Author

A. Escobedo

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· 2 Biochemistry· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Organism:human· 2 Assay:protein structure· 2 Research Focus:chromatin & epigenetic regulation· 1 Approach:deep learning· 1 Research Focus:drug response / drug discovery· 1 Research Focus:protein structure prediction· 1 Assay:proteomics· 1

Frequent Co-Authors

J. Garcia· 3 shared X. Salvatella· 3 shared B. Topal· 2 shared J. Aranda· 2 shared M. Biesaga· 2 shared M. Orozco· 2 shared O. Millet· 2 shared R. Crehuet· 2 shared

Activity by Year

2019-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 39 mutual co-author links

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3 shared papersBiophysics

J. Garcia

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Author profile →

3 papers

Recent·Most cited

Rational optimization of a transcription factor activation domain inhibitor

S. Basu, P. Martinez-Cristobal, M. Pesarrodona, M. Frigole-Vivas, E. Szulc, M. Lewis, A. Banuelos, C. Sanchez-Zarzalejo, S. Bielskute, J. Zhu, K. Pombo-Garcia, C. Garcia-Cabau, C. Batlle, B. Mateos, M. Biesaga, , X. Salvatella

This study optimizes a small molecule inhibitor targeting the aromatic-rich activation domain of the androgen receptor, showing improved affinity and antitumorigenic effects in prostate cancer models.

bioRxiv · Aug 18, 2022Biochemistry

A glutamine-based single α-helix scaffold to target globular proteins

A. Escobedo, J. G. Piccirillo, J. Aranda, T. Diercks, B. Topal, M. Biesaga, L. Staby, B. B. Kragelund, J. Garcia, O. Millet, M. Orozco, M. Coles, R. Crehuet, X. Salvatella

This paper introduces a method to design peptides that fold into single α-helices using glutamine side chain to main chain hydrogen bonds, enabling targeted interactions with globular proteins.

bioRxiv · May 6, 2022Biophysics

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