Publications
Systematic Development of Small Molecules to Inhibit Specific Microscopic Steps of Amyloid-Beta42 Aggregation in Alzheimer's Disease
– Biophysical Journal
(2018)
114,
225a
(DOI: 10.1016/j.bpj.2017.11.1253)
Probing the Interaction of ABETA42 Amyloid Species with an Aggregation Suppressor Molecule by Infrared Nanospectroscopy
– Biophysical Journal
(2018)
114,
224a
(DOI: 10.1016/j.bpj.2017.11.1246)
Modulating Amyloid-Beta Aggregation to Reduce the Toxicity of its Oligomeric Aggregates
– Biophysical Journal
(2018)
114,
430a
(DOI: 10.1016/j.bpj.2017.11.2382)
Monomeric and fibrillar α-synuclein exert opposite effects on the catalytic cycle that promotes the proliferation of Aβ42 aggregates.
– Proceedings of the National Academy of Sciences of the United States of America
(2017)
114,
8005
(DOI: 10.1073/pnas.1700239114)
Attenuating the Toxicity of Amyloid-Beta Aggregation with Specific Species
– Biophysical Journal
(2017)
112,
494A
(DOI: 10.1016/j.bpj.2016.11.2673)
Systematic development of small molecules to inhibit specific microscopic steps of Aβ42 aggregation in Alzheimer’s disease
– Proceedings of the National Academy of Sciences
(2016)
114,
E200
(DOI: 10.1073/pnas.1615613114)
A Fragment-Based Method of Creating Small-Molecule Libraries to Target the Aggregation of Intrinsically Disordered Proteins
– ACS combinatorial science
(2016)
18,
144
(DOI: 10.1021/acscombsci.5b00129)
An anticancer drug suppresses the primary nucleation reaction that initiates the production of the toxic Aβ42 aggregates linked with Alzheimer's disease.
– Sci Adv
(2016)
2,
e1501244
(DOI: 10.1126/sciadv.1501244)
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