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Salvador Ventura

Researcher at Autonomous University of Barcelona

Publications -  263
Citations -  15830

Salvador Ventura is an academic researcher from Autonomous University of Barcelona. The author has contributed to research in topics: Protein aggregation & Protein folding. The author has an hindex of 53, co-authored 263 publications receiving 13730 citations. Previous affiliations of Salvador Ventura include European Bioinformatics Institute & Catalan Institution for Research and Advanced Studies.

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Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition)

Daniel J. Klionsky, +2522 more
- 21 Jan 2016 - 
TL;DR: In this paper, the authors present a set of guidelines for the selection and interpretation of methods for use by investigators who aim to examine macro-autophagy and related processes, as well as for reviewers who need to provide realistic and reasonable critiques of papers that are focused on these processes.
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AGGRESCAN: a server for the prediction and evaluation of "hot spots" of aggregation in polypeptides

Oscar Conchillo-Solé, +6 more
- 27 Feb 2007 - 
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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Protein quality in bacterial inclusion bodies

Salvador Ventura, +1 more
- 01 Apr 2006 - 
TL;DR: Recent data suggest that these protein aggregates might be a reservoir of alternative conformational states, their formation being no less specific than the acquisition of the native-state structure.
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Aggregation as bacterial inclusion bodies does not imply inactivation of enzymes and fluorescent proteins

Elena García-Fruitós, +7 more
- 12 Sep 2005 - 
TL;DR: It is shown that physiological aggregation in bacteria might only result in a moderate loss of biological activity and that inclusion bodies can be used in reaction mixtures for efficient catalysis.
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Short amino acid stretches can mediate amyloid formation in globular proteins: The Src homology 3 (SH3) case

Salvador Ventura, +10 more
- 11 May 2004 - 
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.