Author

José Luis Martínez

Consejo Superior de Investigaciones CientíficasORCID 0000-0001-8813-7607Unclaimed ORCID profile · follow to get notified of new preprints

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José Luis Martínez1 paper

Biology Disciplines

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Biochemistry· 1 Microbiology· 1

Signature Assays, Organisms & Methods

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Organism:bacteria (other)· 1 Research Focus:cell type annotation· 1 Approach:experimental assay· 1 Research Focus:host-pathogen & immune response· 1 Organism:human· 1 Assay:metagenomics· 1 Approach:statistical model· 1

Frequent Co-Authors

Ana Elena Pérez‐CobasiD· 1 shared Antoine AndremontiD· 1 shared Antonio RomeroiD· 1 shared Fernando BaqueroiD· 1 shared Francisco J. MedranoiD· 1 shared Miguel D. Fernández-de-BobadillaiD· 1 shared Sara Hernando‐AmadoiD· 1 shared Teresa M. CoqueiD· 1 shared

Activity by Year

2024-2025 · peak 1/yr

Co-Author Collaboration Network

9 top collaborators · 18 mutual co-author links

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1 shared paperMicrobiology

Ana Elena Pérez‐CobasORCID

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2 papers

Recent·Most cited

MicrobiologybioRxivPreprintJun 30, 2025

The Antimicrobial Gut Resistome of the Wayampi reveals a shared background of antibiotic and metal resistance genes with industrialised populations, underscoring the robust-yet-fragile architecture of human gut microbiomes.

Miguel D. Fernández-de-Bobadilla, Ana Elena Pérez‐Cobas, Antoine Andremont…·Teresa M. Coque

The study analyzes the gut resistome of the Wayampi, revealing similar antibiotic resistance gene richness to Europeans but higher metal resistance gene diversity, highlighting shared and distinct resistance patterns.

1 citation

humanmetagenomics

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BiochemistryInternational Journal of Biological MacromoleculesPeer-reviewedAug 2, 2024

A new type of AmpC β-lactamases defined by PIB-1, a metal-dependent carbapenem-hydrolyzing β-lactamase, from Pseudomonas aeruginosa: structural and functional analysis.

Francisco J. Medrano, Sara Hernando‐Amado, José Luis Martínez, Antonio Romero

The paper identifies PIB-1, a metal-dependent carbapenem-hydrolyzing β-lactamase from Pseudomonas aeruginosa, structurally and functionally distinct from typical AmpC β-lactamases.

7 citations

bacteria (other)experimental assay

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