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- Currently displaying 1 - 20 of 2192 publications
Formation of distinct prion protein amyloid fibrils under identical experimental conditions
– Sci Rep
(2020)
10,
4572
(DOI: 10.1038/s41598-020-61663-2)
The N-terminal Acetylation of α-Synuclein Changes the Affinity for Lipid Membranes but not the Structural Properties of the Bound State
– Scientific Reports
(2020)
10,
204
(DOI: 10.1038/s41598-019-57023-4)
Single molecule secondary structure determination of proteins through infrared absorption nanospectroscopy.
– Nature Communications
(2020)
11,
2945
(DOI: 10.1038/s41467-020-16728-1)
Rapid Structural, Kinetic, and Immunochemical Analysis of Alpha-Synuclein Oligomers in Solution
– Nano letters
(2020)
acs.nanolett.0c03260
(DOI: 10.1021/acs.nanolett.0c03260)
Phase Transition and Crystallization Kinetics of a Supramolecular System in a Microfluidic Platform
– Chemistry of Materials
(2020)
32,
8342
The role of fibril structure and surface hydrophobicity in secondary nucleation of amyloid fibrils
– Proceedings of the National Academy of Sciences of the United States of America
(2020)
117,
25272
(DOI: 10.1073/pnas.2002956117)
Self-Replication of Prion Protein Fragment 89-230 Amyloid Fibrils Accelerated by Prion Protein Fragment 107-143 Aggregates
– International Journal of Molecular Sciences
(2020)
21,
7410
(DOI: 10.3390/ijms21197410)
An intrinsically disordered motif regulates the interaction between the p47 adaptor and the p97 AAA+ ATPase
– Proceedings of the National Academy of Sciences
(2020)
117,
202013920
(DOI: 10.1073/pnas.2013920117)
Direct measurement of lipid membrane disruption connects kinetics and toxicity of A beta 42 aggregation
– Nat Struct Mol Biol
(2020)
27,
886
(DOI: 10.1038/s41594-020-0471-z)
Biomolecular condensates undergo a generic shear-mediated liquid-to-solid transition
– Nat Nanotechnol
(2020)
15,
841
(DOI: 10.1038/s41565-020-0731-4)
A rationally designed bicyclic peptide remodels Aβ42 aggregation in vitro and reduces its toxicity in a worm model of Alzheimer's disease.
– Scientific reports
(2020)
10,
15280
(DOI: 10.1038/s41598-020-69626-3)
Biomimetic peptide self-assembly for functional materials
– Nature Reviews Chemistry
(2020)
1
(DOI: 10.1038/s41570-020-0215-y)
Thermodynamic and kinetic design principles for amyloid-aggregation inhibitors.
– Proceedings of the National Academy of Sciences of the United States of America
(2020)
117,
24251
(DOI: 10.1073/pnas.2006684117)
Probing the unfolded protein response in long-lived naked mole-rats.
– Biochemical and biophysical research communications
(2020)
529,
1151
(DOI: 10.1016/j.bbrc.2020.06.118)
SDS-induced multi-stage unfolding of a small globular protein through different denatured states revealed by single-molecule fluorescence
– Chemical Science
(2020)
11,
9141
(DOI: 10.1039/d0sc02100h)
A prion-like domain in ELF3 functions as a thermosensor inArabidopsis
– Nature
(2020)
585,
256
(DOI: 10.1038/s41586-020-2644-7)
Structural Characterization of Covalently Stabilized Human Cystatin C Oligomers.
– Int J Mol Sci
(2020)
21,
1
(DOI: 10.3390/ijms21165860)
Amelioration of aggregate cytotoxicity by catalytic conversion of protein oligomers into amyloid fibrils.
– Nanoscale
(2020)
12,
18663
(DOI: 10.1039/d0nr01481h)
Kinetic analysis reveals the rates and mechanisms of protein aggregation in a multicellular organism
(2020)
(DOI: 10.1101/2020.08.13.249862)
Trodusquemine displaces protein misfolded oligomers from cell membranes and abrogates their cytotoxicity through a generic mechanism.
– Communications biology
(2020)
3,
435
(DOI: 10.1038/s42003-020-01140-8)