Author

D. Cabezas-Bratesco

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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Biophysics· 3 Evolutionary Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Organism:human· 3 Research Focus:cell signaling & trafficking· 2 Approach:biophysical modeling· 1 Assay:electrophysiology· 1 Assay:fluorescence / live-cell microscopy· 1 Research Focus:host-pathogen & immune response· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

S. E. Brauchi· 4 shared V. Carnevale· 2 shared A. N. Miller· 1 shared B. Cristofori-Armstrong· 1 shared C. A. Ahern· 1 shared C. K. Colenso· 1 shared D. Bustos· 1 shared D. E. Clapham· 1 shared

Activity by Year

2017-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 19 mutual co-author links

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4 shared papersBiophysics

S. E. Brauchi

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Author profile →

4 papers

Recent·Most cited

Intracellular helix-loop-helix domain modulates inactivation kinetics of mammalian TRPV5 and TRPV6 channels.

L. Flores-Aldama, D. Bustos, D. Cabezas-Bratesco, S. E. Brauchi

The paper identifies amino acids and interactions that determine inactivation kinetics of TRPV5 and TRPV6 channels, proposing the HLH-TDh domain association drives faster inactivation in TRPV6.

bioRxiv · Oct 4, 2022Biophysics

The SARS-CoV-2 accessory protein Orf3a is not an ion channel, but does interact with trafficking proteins

A. N. Miller, P. R. Houlihan, E. Matamala, D. Cabezas-Bratesco, G. Y. Lee, B. Cristofori-Armstrong, T. L. Dilan, S. Sanchez-Martinez, D. Matthies, R. Yan, Z. Yu, D. Ren, S. E. Brauchi, D. E. Clapham

This paper shows SARS-CoV-2 Orf3a is not an ion channel but interacts with trafficking proteins, while SARS-CoV-1 Orf3a does not.

bioRxiv · Sep 2, 2022Biophysics

Sequence conservation and structural features that are common within TRP channels

D. Cabezas-Bratesco, C. K. Colenso, K. Zavala, D. Granata, V. Carnevale, J. C. Opazo, S. E. Brauchi

The paper identifies a conserved residue fingerprint in TRP channels that may explain differences in coupling strategies among subgroups.

bioRxiv · Sep 6, 2021Evolutionary Biology

Conformational Dynamics In TRPV1 Channels Reported By An Encoded Coumarin Amino Acid

X. Steinberg, M. A. Kasimova, D. Cabezas-Bratesco, J. Galpin, E. Ladron de Guevara, F. Villa, V. Carnevale, L. D. Islas, C. A. Ahern, S. E. Brauchi

This study uses a genetically encoded fluorescent amino acid to monitor conformational changes in TRPV1 channels, showing that Y671 fluorescence correlates with channel activation by capsaicin.

bioRxiv · May 14, 2017Biophysics