Author

I. Pallares

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· 2

Signature Assays, Organisms & Methods

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Research Focus:differential expression· 2 Approach:experimental assay· 2 Organism:human· 2 Assay:proteomics· 2 Research Focus:drug response / drug discovery· 1 Research Focus:host-pathogen & immune response· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

J. Pujols· 2 shared J. Santos· 2 shared S. Ventura· 2 shared A. Lends· 1 shared A. Loquet· 1 shared A. Muga· 1 shared A. N. Calabrese· 1 shared D. E. Otzen· 1 shared

Activity by Year

2021-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 45 mutual co-author links

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2 shared papersBiophysics

J. Pujols

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2 papers

Recent·Most cited

A targetable N-terminal motif orchestrates α-synuclein oligomer to fibril conversion

J. Santos, J. Cuellar, I. Pallares, E. J. Byrd, A. Lends, F. Moro, M. B. Abdul-Shukkoor, J. Pujols, L. Velasco-Carneros, F. Sobott, D. E. Otzen, A. N. Calabrese, A. Muga, J. S. Pedersen, A. Loquet, , S. Ventura

This study identifies an N-terminal motif in α-synuclein oligomers that drives fibril conversion and shows how a mutation disrupts this process, offering a new therapeutic target.

bioRxiv · Feb 10, 2023Biophysics

α-Helical peptidic scaffolds to target α-synuclein pathogenic species with high affinity and selectivity.

J. Santos, P. Gracia, S. Navarro, S. Pena-Diaz, J. Pujols, N. Cremades, I. Pallares, S. Ventura

The paper identifies α-helical peptides that selectively bind and neutralize pathogenic α-synuclein species with high affinity, suggesting potential therapeutic and diagnostic applications.

bioRxiv · Mar 12, 2021Biophysics