Author

Federica Guarra

University of PaviaORCID 0000-0002-7301-3000Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Biochemistry· 1 Cancer Biology· 1 Cell Biology· 1

Signature Assays, Organisms & Methods

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Organism:human· 2 Research Focus:protein folding & dynamics· 2 Approach:statistical model· 2 Research Focus:cancer & tumor microenvironment· 1 Research Focus:cell signaling & trafficking· 1 Approach:deep learning· 1 Approach:experimental assay· 1 Approach:mechanistic / dynamical model· 1

Frequent Co-Authors

Giorgio ColomboiD· 3 shared Alessia Magro· 2 shared Andrea RasolaiD· 2 shared Claudio LaquatraiD· 2 shared Elisabetta MoroniiD· 2 shared Lavinia FerroneiD· 2 shared Andrea BattistoniiD· 1 shared Azam Roshani Dashtmian· 1 shared

Activity by Year

2025-2025 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 42 mutual co-author links

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3 shared papersCell Biology

Giorgio ColomboORCID

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3 papers

Recent·Most cited

Disulfide-mediated tetramerization of TRAP1 fosters its antioxidant and pro-neoplastic activities.

Fiorella Faienza, Claudio Laquatra, Matteo Castelli, Gianmarco Matrullo, Salvatore Rizza, Federica Guarra, Azam Roshani Dashtmian, Alessia Magro, Paola Giglio, Chiara Pecorari, Lavinia Ferrone, Elisabetta Moroni, Francesca Pacello, Andrea Battistoni, Giorgio Colombo, , Giuseppe Filomeni

This study shows TRAP1 forms redox-sensitive tetramers via disulfide bonds, which are critical for its antioxidant and pro-neoplastic functions in cancer cells.

Redox Biology · May 13, 2025Peer-reviewedCell Biology

How a pathogenic mutation impairs Hsp60 functional dynamics from monomeric to fully assembled states

Luca Torielli, Federica Guarra, Hao Shao, Jason E. Gestwicki, Stefano Artin Serapian, Giorgio Colombo

This study uses molecular dynamics simulations to show that the V72I mutation in Hsp60 disrupts allosteric communication, rigidifying its complexes and impairing function.

Nature Communications · Apr 3, 2025Peer-reviewedBiochemistry

Point mutations of the mitochondrial chaperone TRAP1 affect its functions and pro-neoplastic activity.

Claudio Laquatra, Alessia Magro, Federica Guarra, Matteo Lambrughi, Lavinia Ferrone, Giulio Fracasso, Melissa Bacchin, Martina La Spina, Elisabetta Moroni, Elena Papaleo, Giorgio Colombo, Andrea Rasola

This study examines how point mutations in TRAP1 affect its structure, function, and pro-neoplastic activity using molecular dynamics simulations and structural analysis.

Cell Death and Disease · Mar 12, 2025Peer-reviewedCancer Biology