Author

Lucı́a Álvarez

Centre National de la Recherche ScientifiqueORCID 0000-0002-1437-5773Unclaimed ORCID profile · follow to get notified of new preprints

Additional preprints under this name without ORCID

Lucía Álvarez1 paper · Universitat Autònoma de Barcelona

Biology Disciplines

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Biochemistry· 1 Biophysics· 1 Immunology· 1

Signature Assays, Organisms & Methods

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Organism:human· 3 Research Focus:cell signaling & trafficking· 2 Approach:experimental assay· 2 Research Focus:protein folding & dynamics· 2 Assay:proteomics· 2 Approach:statistical model· 2 Research Focus:chromatin & epigenetic regulation· 1 Approach:deep learning· 1

Frequent Co-Authors

Janosch HennigiD· 2 shared Alexandre BélotiD· 1 shared Alice LepelleyiD· 1 shared Ariane GuillemotiD· 1 shared Benjamin LéonardoniD· 1 shared Brigitte Bader‐MeunieriD· 1 shared Camille BrunaudiD· 1 shared Cécile Lagaudrière‐GesbertiD· 1 shared

Activity by Year

2024-2026 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 36 mutual co-author links

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2 shared papersBiophysics

Janosch HennigORCID

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3 papers

Recent·Most cited

ImmunologyNature CommunicationsPeer-reviewedAug 19, 2026

NAP1 switches from an activator to a limiter of interferon induction by trapping TBK1 in condensates

Damien Glon, Quentin Riller, Lucı́a Álvarez…·Yves Gaudin

This study shows NAP1 switches from enhancing to limiting TBK1 activity through condensate formation, affecting IFN induction and linking to interferonopathies.

DOI 10.1038/s41467-026-76769-w

humanproteomics

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BiophysicsbioRxivPreprintJun 23, 2026

Electrostatic interactions compensate energetic frustration in the coupled folding and binding of intrinsically disordered proteins

Lucı́a Álvarez, Nicolás A. Garrone, Michaël Claron…·Lucia Beatriz Chemes

The paper investigates the energy landscape of coupled folding and binding in intrinsically disordered proteins, finding that electrostatic interactions compensate for energetic frustration.

DOI 10.64898/2026.01.07.698246

humanprotein structure

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BiochemistryThe EMBO JournalPeer-reviewedMar 6, 2024

Structural Insights into The Role of MAGEA4 in RAD18 Regulation: Implications for Ubiquitin Ligase-Binding across the MAGE Protein Family

Simonne Griffith-Jones, Lucía Álvarez, Urbi Mukhopadhyay…·Sagar Bhogaraju

This study identifies the interaction between MAGEA4 and RAD18 using NMR and AlphaFold2, revealing structural insights into how MAGEA4 regulates RAD18's ubiquitination activity and its implications for cancer.

12 citations

humanproteomics

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