Author

F. Dominguez

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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Microbiology· 3 Biochemistry· 1 Biophysics· 1 Physiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 6 Research Focus:host-pathogen & immune response· 5 Organism:human· 4 Assay:proteomics· 2 Research Focus:cell type annotation· 1 Research Focus:differential expression· 1 Research Focus:protein folding & dynamics· 1 Assay:protein sequence· 1

Frequent Co-Authors

D. Velazquez-Carreras· 3 shared E. Herrero-Galan· 3 shared I. Frolov· 3 shared P. Garcia-Pavia· 3 shared C. Suay-Corredera· 2 shared E. I. Frolova· 2 shared I. Martinez-Martin· 2 shared J. Alegre-Cebollada· 2 shared

Activity by Year

2020-2023 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 29 mutual co-author links

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3 shared papersBiochemistry

D. Velazquez-Carreras

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6 papers

Recent·Most cited

Alphavirus-induced transcriptional and translational shutoffs play major roles in blocking the formation of stress granules

O. Palchevska, F. Dominguez, E. I. Frolova, I. Frolov

This study shows that alphavirus-induced transcriptional and translational shutoffs, not nsP3 interactions with G3BP1/2 or ADP-ribosylhydrolase activity, are the main factors inhibiting stress granule formation.

bioRxiv · Jul 5, 2023 · PreprintMicrobiology

Amino acid substitutions hydrophilizing the core of titin domains cause dilated cardiomyopathy

I. Martinez-Martin, A. Crousilles, J. P. Ochoa, D. Velazquez-Carreras, S. A. Mortensen, E. Herrero-Galan, F. Dominguez, P. Garcia-Pavia, D. De Sancho, M. Wilmanns, J. Alegre-Cebollada

The paper identifies amino acid substitutions in titin domains that increase hydrophilicity and cause dilated cardiomyopathy by destabilizing the protein structure.

bioRxiv · Jun 2, 2023Biochemistry

NAP1L1 and NAP1L4 binding to Hypervariable Domain of Chikungunya Virus nsP3 Protein is bivalent and requires phosphorylation

F. Dominguez, N. Shiliaev, T. Lukash, P. Agback, O. Palchevska, J. R. Gould, C. D. Meshram, P. E. Prevelige, T. J. Green, T. Agback, E. I. Frolova, I. Frolov

This study identifies NAP1L1 and NAP1L4 as host factors that bind to the phosphorylated hypervariable domain of CHIKV nsP3, enhancing viral replication through bivalent interactions.

bioRxiv · May 19, 2021Microbiology

Structural and Functional Characterization of Host FHL1 Protein Interaction with Hypervariable Domain of Chikungunya Virus nsP3 Protein

T. Lukash, T. Agback, F. Dominguez, N. Shiliaev, C. Meshram, E. Frolova, P. Agback, I. Frolov

This study identifies FHL1 as a host factor interacting with CHIKV nsP3 HVD, showing it stimulates replication but is not essential, and highlights additive pro-viral effects with CD2AP.

bioRxiv · Sep 29, 2020Microbiology

Nanomechanical phenotypes in cMyBP-C mutants that cause hypertrophic cardiomyopathy

C. Suay-Corredera, M. R. Pricolo, D. Velazquez-Carreras, C. Pimenta-Lopes, D. Sanchez-Ortiz, I. Urrutia-Irazabal, S. Vilches, F. Dominguez, G. Frisso, L. Monserrat, P. Garcia-Pavia, E. Herrero-Galan, J. Alegre-Cebollada

This study investigates nanomechanical changes in cMyBP-C mutants linked to hypertrophic cardiomyopathy, finding that pathogenic mutations alter mechanical properties compared to non-pathogenic variants.

bioRxiv · Sep 19, 2020 · PreprintBiophysics

Conserved cysteines in titin sustain the mechanical function of cardiomyocytes

E. Herrero-Galan, F. Dominguez, I. Martinez-Martin, C. Sanchez-Gonzalez, N. Vicente, L. Lalaguna, E. Bonzon-Kulichenko, E. Calvo, E. Gonzalez-Lopez, M. Cobo-Marcos, B. Bornstein, A. Briceno, J. P. Ochoa, J. M. Garcia-Aznar, C. Suay-Corredera, , Aleg

The paper identifies that mutations in conserved titin cysteines disrupt mechanoredox control, leading to dilated cardiomyopathy in humans.

bioRxiv · Sep 5, 2020Physiology