* 2015: Postdoctoral fellow in Clausen Lab, Vienna, Austria
* 2014: Ph.D. dissertation: “Structural Discrimination between Activating and Repressing Response Elements in the p53 Protein Family” University of California, San Diego, USA
* 2011: M.Sc. Developing a purification scheme to extract the recombinant histone octamer from bacteria. University of California, San Diego, USA
* 2009: B.Sc. thesis: “Physicochemical Characterization of an E.coli Transporter.” National Autonomous University of Mexico, Mexico
Current research interest
Quality-control proteins work by avoiding and reverting protein misfolding and aggregation. Although extensive studies have been made to describe the way these potent machines perform their function, it is still unclear how the combination of different ATP states relates to the proteins’ conformation and their mechanism of action. Therefore, my current interests are to elucidate the mechanism by which AAA+ remodeling machines perform their function of rescuing damaged proteins from aggregated state. I will focus on Hsp104, which is a potent unfoldase and disaggregase chaperone, and its interaction with the general folding factor Hsp70. I will use structural techniques (X-ray crystallography and EM) and single-molecule biochemistry to get a better mechanistic understanding of the 104-70 interplay and its role in protein (mis)folding diseases.
Honors and Awards
* 2012- 2014: UC Mexus Fellow
* 2010- 2011: CONACYT Fellow
* 2009: Graduated with Honors from Chemistry major (UNAM)
Ciribilli Y, Monti P, Bisio A, Nguyen HT, Ethayathulla AS, Ramos A, Foggetti G, Menichini P, Menendez D, Resnick MA, Viadiu H, Fronza G, Inga A. “Transactivation specificity is conserved among p53 family proteins and depends on a response element sequence code.” Nucleic Acids Res, 2013, Vol 41, Issue 18, 8637-53.
Ramos A, Tse P-W, Wang J, Ethayathulla A, Viadiu H. “Sequence Variation in the Response Element Determines Binding by the Transcription Factor p73.” Biochemistry, 2015, in press