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Coauthors
Lucía Citores Department of Biochemistry and Molecular Biology and Physiology, Faculty of Sciences, University of Valladolid, Spain
1 protocol

José Ferreras Department of Biochemistry and Molecular Biology and Physiology, Faculty of Sciences, University of Valladolid, Spain
1 protocol

José M. Ferreras
  • Department of Biochemistry and Molecular Biology and Physiology, Faculty of Sciences, University of Valladolid, Spain
  • 1 Author merit

Education

Ph.D in Biochemistry, Department of Biochemistry and Molecular Biology and Physiology, University of Valladolid, Spain, 1989

Current position

Professor in Biochemistry and Molecular Biology, Department of Biochemistry and Molecular Biology and Physiology, University of Valladolid, Spain

Publications (since 2010)

  1. Ferreras, J. M., Ragucci, S., Citores, L., Iglesias, R., Pedone, P. V. and Di Maro, A. (2016). Insight into the phylogenetic relationship and structural features of vertebrate myoglobin family. Int J Biol Macromol 93(Pt A): 1041-1050.
  2. Iglesias, R., Citores, L., Ragucci, S., Russo, R., Di Maro, A. and Ferreras, J. M. (2016). Biological and antipathogenic activities of ribosome-inactivating proteins from Phytolacca dioica L. Biochim Biophys Acta 1860(6): 1256-1264.
  3. Citores, L., Iglesias, R., Gay, C. and Ferreras, J. M. (2016). Antifungal activity of the ribosome-inactivating protein BE27 from sugar beet (Beta vulgaris L.) against the green mould Penicillium digitatum. Mol Plant Pathol 17(2): 261-271.
  4. Iglesias, R., Citores, L., Di Maro, A. and Ferreras, J. M. (2015). Biological activities of the antiviral protein BE27 from sugar beet (Beta vulgaris L.). Planta 241(2): 421-433.
  5. Di Maro, A., Citores, L., Russo, R., Iglesias, R. and Ferreras, J. M. (2014). Sequence comparison and phylogenetic analysis by the Maximum Likelihood method of ribosome-inactivating proteins from angiosperms. Plant Mol Biol 85(6): 575-588.
  6. Munoz, R., Arias, Y., Ferreras, J. M., Jimenez, P., Langa, C., Rojo, M. A., Gayoso, M. J., Cordoba-Diaz, D., Bernabeu, C. and Girbes, T. (2013). In vitro and in vivo effects of an anti-mouse endoglin (CD105)-immunotoxin on the early stages of mouse B16MEL4A5 melanoma tumours. Cancer Immunol Immunother 62(3): 541-551.
  7. Citores, L., Iglesias, R. and Ferreras, J. M. (2013). Ribosome inactivating proteins from plants: biological properties and their use in experimental therapy. In: Fang, E. F. and Ng, T. B. (Eds). Antitumor Potential and Other Emerging Medicinal Properties of Natural Compounds. Springer, 127-143.
  8. Munoz, R., Arias, Y., Ferreras, J. M., Jimenez, P., Rojo, M. A., Bernabeu, C., Cordoba-Diaz, D. and Girbes, T. (2012). Transient injury-dependent up-regulation of CD105 and its specific targeting with an anti-vascular anti-mouse endoglin-nigrin b immunotoxin. Med Chem 8(6): 996-1002.
  9. Ferreras, J. M., Citores, L., Iglesias, R., Jimenez, P. and Girbes, T. (2011). Use of ribosome-inactivating proteins from Sambucus for the construction of immunotoxins and conjugates for cancer therapy. Toxins (Basel) 3(5): 420-441.
  10. Ferreras, J. M., Citores, L., Iglesias, R., Jiménez, P., Souza, A. M., Gayoso, M. J. and Girbés, T. (2011). Occurrence and new procedure of preparation of nigrin, an antiribosomal lectin present in elderberry bark. Food Res Int 44(9): 2798–2805.
  11. Iglesias, R., Citores, L., Ferreras, J. M., Perez, Y., Jimenez, P., Gayoso, M. J., Olsnes, S., Tamburino, R., Di Maro, A., Parente, A. and Girbes, T. (2010). Sialic acid-binding dwarf elder four-chain lectin displays nucleic acid N-glycosidase activity. Biochimie 92(1): 71-80.
  12. Ferreras, J. M., Citores, L., Iglesias, R., Jiménez, P. and Girbes, T. (2010). Sambucus Ribosome-Inactivating Proteins and Lectins. In: Lord, J. M. and Hartley, M. R. (Eds). Toxic Plant Proteins, Plant Cell Monographs. Springer, 18: 107-131.
1 Protocol published
Ribosomal RNA N-glycosylase Activity Assay of Ribosome-inactivating Proteins
Authors:  Rosario Iglesias, Lucía Citores and José M. Ferreras, date: 03/20/2017, view: 2125, Q&A: 0
Ribosome-inactivating proteins (RIPs) are enzymes that irreversibly inactivate ribosomes as a consequence of their N-glycosylase (EC 3.2.2.22) activity. The enzyme cleaves the N-glycosidic bond between the adenine No. 4324 from the 28S rRNA and its ...