Author

V. M. Faca

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· 2 Immunology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Organism:human· 2 Research Focus:protein folding & dynamics· 2 Assay:proteomics· 2 Research Focus:cell signaling & trafficking· 1 Approach:deep learning· 1 Approach:genetic perturbation / CRISPR· 1 Research Focus:host-pathogen & immune response· 1

Frequent Co-Authors

A. P. Masson· 2 shared A. Akturk· 1 shared A. S. Sebollela· 1 shared A. Sulpizio· 1 shared E. A. Donadi· 1 shared G. A. Passos· 1 shared G. D. Ferrari· 1 shared H. M. K. Schwaemmle· 1 shared

Activity by Year

2019-2021 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 17 mutual co-author links

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2 shared papersImmunology

A. P. Masson

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3 papers

Recent·Most cited

The AIRE G228W mutation disturbs the interaction of AIRE with its partner molecule SIRT1

J. C. Santos, M. Dametto, A. P. Masson, V. M. Faca, R. Bonacin, E. A. Donadi, G. A. Passos

This study investigates how the AIRE G228W mutation disrupts the AIRE-SIRT1 interaction, affecting transcriptional processes in medullary thymic epithelial cells.

bioRxiv · Aug 24, 2021Immunology

A freeze-and-thaw induced-fragment of the microtubule-associated protein Tau in rat brain extracts: implications for the biochemical assessment of neurotoxicity

I. C. Vasconcelos, R. M. d. Campos, H. M. K. Schwaemmle, A. P. Masson, G. D. Ferrari, L. C. Alberici, V. M. Faca, N. Garcia-Cairasco, A. S. Sebollela

This study shows that freeze-and-thaw cycles cause Tau fragmentation in rodent brain extracts, affecting WB results, but not in human samples.

bioRxiv · Nov 16, 2020Biochemistry

Deubiquitination of phosphoribosyl-ubiquitin conjugates by PDE domain-containing Legionella effectors

M. Wan, A. Sulpizio, A. Akturk, W. H. J. Beck, M. Lanz, V. M. Faca, M. B. Smolka, J. P. Vogel, Y. Mao

This paper identifies DupA and DupB as deubiquitinases that reverse PR-ubiquitination, a novel modification mediated by Legionella effectors, and shows their role in modulating host-pathogen interactions.

bioRxiv · Aug 23, 2019Biochemistry