Author

Amandine Berthet

Gladstone InstitutesORCID 0000-0002-8529-6562Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Neuroscience· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Research Focus:drug response / drug discovery· 1 Organism:human· 1

Frequent Co-Authors

David A. AgardiD· 2 shared Jiahui TaoiD· 2 shared Lisa McConlogueiD· 2 shared Balazs G. Szoke· 1 shared Brian J. SpenceriD· 1 shared Carlos W. BertonciniiD· 1 shared Dale Schenk· 1 shared Daniel Schwizer· 1 shared

Activity by Year

2019-2021 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 45 mutual co-author links

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2 shared papersNeuroscience

David A. AgardORCID

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2 papers

Recent·Most cited

Hsp70 chaperone blocks α-synuclein oligomer formation via a novel engagement mechanism

Jiahui Tao, Amandine Berthet, Y. Rose Citron, Paraskevi L. Tsiolaki, Robert F. Stanley, Jason E. Gestwicki, David A. Agard, Lisa McConlogue

This study identifies a novel non-canonical mechanism by which Hsp70 blocks α-synuclein oligomer formation, independent of ATP and the typical substrate-binding cleft.

Journal of Biological Chemistry · Jan 1, 2021Peer-reviewedNeuroscience

Novel Small Molecules Targeting the Intrinsically Disordered Structural Ensemble of α-Synuclein Protect Against Diverse α-Synuclein Mediated Dysfunctions

Gergely Tóth, Thomas Neumann, Amandine Berthet, Eliezer Masliah, Brian J. Spencer, Jiahui Tao, Michael F. Jobling, Shyra J. Gardai, Carlos W. Bertoncini, Nunilo Cremades, Michael P. Bova, Stephen J. Ballaron, Xiao-Hua Chen, Wenxian Mao, Phuong Trang Nguyen, , Lisa McConlogue

This study identifies small molecules that target the intrinsically disordered ensemble of α-synuclein, showing they can inhibit misfolding, restore phagocytosis, and block cellular transmission of α-synuclein.

Scientific Reports · Nov 18, 2019Peer-reviewedNeuroscience