Author

Jaime Alegrio Louro

University of California San DiegoORCID 0000-0002-2800-923XUnclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Molecular Biology· 2 Biophysics· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Assay:cryo-EM· 1 Organism:human· 1 Approach:microscopy & imaging analysis· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

Andrés E. LeschzineriD· 2 shared Amalia C. Villagran SuareziD· 1 shared Andrés López‐PerroteiD· 1 shared Carlos Chacón-SáncheziD· 1 shared Clara RegleroiD· 1 shared Elena Blanco‐RomeroiD· 1 shared Elizabeth VillaiD· 1 shared Erica XiongiD· 1 shared

Activity by Year

2024-2026 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 21 mutual co-author links

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2 shared papersMolecular Biology

Andrés E. LeschzinerORCID

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Disruption of R2TP-mediated PIKK maturation with de novo designed binders

Nayim González-Rodríguez, Andrés López‐Perrote, Clara Reglero, Jaime Alegrio Louro, Marta Failde-Soler, Carlos Chacón-Sánchez, Elena Blanco‐Romero, Ester Casajús-Pelegay, Gema López-Pernas, Ivó H. Hernández, Matilde Murga, Óscar Fernández-Capetillo, Óscar Llorca, Rafael Fernández-Leiro

The paper identifies RUVBL1/2-RPAP3 interface as a vulnerability and develops de novo protein binders that selectively disrupt R2TP, reducing PIKK levels without affecting other RUVBL1/2 complexes.

bioRxiv · Oct 28, 2026 · PreprintMolecular Biology

Structural basis of nucleosome recognition by the conserved Dsup and HMGN nucleosome-binding motif

Jaime Alegrio Louro, Grisel Cruz‐Becerra, George A. Kassavetis, James T. Kadonaga, Andrés E. Leschziner

This study determines the structure of the Dsup and HMGN nucleosome-binding motif using cryo-EM, revealing their binding to the nucleosome acidic patch.

Genes & Development · Jul 28, 2025Peer-reviewedMolecular Biology

Cryo-electron tomography reveals the microtubule-bound form of inactive LRRK2

Siyu Chen, Tamar Basiashvili, Joshua Hutchings, Marta M. Sanz Murillo, Amalia C. Villagran Suarez, Erica Xiong, Jaime Alegrio Louro, Andrés E. Leschziner, Elizabeth Villa

This study uses cryo-ET to show that LRRK2 can form microtubule-bound filaments in its autoinhibited state, with structural differences compared to active-LRRK2 filaments.

eLife · Sep 9, 2024Peer-reviewedBiophysics