Author

P. Gracia

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 Plant Biology· 1

Signature Assays, Organisms & Methods

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Approach:statistical model· 2 Research Focus:differential expression· 1 Research Focus:drug response / drug discovery· 1 Approach:experimental assay· 1 Research Focus:GWAS / association mapping· 1 Organism:human· 1 Approach:mechanistic / dynamical model· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

N. Cremades· 2 shared A. H. Schulman· 1 shared A. M. Casas· 1 shared A. Tondelli· 1 shared C. M. Dobson· 1 shared E. Igartua· 1 shared F. Goni· 1 shared G. Bretani· 1 shared

Activity by Year

2020-2022 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 21 mutual co-author links

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2 shared papersBiophysics

N. Cremades

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Multi-environment genome-wide association mapping of culm morphology traits in barley

G. Bretani, S. Shaaf, A. Tondelli, L. Cattivelli, S. Delbono, R. Waugh, W. T. B. Thomas, J. Russel, H. Bull, E. Igartua, A. M. Casas, P. Gracia, R. Rossi, A. H. Schulman, L. Rossini

Genetic analysis of a diverse collection of European barleys reveals genomic regions underpinning stem morphological features associated with lodging resistance.

bioRxiv · Mar 30, 2022Plant Biology

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

The extent of protein hydration dictates the preference for heterogeneous or homogeneous nucleation generating either parallel or antiparallel β-sheet α-synuclein aggregates

J. D. Camino, P. Gracia, S. W. Chen, J. Sot, I. de la Arada, V. Sebastian, J. L. R. Arrondo, F. Goni, C. M. Dobson, N. Cremades

This study shows that α-synuclein can form amyloid aggregates via homogeneous nucleation under limited hydration, leading to antiparallel β-sheet structures, which are more stable than parallel ones under such conditions.

bioRxiv · Sep 28, 2020Biophysics