Author

P. Vergani

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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Biochemistry· 1 Biophysics· 1 Pharmacology & Toxicology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Organism:human· 2 Research Focus:protein folding & dynamics· 2 Approach:biophysical modeling· 1 Research Focus:cell type annotation· 1 Research Focus:chromatin & epigenetic regulation· 1 Research Focus:drug response / drug discovery· 1 Assay:fluorescence / live-cell microscopy· 1

Frequent Co-Authors

D. P. Tieleman· 2 shared S. Prins· 2 shared V. Corradi· 2 shared A. C. Stefan· 1 shared C. Hastings· 1 shared D. N. Sheppard· 1 shared E. J. Hill· 1 shared E. Langron· 1 shared

Activity by Year

2017-2021 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 23 mutual co-author links

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2 shared papersBiophysics

D. P. Tieleman

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3 papers

Recent·Most cited

Can two wrongs make a right? F508del-CFTR ion channel rescue by second-site mutations in its transmembrane domains

S. Prins, V. Corradi, D. N. Sheppard, D. P. Tieleman, P. Vergani

This study identifies second-site mutations that rescue F508del-CFTR dysfunction by restoring hydrophobic interactions and conformational flexibility at the ICL4/NBD1 interface.

bioRxiv · Sep 7, 2021Biophysics

Fluorescence assay for simultaneous quantification of CFTR ion-channel function and plasma membrane proximity

S. Prins, E. Langron, C. Hastings, E. J. Hill, A. C. Stefan, L. D. Griffin, P. Vergani

This paper introduces a fluorescence assay to simultaneously measure CFTR ion-channel function and membrane proximity, validating it with published data and drug treatments.

bioRxiv · May 5, 2020Pharmacology & Toxicology

Structure of transmembrane helix 8 and possible membrane defects in CFTR

V. Corradi, R.-X. Gu, P. Vergani, D. P. Tieleman

This study uses molecular dynamics simulations to analyze the structural role of transmembrane helix 8 in CFTR and identifies a membrane defect specific to the ATP-free state.

bioRxiv · Nov 13, 2017Biochemistry