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neXtProt (http://www.nextprot.org) is a human protein-centric knowledgebase developed at the SIB Swiss Institute of Bioinformatics. Focused solely on human proteins, neXtProt aims to provide a state of the art resource for the representation of human biology by capturing a wide range of data, precise annotations, fully traceable data provenance and a web interface which enables researchers to find and view information in a comprehensive manner. Since the introductory neXtProt publication, significant advances have been made on three main aspects: the representation of proteomics data, an extended representation of human variants and the development of an advanced search capability built around semantic technologies. These changes are presented in the current neXtProt update

The stroma of higher plant chloroplasts contains two thioredoxins (Trx) with different specificity for the reduction of protein disulfide bonds. Based upon electrostatic features of domains that participate in the thiol/disulfide exchange, we prepared mutants of rapeseed Trx-m bearing opposite charges at a single position and subsequently analyzed their action on the activation of rapeseed chloroplast fructose 1,6-phosphate (CFBPase). The replacement of Pro-35 with lysine and glutamic residues enhanced and impaired, respectively, the stimulation of CFBPase relative to the wild-type and the P35A mutant. Furthermore, the shielding of electrostatic interactions with high concentrations of KCl greatly increased and concurrently made indistinguishable the affinity of all variants for CFBPase. The capacity to stimulate the enzyme activity likewise was enhanced concertedly by fructose-1,6-bisphosphate and Ca(2+) but, at variance with the action of KCl, remained sensitive to charges in the side chain of mutants. These results were consistent with a mechanism in which intermolecular electrostatic interactions and intramolecular non-covalent interactions control the formation of the non-covalent complex between reduced Trx and oxidized CFBPase and, in so doing, modulate the thiol/disulfide exchange. Fil: Duek, Paula D.. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina Fil: Wolosiuk, Ricardo Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina