Author

M. Gairi

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

Click to filter author papers

Biophysics· 2

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:chromatin & epigenetic regulation· 1 Organism:human· 1 Research Focus:protein folding & dynamics· 1 Assay:protein structure· 1 Assay:proteomics· 1 Approach:wet-lab / biochemical assay· 1

Frequent Co-Authors

A. Escobedo· 1 shared A. Fernandez· 1 shared A. Lang· 1 shared B. Eftekharzadeh· 1 shared B. Topal· 1 shared D. Mungianu· 1 shared F. Cardenas· 1 shared G. Bernardo-Seisedos· 1 shared

Activity by Year

2019-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 24 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

1 shared paperBiophysics

A. Escobedo

Mutual co-authors in cluster

Author profile →

2 papers

Recent·Most cited

Modulation of functional phosphorylation sites by basic residues in the Unique domain of c-Src

A. Lang, A. Fernandez, M. Diaz-Lobo, M. Vilanova, F. Cardenas, M. Gairi, M. Pons

The paper investigates how basic residues modulate phosphorylation sites in the SNRE of c-Src using NMR and mutations, revealing electrostatic interactions and their effects on conformation.

bioRxiv · May 23, 2023Biophysics

Side chain to main chain hydrogen bonds stabilize a polyglutamine helix in the activation domain of a transcription factor

A. Escobedo, B. Topal, M. B. A. Kunze, J. Aranda, G. Chiesa, D. Mungianu, G. Bernardo-Seisedos, B. Eftekharzadeh, M. Gairi, R. Pieratelli, I. Felli, T. Diercks, O. Millet, J. Garcia, M. Orozco, , X. Salvatella

This study investigates how polyglutamine tract length affects the structure and function of the androgen receptor, revealing hydrogen bonds that stabilize a helical conformation linked to transcriptional activity and disease.

bioRxiv · Feb 28, 2019Biophysics