Denise Aparecida Berti, Ph.D.

Senior Research Staff Scientist

I received my Ph.D. in 2010 under the supervision of Dr. Emer S. Ferro at the University of São Paulo, Brazil, studying mechanisms of intracellular peptide signaling in a model of insulin resistance and obesity in rats. In 2010, I joined the lab of Dr. Deborah Schechtman as a postdoctoral fellow at the Biochemistry Department of the University of São Paulo. My research focus was signaling pathways mediated by protein kinase C (PKC), specifically trying to elucidate the regulation of self-renewal of embryonic stem cells (ESC) by this family of kinase. In 2013, I moved to Israel as a visiting scientist at the Weizmann Institute of Science to start a collaboration with Dr. Rony Seger. The primary goal of this collaboration was to deepen my knowledge and gain new insights into the nuclear translocation of MAP kinases and their role on pluripotency and self-renewal of ESC. Considering my knowledge and experience with ESC, I decided to take on the challenge to explore my skills in the field of regenerative medicine. Therefore, in 2016 I joined Kadimastem, an Israel-based biotech company that was founded by Dr. Michel Revel. In this new role, I had the opportunity to be a part of the R&D team on diabetes, which focused on hESC differentiation to insulin-producing cells for cell therapy. In 2020, I joined Dr. Maike Sander’s lab as a senior research staff scientist where I am leading studies on ESC-derived beta cells to understand the pathogenesis of diabetes.


Berti DA, Seger R. (2017). The nuclear translocation of ERK. Methods Mol Biol. 1487:175-194.

Qvit N, Schechtman D, Pena DA, Berti DA, Soares CO, Miao Q, Liang LA, Baron LA, Teh-Poot C, Martínez-Vega P, Ramirez-Sierra MJ, Churchill E, Cunningham AD, Malkovskiy AV, Federspiel NA, Gozzo FC, Torrecilhas AC, Manso Alves MJ, Jardim A, Momar N, Dumonteil E, Mochly-Rosen D. (2016). Scaffold proteins LACK and TRACK as potential drug targets in kinetoplastid parasites: Development of inhibitors. Int J Parasitol Drugs Drug Resist. 6: 74-84.

Plotnikov A, Flores K, Maik-Rachline G, Zehorai E, Kapri-Pardes E, Berti DA, Hanoch T, Besser MJ, Seger R. (2015). The nuclear translocation of ERK1/2 as an anticancer target. Nat Commun. 6:6685.

Duarte ML, Pena DA, Nunes Ferraz FA, Berti DA, Paschoal Sobreira TJ, Costa-Junior HM, Abdel Baqui MM, Disatnik MH, Xavier-Neto J, Lopes de Oliveira PS, Schechtman D. (2014). Protein folding creates structure-based, noncontiguous consensus phosphorylation motifs recognized by kinases. Sci Signal. 7:1-8.

Berti DA, Russo LC, Castro LM, Cruz L, Gozzo FC, Heimann JC, Lima FB, Oliveira AC, Andreotti S, Prada PO, Heimann AS, Ferro ES. (2012). Identification of intracellular peptides in rat adipose tissue: Insights into insulin resistance. Proteomics. 12:2668-2681.

Costa-Junior HM, Garavello NM, Duarte ML, Berti DA, Glaser T, de Andrade A, Labate CA, Ferreira AT, Perales JE, Xavier-Neto J, Krieger JE, Schechtman D. (2010). Phosphoproteomics profiling suggests a role for nuclear βΙPKC in transcription processes of undifferentiated murine embryonic stem cells. J Proteome Res. 9:6191-6206.

Castro LM, Berti DA, Russo LC, Coelho V, Gozzo FC, Oliveira V, Ferro ES. (2010). Similar intracellular peptide profile of TAP1/β2 microglobulin double-knockout mice and C57BL/6 wild-type mice as revealed by peptidomic analysis. AAPS J. 12:608-616.

Berti DA, Morano C, Russo LC, Castro LM, Cunha FM, Zhang X, Sironi J, Klitzke CF, Ferro ES, Fricker LD. (2009). Analysis of intracellular substrates and products of thimet oligopeptidase in human embryonic kidney 293 cells. J Biol Chem. 284:14105-14116.

Cunha FM, Berti DA, Ferreira ZS, Klitzke CF, Markus RP, Ferro ES. (2008). Intracellular peptides as natural regulators of cell signaling. J Biol Chem. 283:24448-24459.

Machado MF, Cunha FM, Berti DA, Heimann AS, Klitzke CF, Rioli V, Oliveira V, Ferro ES. (2006). Substrate phosphorylation affects degradation and interaction to endopeptidase 24.15, neurolysin, and angiotensin-converting enzyme. Biochem Biophys Res Commun. 339:520-525.