci U S A
(2015)
112
5267
(doi: 10.1073/pnas.1505170112)