Zobrazeno 1 - 10
of 16
pro vyhledávání: '"Tomás Mayoral"'
Autor:
Natalia Fernández-Borges, Beatriz Parra, Enric Vidal, Hasier Eraña, Manuel A Sánchez-Martín, Jorge de Castro, Saioa R Elezgarai, Martí Pumarola, Tomás Mayoral, Joaquín Castilla
Publikováno v:
PLoS Pathogens, Vol 13, Iss 11, p e1006716 (2017)
One of the characteristics of prions is their ability to infect some species but not others and prion resistant species have been of special interest because of their potential in deciphering the determinants for susceptibility. Previously, we develo
Externí odkaz:
https://doaj.org/article/66df325ea43344228cc46fa53c68007e
Autor:
Jorge M. Charco, Belén Pintado, Miguel A. Pérez-Castro, Manuel Sánchez-Martín, Tomás Mayoral, Hasier Eraña, Joaquín Castilla, Enric Vidal, Martí Pumarola, Montserrat Ordóñez, Natalia Fernández-Borges, Candace K. Mathiason, Beatriz Parra
Publikováno v:
Digital.CSIC. Repositorio Institucional del CSIC
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Unlike other species, prion disease has never been described in dogs even though they were similarly exposed to the bovine spongiform encephalopathy (BSE) agent. This resistance prompted a thorough analysis of the canine PRNP gene and the presence of
Autor:
Beatriz Parra, Hasier Eraña, Tomás Mayoral, Manuel Sánchez-Martín, Jorge M. Charco, Candace K. Mathiason, Enric Vidal, Miguel A. Pérez-Castro, Belén Pintado, Martí Pumarola, Joaquín Castilla, Natalia Fernández-Borges, Montserrat Ordóñez
Unlike other species, such as cattle, cats or humans, prion disease has never been described in dogs, even though they were similarly exposed to the bovine spongiform encephalopathy (BSE) agent. This resistance prompted a thorough analysis of the can
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cb65c1615301a9bd5181dbbe13093828
https://doi.org/10.1101/800698
https://doi.org/10.1101/800698
Autor:
Beatriz Parra, Jorge M. Charco, Manuel Sánchez-Martín, Umberto Agrimi, Natalia Fernández-Borges, Claudia D'Agostino, Michele Angelo Di Bari, Tomás Mayoral, Gabriele Vaccari, Laura Pirisinu, Joaquín Castilla, Vanessa Venegas, Hasier Eraña, Chafik Harrathi, Jesús R. Requena, David Gil, Romolo Nonno, Saioa R. Elezgarai, Rafael López-Moreno, Ilaria Vanni
Publikováno v:
Acta neuropathologica. 135(2)
Prion diseases are caused by a misfolding of the cellular prion protein (PrP) to a pathogenic isoform named PrPSc. Prions exist as strains, which are characterized by specific pathological and biochemical properties likely encoded in the three-dimens
Autor:
Julia Sanz-Aparicio, Tomás Mayoral, Juan A. Hermoso, Marta Martínez-Júlvez, Carlos Gómez-Moreno, Inmaculada Pérez-Dorado, Milagros Medina
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 59:592-602
The three-dimensional structures of K72E, K75R, K75S, K75Q, and K75E Anabaena Ferredoxin-NADP reductase (FNR) mutants have been solved, and particular structural details of these mutants have been used to assess the role played by residues 72 and 75
Autor:
Susana Frago, Tomás Mayoral, Milagros Medina, Juan A. Hermoso, Carlos Gómez-Moreno, Julia Sanz-Aparicio, Merche Faro
Publikováno v:
European Journal of Biochemistry. 269:4938-4947
The role of the negative charge of the E139 side-chain of Anabaena Ferredoxin-NADP+ reductase (FNR) in steering appropriate docking with its substrates ferredoxin, flavodoxin and NADP+/H, that leads to efficient electron transfer (ET) is analysed by
Autor:
Milagros Medina, Tomás Mayoral, Carlos Gómez-Moreno, Julia Sanz-Aparicio, Merche Faro, Juan A. Hermoso
Publikováno v:
Journal of Molecular Biology. 319:1133-1142
The flavoenzyme ferredoxin-NADP+ reductase (FNR) catalyses the production of NADPH in photosynthesis. The three-dimensional structure of FNR presents two distinct domains, one for binding of the FAD prosthetic group and the other for NADP+ binding. I
Autor:
Julia Sanz-Aparicio, Tammy B. Brodie, Milagros Medina, Juan A. Hermoso, Marian T. Stankovich, Isabel Nogués, Tomás Mayoral, Merche Faro, Gordon Tollin, Carlos Gómez-Moreno, Marta Martínez-Júlvez, John K. Hurley
Publikováno v:
Journal of Biological Chemistry. 276:27498-27510
In the ferredoxin-NADP(+) reductase (FNR)/ferredoxin (Fd) system, an aromatic amino acid residue on the surface of Anabaena Fd, Phe-65, has been shown to be essential for the electron transfer (ET) reaction. We have investigated further the role of h
Autor:
Alejandra Luquita, Tomás Mayoral, Julia Sanz-Aparicio, Jesús Tejero, Milagros Medina, Carlos Gómez-Moreno, Koert Grever, Juan A. Hermoso
Publikováno v:
Journal of Biological Chemistry. 276:11902-11912
On the basis of sequence and three-dimensional structure comparison between Anabaena PCC7119 ferredoxin-NADP(+) reductase (FNR) and other reductases from its structurally related family that bind either NADP(+)/H or NAD(+)/H, a set of amino acid resi
Publikováno v:
Proteins: Structure, Function, and Genetics. 38:60-69
The three-dimensional crystal structure of the Glu301Ala site-directed mutant of ferredoxin-NADP+ reductase from Anabaena PCC 7119 has been determined at 1.8A resolution by x-ray diffraction. The overall folding of the Glu301Ala FNR mutant shows no s