Mauro Salvi

Associate Professor

Italy

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About

Mauro Salvi is an Associate Professor at Mauro Salvi, Italy. His research focuses on protein kinases, post-translational modifications, and their implications in disease models, notably cystic fibrosis and cancer. Recent articles by Professor Salvi delve into the roles of FAM20C and CK2, exploring substrate recognition, SUMOylation, and ubiquitination mechanisms.

Articles (15)

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2025

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2025

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2024

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2024

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2023

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2022

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2022

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2022

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2022

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2021

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2021

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2021

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2021

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2021

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2021

Collaborators (6)

David R. Spring

University of Cambridge

UNITED KINGDOM

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Lorenzo A. Pinna

Professor emeritus

University of Padova

ITALY

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Maria Ruzzene

University of Padova

ITALY

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Andrea Rasola

Associate Professor

University of Padova

ITALY

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Tsuyoshi Hirota

Nagoya University

JAPAN

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Marko Hyvönen

University of Cambridge

UNITED KINGDOM

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Mauro Salvi

Research Interests

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Articles (15)

Past, Present and Future of Protein Kinase CK2 Research

Protein kinase FAM20C—when subcellular localization matters

SUMOylation Inhibition Enhances Protein Transcription under CMV Promoter: A Lesson from a Study with the F508del-CFTR Mutant

Targeting ubiquitination machinery in cystic fibrosis: Where do we stand?

Exploring Protein Kinase CK2 Substrate Recognition and the Dynamic Response of Substrate Phosphorylation to Kinase Modulation

Kinases and Phosphatases: The Challenge of a New Journal Entirely Focused on Post-Translational Modifications

KDM2A and KDM3B as Potential Targets for the Rescue of F508del-CFTR

Targeting the E1 ubiquitin-activating enzyme (UBA1) improves elexacaftor/tezacaftor/ivacaftor efficacy towards F508del and rare misfolded CFTR mutants

Development of small cyclic peptides targeting the CK2α/β interface

Targeting CK2 in cancer: a valuable strategy or a waste of time?

How can a traffic light properly work if it is always green? The paradox of CK2 signaling

Comparing the efficacy and selectivity of Ck2 inhibitors. A phosphoproteomics approach

Contribution of the CK2 Catalytic Isoforms α and α’ to the Glycolytic Phenotype of Tumor Cells

A mutational approach to dissect the functional role of the putative CFTR “PTM-CODE”

Editorial of Special Issue “Protein Post-Translational Modifications in Signal Transduction and Diseases”

Collaborators (6)

David R. Spring

Lorenzo A. Pinna

Maria Ruzzene

Andrea Rasola

Tsuyoshi Hirota

Marko Hyvönen

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