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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Nelson Carvajal

Departamento de Biología Molecular

Facultad de Ciencias Biológicas

Universidad de Concepción

Casilla 160-C



Name/email consistency: high



  • Departamento de Biología Molecular, Facultad de Ciencias Biológicas, Universidad de Concepción, Casilla 160-C, Chile. 1999 - 2004


  1. Inactivation of human liver arginase by Woodward's reagent K: evidence for reaction with His141. Carvajal, N., Uribe, E., López, V., Salas, M. Protein J. (2004) [Pubmed]
  2. Non-chelating inhibition of the H101N variant of human liver arginase by EDTA. Carvajal, N., Orellana, M.S., Bórquez, J., Uribe, E., López, V., Salas, M. J. Inorg. Biochem. (2004) [Pubmed]
  3. Kinetic studies and site-directed mutagenesis of Escherichia coli agmatinase. A role for Glu274 in binding and correct positioning of the substrate guanidinium group. Carvajal, N., Orellana, M.S., Salas, M., Enríquez, P., Alarcón, R., Uribe, E., López, V. Arch. Biochem. Biophys. (2004) [Pubmed]
  4. Manganese is essential for catalytic activity of Escherichia coli agmatinase. Carvajal, N., López, V., Salas, M., Uribe, E., Herrera, P., Cerpa, J. Biochem. Biophys. Res. Commun. (1999) [Pubmed]
  5. Evidence that histidine-163 is critical for catalytic activity, but not for substrate binding to Escherichia coli agmatinase. Carvajal, N., Olate, J., Salas, M., López, V., Cerpa, J., Herrera, P., Uribe, E. Biochem. Biophys. Res. Commun. (1999) [Pubmed]
  6. Chemical modification and site-directed mutagenesis of human liver arginase: evidence that the imidazole group of histidine-141 is not involved in substrate binding. Carvajal, N., Olate, J., Salas, M., Uribe, E., López, V., Herrera, P., Cerpa, J. Arch. Biochem. Biophys. (1999) [Pubmed]
  7. Manganese-dependent inhibition of human liver arginase by borate. Carvajal, N., Salas, M., López, V., Uribe, E., Herrera, P., Cerpa, J., Fuentes, M. J. Inorg. Biochem. (1999) [Pubmed]
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