Education

Ph.D. in Biology University of Valencia,1982

Current position

Professor, Dept. Biochemistry and Molecular Biology, Faculty of Biology, University of Valencia

Publications (since 2005)

1. Sudhani, H. P. and Moreno, J. (2015). Control of the ribulose 1,5-bisphosphate carboxylase/oxygenase activity by the chloroplastic glutathione pool. Arch Biochem Biophys 567: 30-34.
   
2. Penarrubia, L., Romero, P., Carrio-Segui, A., Andres-Borderia, A., Moreno, J. and Sanz, A. (2015). Temporal aspects of copper homeostasis and its crosstalk with hormones. Front Plant Sci 6: 255.
   
3. Sudhani, H. P., Garcia-Murria, M. J. and Moreno, J. (2013). Reversible inhibition of CO₂ fixation by ribulose 1,5-bisphosphate carboxylase/oxygenase through the synergic effect of arsenite and a monothiol. Plant Cell Environ 36(6): 1160-1170.
   
4. Alic, A., Perez-Ortin, J. E., Moreno, J. and Arnau, V. (2013). mRNAStab--a web application for mRNA stability analysis. Bioinformatics 29(6): 813-814.
   
5. Perez-Ortin, J. E., Medina, D. A., Chavez, S. and Moreno, J. (2013). What do you mean by transcription rate?: the conceptual difference between nascent transcription rate and mRNA synthesis rate is essential for the proper understanding of transcriptomic analyses. Bioessays 35(12): 1056-1062.
   
6. Castells-Roca, L., Garcia-Martinez, J., Moreno, J., Herrero, E., Belli, G. and Perez-Ortin, J. E. (2011). Heat shock response in yeast involves changes in both transcription rates and mRNA stabilities. PLoS One 6(2): e17272.
   
7. Marín-Navarro, J., Jauhiainen, A., Moreno, J., Alepuz, P., Pérez-Ortín, J. E. and Sunnerhagen, P. (2011). Global estimation of mRNA stability in yeast. Yeast Genetic Networks, Springer: 3-23.
   
8. Penarrubia, L., Andres-Colas, N., Moreno, J. and Puig, S. (2010). Regulation of copper transport in Arabidopsis thaliana: a biochemical oscillator? J Biol Inorg Chem 15(1): 29-36.
   
9. Marín‐Navarro, J., García‐Murria, M. J. and Moreno, J. (2010). REDOX PROPERTIES ARE CONSERVED IN RUBISCOS FROM DIATOMS AND GREEN ALGAE THROUGH A DIFFERENT PATTERN OF CYSTEINES1. Journal of Phycology 46(3): 516-524.
   
10. Marín-Navarro, J., Esquivel, M. G. and Moreno, J. (2010). Hydrogen production by Chlamydomonas reinhardtii revisited: Rubisco as a biotechnological target. World Journal of Microbiology and Biotechnology 26(10): 1785-1793.
    
11. Romero-Santacreu, L., Moreno, J., Perez-Ortin, J. E. and Alepuz, P. (2009). Specific and global regulation of mRNA stability during osmotic stress in Saccharomyces cerevisiae. RNA 15(6): 1110-1120.
    
12. Molina-Navarro, M. M., Castells-Roca, L., Belli, G., Garcia-Martinez, J., Marin-Navarro, J., Moreno, J., Perez-Ortin, J. E. and Herrero, E. (2008). Comprehensive transcriptional analysis of the oxidative response in yeast. J Biol Chem 283(26): 17908-17918.
    
13. Garcia-Murria, M. J., Karkehabadi, S., Marin-Navarro, J., Satagopan, S., Andersson, I., Spreitzer, R. J. and Moreno, J. (2008). Structural and functional consequences of the replacement of proximal residues Cys(172) and Cys(192) in the large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase from Chlamydomonas reinhardtii. Biochem J 411(2): 241-247.
    
14. Moreno, J., Garcia-Murria, M. J. and Marin-Navarro, J. (2008). Redox modulation of Rubisco conformation and activity through its cysteine residues. J Exp Bot 59(7): 1605-1614.
    
15. Perez-Ortin, J. E., Alepuz, P. M. and Moreno, J. (2007). Genomics and gene transcription kinetics in yeast. Trends Genet 23(5): 250-257.
    
16. Marin-Navarro, J. and Moreno, J. (2006). Cysteines 449 and 459 modulate the reduction-oxidation conformational changes of ribulose 1.5-bisphosphate carboxylase/oxygenase and the translocation of the enzyme to membranes during stress. Plant Cell Environ 29(5): 898-908.
    
17. Esquivel, M. G., Pinto, T. S., Marin-Navarro, J. and Moreno, J. (2006). Substitution of tyrosine residues at the aromatic cluster around the betaA-betaB loop of rubisco small subunit affects the structural stability of the enzyme and the in vivo degradation under stress conditions. Biochemistry 45(18): 5745-5753.