Author

N. Cremades

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· 1 Research Focus:drug response / drug discovery· 1 Approach:experimental assay· 1 Organism:human· 1 Approach:mechanistic / dynamical model· 1 Research Focus:protein folding & dynamics· 1 Assay:protein structure· 1 Assay:proteomics· 1

Frequent Co-Authors

P. Gracia· 2 shared C. M. Dobson· 1 shared F. Goni· 1 shared I. de la Arada· 1 shared I. Pallares· 1 shared J. D. Camino· 1 shared J. L. R. Arrondo· 1 shared J. Pujols· 1 shared

Activity by Year

2020-2021 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 27 mutual co-author links

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2 shared papersBiophysics

P. Gracia

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Author profile →

2 papers

Recent·Most cited

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