Author

B. Topal

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 Immunology· 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:differential expression· 1 Research Focus:host-pathogen & immune response· 1 Assay:metabolomics· 1

Frequent Co-Authors

A. Escobedo· 2 shared J. Aranda· 2 shared J. Garcia· 2 shared M. Orozco· 2 shared O. Millet· 2 shared R. Crehuet· 2 shared T. Diercks· 2 shared X. Salvatella· 2 shared

Activity by Year

2019-2022 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 29 mutual co-author links

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2 shared papersBiophysics

A. Escobedo

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

BiophysicsbioRxivMay 6, 2022

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

A. Escobedo, J. G. Piccirillo, J. Aranda…·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.

DOI 10.1038/s41467-022-34793-6

protein structuredeep learning

𝕏 PostBluesky

ImmunologybioRxivFeb 1, 2020

Macrophage Scavenger Receptor 1 mediates lipid-induced inflammation in non-alcoholic fatty liver disease

O. Govaere, S. K. Petersen, N. Martinez-Lopez…·A. Hartlova

This study identifies MSR1 as a key mediator of lipid-induced inflammation in NAFLD, showing its role in macrophage activation and potential as a therapeutic target.

DOI 10.1016/s0168-8278(20)30598-5

humanmouse

𝕏 PostBluesky

BiophysicsbioRxivFeb 28, 2019

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…·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.

DOI 10.1038/s41467-019-09923-2

humanprotein structure

𝕏 PostBluesky