F
Francesc X. Avilés
Researcher at Autonomous University of Barcelona
Publications - 272
Citations - 11045
Francesc X. Avilés is an academic researcher from Autonomous University of Barcelona. The author has contributed to research in topics: Carboxypeptidase & Carboxypeptidase A. The author has an hindex of 54, co-authored 267 publications receiving 10462 citations. Previous affiliations of Francesc X. Avilés include Max Planck Society & National University of La Plata.
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Journal ArticleDOI
AGGRESCAN: a server for the prediction and evaluation of "hot spots" of aggregation in polypeptides
Oscar Conchillo-Solé,Natalia Sanchez de Groot,Francesc X. Avilés,Josep Vendrell,Xavier Daura,Xavier Daura,Salvador Ventura +6 more
TL;DR: The algorithm is shown to identify a series of protein fragments involved in the aggregation of disease-related proteins and to predict the effect of genetic mutations on their deposition propensities, which shall facilitate the identification of possible therapeutic targets for anti-depositional strategies in conformational diseases.
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The structure of histone H1 and its location in chromatin.
TL;DR: On the basis of their primary structure, the lysine-rich histones are a unified family of proteins that are protected from trypsin digestion in chromatin and corresponds to the segment of highest sequence conservation.
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Automated structure-based prediction of functional sites in proteins: applications to assessing the validity of inheriting protein function from homology in genome annotation and to protein docking.
TL;DR: In this article, the authors used a multiple sequence alignment to identify invariant polar residues, which were then mapped onto the protein structure and spatial clusters of these invariant residues formed the predicted functional sites.
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Short amino acid stretches can mediate amyloid formation in globular proteins: The Src homology 3 (SH3) case
Salvador Ventura,Jesús Zurdo,Saravanakumar Narayanan,Matilde Parreño,Ramon Mangues,Bernd Reif,Fabrizio Chiti,Elisa Giannoni,Christopher M. Dobson,Francesc X. Avilés,Luis Serrano +10 more
TL;DR: These findings show that short specific amino acid stretches can act as mediators or facilitators in the incorporation of globular proteins into amyloid structures, and they support the suggestion that natural protein sequences have evolved in part to code for structural characteristics other than those included in the native fold, such as avoidance of aggregation.
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Amyloid Fibril Formation by a Partially Structured Intermediate State of α-Chymotrypsin
TL;DR: The data support the hypothesis that amyloid formation involves the ordered self-assembly of partially folded species that are critical soluble precursors of fibrilar aggregates.