Author

I. E. Sanchez

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:statistical model· 2 Approach:experimental assay· 1 Research Focus:host-pathogen & immune response· 1 Research Focus:protein folding & dynamics· 1 Assay:protein sequence· 1 Assay:protein structure· 1 Assay:proteomics· 1 Research Focus:sequence-to-function modeling· 1

Frequent Co-Authors

A. A. Aptekmann· 1 shared A. Barozet· 1 shared A. Estana· 1 shared A. S. H. Berthet· 1 shared A. S. Holehouse· 1 shared A. Sagar· 1 shared C. Blanes-Mira· 1 shared C. Löw· 1 shared

Activity by Year

2021-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 18 mutual co-author links

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1 shared paperBiophysics

A. A. Aptekmann

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Author profile →

3 papers

Recent·Most cited

PhISCO: a simple method to infer phenotypes from protein sequences

A. S. H. Berthet, A. A. Aptekmann, j. t. bravo, I. E. Sanchez, M. E. Noguera, E. A. Roman

PhISCO infers phenotypes from protein sequences using a simple linear model, achieving comparable accuracy to complex methods with minimal input.

bioRxiv · Oct 23, 2022 · PreprintBiophysics

Deamidation drives molecular aging of the SARS-CoV-2 spike receptor-binding motif

R. Lorenzo, L. A. Defelipe, L. Aliperti, S. Niebling, T. F. Custodio, C. Löw, J. J. Schwarz, K. Remans, P. O. Craig, L. H. Otero, S. Klinke, M. Garcia-Alai, I. E. Sanchez, L. G. Alonso

This study identifies deamidation hotspots in the SARS-CoV-2 spike receptor-binding motif, showing how this post-translational modification affects viral infectivity and immune response over time.

bioRxiv · May 20, 2021Biochemistry

Conformational buffering underlies functional selection in intrinsically disordered protein regions

N. S. Gonzalez-Foutel, W. M. Borcherds, J. Glavina, S. Barrera-Vilarmau, A. Sagar, A. Estana, A. Barozet, G. Fernandez-Ballester, C. Blanes-Mira, I. E. Sanchez, G. de Prat Gay, J. Cortes, P. Bernado, R. V. Pappu, A. S. Holehouse, , L. B. Chemes

The paper identifies conformational buffering as a mechanism that conserves spatial dimensions in disordered protein regions despite sequence variation, enabling functional selection.

bioRxiv · May 14, 2021Biophysics