Author

G. Jimenez-Oses

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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Biochemistry· 2 Biophysics· 1

Signature Assays, Organisms & Methods

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Assay:protein structure· 3 Approach:experimental assay· 2 Research Focus:protein folding & dynamics· 2 Research Focus:protein structure prediction· 2 Approach:biophysical modeling· 1 Approach:deep learning· 1 Organism:human· 1 Approach:statistical model· 1

Frequent Co-Authors

R. Nunez-Franco· 2 shared A. Astegno· 1 shared A. Schedlbauer· 1 shared A. Torres-Mozas· 1 shared C. Conter· 1 shared C. D. Navo· 1 shared C. Fernandez-Rodriguez· 1 shared C. Gil-Pitarch· 1 shared

Activity by Year

2018-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 17 mutual co-author links

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2 shared papersBiophysics

R. Nunez-Franco

Mutual co-authors in cluster

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3 papers

Recent·Most cited

Thermodynamic Stabilization of Human Frataxin

R. Nunez-Franco, A. Torres-Mozas, C. D. Navo, A. Schedlbauer, M. Azkargorta, I. Iloro, F. Elortza, G. Ortega, O. Millet, F. Peccati, G. Jimenez-Oses

This study thermodynamically stabilizes human frataxin using computational methods, improving its stability and resistance to proteolysis without compromising function.

bioRxiv · Sep 8, 2023 · PreprintBiophysics

Structure of Cystathionine β-Synthase from Toxoplasma gondii, a key enzyme in its H2S production machinery.

C. Fernandez-Rodriguez, I. Oyenarte, C. Conter, I. Gonzalez-Recio, R. Nunez-Franco, C. Gil-Pitarch, I. Quintana, G. Jimenez-Oses, P. Dominici, M. L. Martinez-Chantar, A. Astegno, L. A. Martinez-Cruz

The paper reports the crystal structure of TgCBS from Toxoplasma gondii, revealing a novel fold distinct from other CBS structures but similar to a human pathogenic mutant.

bioRxiv · Jan 15, 2021 · PreprintBiochemistry

Substrate-assisted Enzymatic Formation of Lysinoalanine in Duramycin

L. An, D. Cogan, C. Navo, G. Jimenez-Oses, S. Nair, W. van der Donk

The paper investigates the mechanism of lysinoalanine formation in duramycin, showing that it is catalyzed by DurN through a substrate-assisted process involving Hya15 as a base.

bioRxiv · Jul 8, 2018Biochemistry