Author

Marco Bardelli

Institute for Research in BiomedicineORCID 0000-0002-1501-9252Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Molecular Biology· 2

Signature Assays, Organisms & Methods

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Research Focus:drug response / drug discovery· 2 Approach:experimental assay· 2 Organism:mouse· 2 Assay:protein structure· 1

Frequent Co-Authors

Adriano AguzziiD· 2 shared Federica Mazzola· 2 shared Karl FrontzekiD· 2 shared Luca SimonelliiD· 2 shared Luca VaraniiD· 2 shared Mattia PedottiiD· 2 shared Simone HornemanniD· 2 shared Anna HenziiD· 1 shared

Activity by Year

2018-2022 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 45 mutual co-author links

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2 shared papersMolecular Biology

Adriano AguzziORCID

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2 papers

Recent·Most cited

A conformational switch controlling the toxicity of the prion protein

Karl Frontzek, Marco Bardelli, Assunta Senatore, Anna Henzi, Regina Reimann, Seden Bedir, Marika Marino, Rohanah Hussain, Simon Jurt, Georg Meisl, Mattia Pedotti, Federica Mazzola, Giuliano Siligardi, Oliver Zerbe, Marco Losa, , Adriano Aguzzi

This study identifies an H-latch conformational switch in PrPC that drives prion toxicity and shows that disrupting this switch can protect against prion-related neurodegeneration.

Nature Structural & Molecular Biology · Aug 1, 2022Peer-reviewedMolecular Biology

A bispecific immunotweezer prevents soluble PrP oligomers and abolishes prion toxicity

Marco Bardelli, Karl Frontzek, Luca Simonelli, Simone Hornemann, Mattia Pedotti, Federica Mazzola, Manfredi C. Carta, Valeria Eckhardt, Rocco D’Antuono, Tommaso Virgilio, Santiago González, Adriano Aguzzi, Luca Varani

This paper introduces a bispecific antibody that targets both the globular domain and flexible tail of PrP, preventing prion toxicity and oligomer formation.

PLoS Pathogens · Oct 1, 2018Peer-reviewedMolecular Biology