V
Valentina Riveros-Moreno
Researcher at Wellcome Trust
Publications - 7
Citations - 903
Valentina Riveros-Moreno is an academic researcher from Wellcome Trust. The author has contributed to research in topics: Peptide sequence & Nitric oxide synthase. The author has an hindex of 6, co-authored 7 publications receiving 888 citations.
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Journal ArticleDOI
Localization of Nitric Oxide Synthase in the Adult Rat Brain
José Rodrigo,David R. Springall,O. Uttenthal,M. L. Bentura,Francisco Abadía-Molina,Valentina Riveros-Moreno,Ricardo Martínez-Murillo,Julia M. Polak,Salvador Moncada +8 more
TL;DR: The distribution of the immunoreactivity to nitric oxide synthase has been examined from rostral to caudal areas of the rat central nervous system using light microscopy.
Journal ArticleDOI
Primary structure of the precursor to the three major surface antigens of Plasmodium falciparum merozoites.
Anthony A. Holder,Michael Lockyer,Karel G. Odink,Jasbir Singh Sandhu,Valentina Riveros-Moreno,Stephen C. Nicholls,Yvonne Hillman,Lynne S. Davey,Mark Tizard,Ralph T. Schwarz,Robert R. Freeman +10 more
TL;DR: The complete structure of the P195 gene determined from further DNA clones is described, its organization within genomic DNA and the location of the specific processing fragments within the primary amino-acid sequence are described.
Journal ArticleDOI
Induction of nitric oxide synthase in colonic smooth muscle from patients with toxic megacolon
Marisabel Mourelle,Francesc Casellas,Francisco Guarner,Antonio Salas,Valentina Riveros-Moreno,Salvador Moncada,Juan-R. Malagelada +6 more
TL;DR: Toxic megacolon is associated with the appearance of inducible NO synthase in the Colonic muscularis propria, and local generation of excessive amounts of NO may be responsible for the colonic dilatation that is the hallmark of this syndrome.
Journal ArticleDOI
Nitric oxide synthase. Structural studies using anti-peptide antibodies.
TL;DR: The amino acid sequence for the constitutive rat brain nitric oxide (NO) synthase was analysed by a set of computer programs that estimate and display physicochemical properties such as hydrophilicity, flexibility, accessibility, hydrophilic periodicity and conformation to postulate that either the peptides when conjugated to the carrier protein attain a different conformed to that in the native NO synthase, or alternatively the accessibility of the antibodies to substrate binding sites is highly restricted by steric
Journal ArticleDOI
Purification to homogeneity and characterisation of rat brain recombinant nitric oxide synthase
Valentina Riveros-Moreno,Brian Heffernan,Belkis Torres,Ann Chubb,I. G. Charles,Salvador Moncacdta +5 more
TL;DR: A substantial proportion of the total NO synthase produced becomes soluble following addition of hemin to the culture medium, and it is demonstrated that the enzyme activity is exclusively associated with the dimeric form of the enzyme, which had the following molar ratios for the cofactors.