CV Lattes
ResearcherID
Universidade Estadual Paulista (UNESP). Campus de Araraquara. Faculdade de Ciências Farmacêuticas (FCFAR) (Institutional affiliation from the last research proposal) Birthplace: Brazil
Danuza Rossi is graduated in Biochemistry at the Pharmacy Faculty of Pharmaceutical Sciences, Univ Estadual Paulista Julio de Mesquita Filho - UNESP. Danuza has experience in Microbiology, Molecular and Cellular Biology of Microorganisms and Biochemistry, with emphasis in Saccharomyces cerevisiae genetics. She concluded her PhD in March 2013 with the doctoral degree in Biociênicasand Biotechnology applied to Pharmacy, and thee hesis was entitled "Study of the Initiation Factor Eukaryotic Translation 5A (eIF5A) in translation and in connection with specific ribosome". Danuza developed her PhD studies in the laboratory of Molecular and Cellular Biology of Microrganisms at UNESP, Araraquara (FAPESP fellowship) and laboratory of Molecular Biology and Biochemistry at Univ of California, Davis (CAPES fellowship). Since May/2013, she is post-doc at UNESP under supervision of the Prof. Dr. Sandro R. Valentini, developing the project "Study of biochemical and kinetic direct physical interaction between eIF5A and the ribosome of Saccharomyces cerevisiae and human" (FAPESP 2012/23890-9). In 2014, she stayed at the Univ of California, Davis, in the collaborators lab to study the "Biochemical and kinetic study of eIF5A ribosome and direct interaction , using Saccharomyces cerevisiae and the human models" (FAPESP 2013/16744-9) under the supervision of Prof. Dr. Christopher Fraser. (Source: Lattes Curriculum)
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The translation initiation factor 5A (eIF5A) is highly conserved in archaea and eukaryotes and is essential for cell viability. This is the only known protein containing the amino acid hypusine, essential for the function of eIF5A and it is generated in a post-translational modification. After being extensively involved in several cellular processes, only recently it was better determined…
The translation factor 5A (eIF5A) is highly conserved in Archaea and eukaryotes and is essential for cell viability. This is the only protein known to contain the amino acid residue hypusine, essential for eIF5A function, generated by a post-translational modification. Although eIF5A has been extensively involved in several cellular processes, it was only recently determined a role for eI…
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