Author

M. J. Marcaida

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· 1 Cancer Biology· 1 Cell Biology· 1 Immunology· 1

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Approach:experimental assay· 4 Approach:biophysical modeling· 2 Organism:Arabidopsis· 1 Assay:cryo-EM· 1 Research Focus:drug response / drug discovery· 1 Research Focus:gene regulatory network inference· 1 Research Focus:host-pathogen & immune response· 1 Organism:human· 1

Frequent Co-Authors

M. Dal Peraro· 3 shared F. Pojer· 2 shared A. J. Lamontanara· 1 shared A. Panjkovich· 1 shared C. Cao· 1 shared D. P. Duarte· 1 shared D. Svergun· 1 shared D. Y. Chirgadze· 1 shared

Activity by Year

2019-2024 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 20 mutual co-author links

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3 shared papersBiophysics

M. Dal Peraro

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Author profile →

4 papers

Recent·Most cited

Exploring new nanopore sensors from the aerolysin family

N. Cirauqui Diaz, J. F. Bada Juarez, F. A. Meireles, J. Barry, M. Bokori-Brown, M. J. Marcaida, C. Cao, M. Dal Peraro

The paper explores new nanopore sensors from the aerolysin family by analyzing structure and sensing capabilities of three family members, finding ETX can translocate ssDNA with higher sensitivity than aerolysin.

bioRxiv · Apr 7, 2024 · PreprintBiophysics

Structure and dynamics of Toll immunoreceptor activation in the mosquito Aedes aegypti

Y. Saucereau, T. H. Wilson, M. C. , K. Tang, M. C. Moncrieffe, S. W. Hardwick, D. Y. Chirgadze, S. G. Soares, M. J. Marcaida, N. J. Gay, M. Gangloff

The paper presents cryo-EM structures of Toll5A and Spaetzle1C complexes in Aedes aegypti, revealing their asymmetric interactions and distinct transcriptional roles in immune response.

bioRxiv · Sep 6, 2021Immunology

Molecular mode of action of an Acyl Protein thioesterase

L. Abrami, M. Audagnotto, S. Ho, M. J. Marcaida, F. Mesquita, M. Anward, P. A. Sandoz, G. Fonti, F. Pojer, M. Dal Peraro, F. G. van der Goot

The paper investigates the molecular mechanism of APT2, showing it interacts with membranes via a hydrophobic loop and S-acylation, deforms lipid bilayers to extract acyl chains, and is subject to ubiquitination and degradation.

bioRxiv · Jun 18, 2020 · PreprintCell Biology

Btk SH2-kinase interface is critical for allosteric kinase activation and its targeting inhibits B-cell neoplasms

D. P. Duarte, A. J. Lamontanara, G. La Sala, S. Jeong, Y.-K. Sohn, A. Panjkovich, S. Georgeon, T. Kukenshoner, M. J. Marcaida, F. Pojer, M. De Vivo, D. Svergun, H.-S. Kim, M. Dal Peraro, O. Hantschel

This study identifies the Btk SH2-kinase interface as critical for activation and shows that targeting it with a repebody inhibits B-cell neoplasms.

bioRxiv · Dec 10, 2019Cancer Biology