Adriana Firooznia, Ph.D.
- Biochemistry Lecture (BCHM 4115)
- Biochemistry Laboratory (BCHM 4115L)
- Seminar in Chemistry (CHEM 4908)
- Principles of Organic Chemistry Lecture and Laboratory (CHEM 2180)
- General Chemistry I Lecture and Laboratory (CHEM 1083)
- Essentials of Chemistry Lecture and Laboratory (CHEM 1030)
- Preparatory Chemistry Lecture and Laboratory (CHEM 1010)
- Chemistry in Your World (CHEM 1200)
An understanding of basic chemistry and biochemistry is important throughout the lifetime of anyone since chemical principles help one understand issues related to human health, medicine, natural resources and environmental problems. In addition, learning chemistry brings about an appreciation for the numerous chemical commodities ubiquitously used around us. My ultimate goal as an educator is not only to foster the thirst for knowledge but more importantly to encourage the students to use critical observation and analytical thinking in order to see the future goals and possibilities of scientific endeavors beyond the present state.
Vasileva, A.; Tiedau, D.; Firooznia, A.; Müller-Reichert, T.; Jessberger, R. Tdrd6 is required for spermiogenesis, chromatoid body architecture, and regulation of miRNA expression. Curr Biol (2009), 19(8), 630-639.
Sevcik, J.; Hostinová, E.; Solovicová, A.; Gašperík, J.; Dauter, Z.; Wilson, K. S. Structure of the complex of a yeast glucoamylase with acarbose reveals the presence of a raw starch binding site on the catalytic domain. FEBS Journal (2006), 273(10), 2161-2171.
Firooznia, A., Revenkova, E., and Jessberger R. The function of SMC and other cohesin proteins in meiosis. Journal of Andrology (2005), 26(1), 1-10.
Solovicová, A., Christensen, T., Hostinová, E., Gašperík, J., Ševčík, J., and Svensson B. Structure-function relationships in glucoamylases encoded by variant Saccharomycopsis fibuligera genes. Eur. J. Biochem. (1999), 264, 756-764.
Solovicová, A., Gašperík, J., and Hostinová E. High-yield production of Saccharomycopsis fibuligera glucoamylase in Escherichia coli, refolding, and comparison of the nonglycosylated and glycosylated enzyme forms. Biochem. Biophys. Res. Comm. (1996), 224, 790-795.