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- Currently displaying 581 - 600 of 1158 publications
Massively parallel C elegans tracking provides multi-dimensional fingerprints for phenotypic discovery
Journal of neuroscience methods
(2018)
306
57
Conserved S/T Residues of the Human Chaperone DNAJB6 Are Required for Effective Inhibition of Aβ42 Amyloid Fibril Formation.
Biochemistry
(2018)
57
4891
(doi: 10.1021/acs.biochem.8b00353)
O2‐02‐02: TARGETING AMYLOID FORMATION USING RATIONALLY DESIGNED ANTIBODIES
Alzheimer's & Dementia
(2018)
14
p611
(doi: 10.1016/j.jalz.2018.06.2646)
Fabrication of Scaffold-Based 3D Magnetic Nanowires for Domain Wall Applications
Nanomaterials (Basel, Switzerland)
(2018)
8
E483
(doi: 10.3390/nano8070483)
FRET-enhanced photostability allows improved single-molecule tracking of proteins and protein complexes in live mammalian cells.
Nature communications
(2018)
9
2520
(doi: 10.1038/s41467-018-04486-0)
Multistep Inhibition of α-Synuclein Aggregation and Toxicity in Vitro and in Vivo by Trodusquemine
ACS chemical biology
(2018)
13
2308
(doi: 10.1021/acschembio.8b00466)
Enhancing the Resolution of Micro Free Flow Electrophoresis through Spatially Controlled Sample Injection
Analytical Chemistry
(2018)
90
8998
(doi: 10.1021/acs.analchem.8b01205)
Identification and nanomechanical characterization of the fundamental single-strand protofilaments of amyloid α-synuclein fibrils.
Proc Natl Acad Sci U S A
(2018)
115
7230
(doi: 10.1073/pnas.1721220115)
Determination of Polypeptide Conformation with Nanoscale Resolution in Water
ACS nano
(2018)
12
6612
(doi: 10.1021/acsnano.8b01425)
Single-Molecule Characterization of the Interactions between Extracellular Chaperones and Toxic α-Synuclein Oligomers.
Cell Rep
(2018)
23
3492
(doi: 10.1016/j.celrep.2018.05.074)
Origin of metastable oligomers and their effects on amyloid fibril self- assembly
Chemical Science
(2018)
9
5937
(doi: 10.1039/c8sc01479e)
On the role of sidechain size and charge in the aggregation of Aβ42 with familial mutations.
Proc Natl Acad Sci U S A
(2018)
115
E5849
(doi: 10.1073/pnas.1803539115)
α-synuclein oligomers interact with ATP synthase and open the permeability transition pore in Parkinson's disease
Nature Communications
(2018)
9
2293
(doi: 10.1038/s41467-018-04422-2)
Kinetic Analysis of Amyloid Formation
Methods Mol Biol
(2018)
1779
181
(doi: 10.1007/978-1-4939-7816-8_12)
Budding-like division of all-aqueous emulsion droplets modulated by networks of protein nanofibrils
Nature communications
(2018)
9
2110
(doi: 10.1038/s41467-018-04510-3)
Cooperative Assembly of Hsp70 Subdomain Clusters.
Biochemistry
(2018)
57
3641
(doi: 10.1021/acs.biochem.8b00151)
Reaction rate theory for supramolecular kinetics: application to protein aggregation
Molecular Physics
(2018)
116
3055
C-terminal truncation of α-synuclein promotes amyloid fibril amplification at physiological pH
Chemical science
(2018)
9
5506
(doi: 10.1039/c8sc01109e)
Stochastic calculus of protein filament formation under spatial confinement
New Journal of Physics
(2018)
20
055007
(doi: 10.1088/1367-2630/aac0bc)
Rapid Growth of Acetylated Aβ(16–20) into Macroscopic Crystals
ACS Nano
(2018)
12
5408
(doi: 10.1021/acsnano.8b00448)