Author

Federica Mazzola

Institute for Research in Biomedicine

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Molecular Biology· 2 Neuroscience· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Organism:mouse· 3 Research Focus:drug response / drug discovery· 2 Assay:protein structure· 2 Research Focus:cell-cell communication· 1 Research Focus:differential expression· 1 Research Focus:protein structure prediction· 1

Frequent Co-Authors

Adriano AguzziiD· 3 shared Karl FrontzekiD· 3 shared Luca VaraniiD· 3 shared Simone HornemanniD· 3 shared Luca SimonelliiD· 2 shared Marco BardelliiD· 2 shared Mattia PedottiiD· 2 shared Alexander SchwarziD· 1 shared

Activity by Year

2018-2022 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 36 mutual co-author links

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3 shared papersMolecular Biology

Adriano AguzziORCID

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Author profile →

3 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

Ligands binding to the cellular prion protein induce its protective proteolytic release with therapeutic potential in neurodegenerative proteinopathies

Luise Linsenmeier, Behnam Mohammadi, Mohsin Shafiq, Karl Frontzek, Julia Bär, Amulya Nidhi Shrivastava, Markus Daμμe, Feizhi Song, Alexander Schwarz, Stefano Da Vela, Tania Massignan, Sebastian Jung, Angela da Silva Correia, Matthias Schmitz, Berta Puig, , Markus Glatzel

The paper shows that ligands binding to PrPC induce its proteolytic release, which has neuroprotective effects, and identifies mechanisms and exceptions in this process.

Science Advances · Nov 24, 2021Peer-reviewedNeuroscience

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