Directorio de personas
Jordi Tamarit Sumalla

Jordi Tamarit Sumalla

Grado: Doctor/a

973 702 475
jordi.tamarit(ELIMINAR)@udl.cat

ResearcherID: http://www.researcherid.com/rid/C-6316-2008

Publicaciones

  • Echave, P; Esparza-Ceron, MA; Cabiscol, E; Tamarit, J; Ros, J; Membrillo-Hernandez, J; Lin, ECC

    DnaK dependence of mutant ethanol oxidoreductases evolved for aerobic function and protective role of the chaperone against protein oxidative damage in Escherichia coli.

    PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 99 4626-4631. .

    [doi:10.1073/pnas.072504199]

  • Rodriguez-Manzaneque, MT; Tamarit, J; Belli, G; Ros, J; Herrero, E

    Grx5 is a mitochondrial glutaredoxin required for the activity of iron/sulfur enzymes.

    MOLECULAR BIOLOGY OF THE CELL 13 1109-1121. .

    [doi:10.1091/mbc.01-10-0517]

  • Belli, G; Rodriguez-Manzaneque, MT; Torres, J; Tamarit, J; Ros, J; Herrero, E

    Characterisation of essential residues for the activity of the Saccharomyces cerevisiae Grx5 monothiol glutaredoxin.

    YEAST 18 171-171. .

  • Rodriguez-Manzaneque, MT; Tamarit, J; Belli, G; de la Torre, MA; Ros, J; Herrero, E

    The mitochondrial Grx5 glutaredoxin is involved in Fe/S cluster assembly and iron homeostasis in Saccharomyces cerevisiae.

    YEAST 18 172-172. .

  • Membrillo-Hernandez, J; Echave, P; Cabiscol, E; Tamarit, J; Ros, J; Lin, ECC

    Evolution of the adhE gene product of Escherichia coli from a functional reductase to a dehydrogenase. Genetic and biochemical studies of the mutant proteins.

    Journal Of Biological Chemistry 275 33869-33875. .

    [doi:10.1074/jbc.M005464200]

  • Tamarit, J; Gerez, C; Meier, C; Mulliez, E; Trautwein, A; Fontecave, M

    The activating component of the anaerobic ribonucleotide reductase from Escherichia coli - an iron-sulfur center with only three cysteines

    Journal Of Biological Chemistry 275 15669-15675. .

    [doi:10.1074/jbc.275.21.15669]

  • Tamarit, J; Mulliez, E; Meier, C; Trautwein, A; Fontecave, M

    The anaerobic ribonucleotide reductase from Escherichia coli - The small protein is an activating enzyme containing a [4Fe-4S](2+) center

    Journal Of Biological Chemistry 274 31291-31296. .

    [doi:10.1074/jbc.274.44.31291]

  • Lu, Z; Cabiscol, E; Obradors, N; Tamarit, J; Ros, J; Aguilar, J; Lin, ECC

    Evolution of an Escherichia coli protein with increased resistance to oxidative stress.

    Journal Of Biological Chemistry 273 8308-8316. .

    [doi:10.1074/jbc.273.14.8308]

  • Tamarit, J; Cabiscol, E; Ros, J

    Identification of the major oxidatively damaged proteins in Escherichia coli cells exposed to oxidative stress.

    Journal Of Biological Chemistry 273 3027-3032. .

    [doi:10.1074/jbc.273.5.3027]

  • Tamarit, J; Cabiscol, E; Aguilar, J; Ros, J

    Differential inactivation of alcohol dehydrogenase isoenzymes in Zymomonas mobilis by oxygen.

    Journal Of Bacteriology 179 1102-1104. .

Proyectos

  • FI-SDUR
  • Alteraciones moleculares en el modelo murino FXNI151F de Ataxia de Friedreich y análisis de nuevas estrategias terapéuticas
  • Uncovering the function of a conserved site in eukaryotic frataxins.
  • Mecanismos de disfuncion mitocondrial y nuevas estrategias terapéuticas en modelos celulares y animales de Ataxia de Friedreich
  • Nuevo fármaco dirigido a la Ataxia de Friedreich
  • Targeting mitochondria in Friedreich Ataxia: molecular mechanisms and therapeutic approaches
  • MODELOS CELULARES DE ATAXIA DE FRIEDREICH: BASES MOLECULARES DE LA PATOLOGIA E IDENTIFICACION DE BIOMARCADORES Y COMPUESTOS CON POTENCIAL TERAPEUTICO
  • Modelos celulares de ataxia de Friedreich: bases moleculares de la patología e identificación de biomarcadores y compuestos con potencial terapéutico
  • PATHOPHYSIOLOGY AND THERAPEUTICS OF FRIENDREICH ATAXIA: MARKERS OR OXIDATIVE STRESS FROM YEAST TO CARDIOMYOCYTES
  • Papel funcional del estrés oxidativo y nitrosativo en grandes sistemas biológicos.
  • Estrés oxidativo, envejecimiento celular, homeostasis del hierro y patologías relacionadas en S. cerevisae como modelo celular