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- Currently displaying 721 - 740 of 1100 publications
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
– Proceedings of the National Academy of Sciences
(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 Dis
(2015)
6,
e1820
(doi: 10.1038/cddis.2015.166)
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
(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
– Chem Sci
(2015)
6,
4215
(doi: 10.1039/c4sc02517b)
A mechanistic model of tau amyloid aggregation based on direct observation of oligomers
– Nat Commun
(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)
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.)
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)
On-demand delivery of single DNA molecules using nanopipets
– ACS nano
(2015)
9,
3587
(doi: 10.1021/acsnano.5b00911)
Lipid peroxidation is essential for α-synuclein-induced cell death
– Journal of Neurochemistry
(2015)
133,
582
(doi: 10.1111/jnc.13024)
A molecular chaperone breaks the catalytic cycle that generates toxic Aβ oligomers.
– Nature Structural and Molecular Biology
(2015)
22,
207
(doi: 10.1038/nsmb.2971)
Lipid peroxidation is essential for α‐synuclein‐induced cell death
– J Neurochem
(2015)
133,
582
(doi: 10.1111/jnc.13024)
The physical basis of protein misfolding disorders
– Physics Today
(2015)
68,
36
(doi: 10.1063/pt.3.2719)
A molecular chaperone breaks the catalytic cycle that generates toxic Aβ oligomers.
– Nature Structural & Molecular Biology
(2015)
22,
207
(doi: 10.1038/nsmb.2971)