Anna Rodina, PhD

Senior Research Scientist
Anna Rodina, PhD

Lab Phone


My research interests are broad and include areas in basic and translational oncology research. I have a broad background in cancer biology and biochemistry with a specific training and expertise in evaluation of chemical tools in in vitro and in vivo systems. As a postdoctoral fellow at Colorado University Health Sciences Center I have been analyzing molecular mechanisms of gap junction protein involvement in carcinogenesis using molecular genetics methods and transgenic mice models. At New York University Medical Center I expanded my expertise in biochemistry studying an individual protein activity in a purified system. Being at Memorial Sloan Kettering Cancer Center, I have extended my expertise to drug discovery by developing selectivity- and phenotypical assays for chaperome inhibitors and studying chaperome biology in cancer and neurodegenerative diseases using these tools. My efforts have resulted in multiple publications and patent applications.

My major focus is to study the biochemical and functional mechanism behind the epichaperome, and to investigate the translational significance of epichaperome multi-protein complexes in cancer. Towards this goal, I studied the mechanisms behind the formation of the complex and its role in the sensitivity of tumors to HSP90 inhibitors. Specifically, I have developed methods to identify and characterize the epichaperome complex, and I have investigated mechanisms associated with epichaperome formation. Another way to inhibit epichaperome networks in cancer is through targeting HSP70. Towards this goal we have discovered an inhibitor of a previously unknown allosteric HSP70 site, YK5. Derivatives of this compounds have been made by my chemistry colleagues to identify those that are potent and selective binders of HSP70 epichaperomes. This generation of inhibitors represents a viable starting point for the development of novel anticancer therapeutics; high potency agents are now on the way to clinical translation. I am deeply involved in the investigation of these agents, of their mechanism of action and in the development of strategies for their rational translation to clinic.



  1. Rodina, A.; Wang, T.; Yan, P.; Gomes, E. D.; Dunphy, M. P.; Pillarsetty, N.; Koren, J.; Gerecitano, J. F.; Taldone, T.; Zong, H.; Caldas-Lopes, E.; Alpaugh, M.; Corben, A.; Riolo, M.; Beattie, B.; Pressl, C.; Peter, RI.; Xu, C.; Trondl, R.; Patel, HJ.; Shimizu, F.; Bolaender, A.; Yang, C.; Panchal, P.; Farooq, MF.; Kishinevsky, S.; Modi, S.; Lin, O.; Chu, F.; Patil, S.; Erdjument-Bromage, H.; Zanzonico, P.; Hudis, C.; Studer, L.; Roboz, GJ.; Cesarman, E.; Cerchietti, L.; Levine, R.; Melnick, A.; Larson, SM.; Lewis, JS.; Guzman, ML.; Chiosis, G. The epichaperome is an integrated chaperome network that facilitates tumour survival. Nature 2016, 538(7625):397-401.
  2. Kishinevsky S, Wang T, Rodina A, Chung SY, Xu C, Philip J, Taldone T, Joshi S, Alpaugh ML, Bolaender A, Gutbier S, Sandhu D, Fattahi F, Zimmer B, Shah SK, Chang E, Inda C, Koren J 3rd, Saurat NG, Leist M, Gross SS, Seshan VE, Klein C, Tomishima MJ, Erdjument-Bromage H, Neubert TA, Henrickson RC, Chiosis G*, Studer L*. HSP90-incorporating chaperome networks as biosensor for disease-related pathways in patient-specific midbrain dopamine neurons. Nat Commun. 2018 Oct 19;9(1):4345. doi: 10.1038/s41467-018-06486-6.
  3. Giulino-Roth L, van Besien HJ, Dalton T, Totonchy JE, Rodina A, Taldone T, Bolaender A, Erdjument-Bromage H, Sadek J, Chadburn A, Barth MJ, Dela Cruz FS, Rainey A, Kung AL, Chiosis G, Cesarman E. Inhibition of Hsp90 Suppresses PI3K/AKT/mTOR Signaling and Has Antitumor Activity in Burkitt Lymphoma. Mol Cancer Ther. 2017 Sep;16(9):1779-1790.
  4. Rodina, A.; Taldone, T.; Kang, Y.; Patel, PD.; Koren, J 3rd; Yan, P.; DaGama Gomes, EM.; Yang, C.; Patel, MR.; Shrestha, L.; Ochiana, SO.; Santarossa, C.; Maharaj, R.; Gozman, A.; Cox, MB.; Erdjument-Bromage, H.; Hendrickson, RC.; Cerchietti, L.; Melnick, A.; Guzman, ML.; Chiosis, G. Affinity purification probes of potential use to investigate the endogenous Hsp70 interactome in cancer. ACS Chem Biol. 2014, 9(8):1698-705.
  5. Taldone, T.; Kang, Y.; Patel, HJ.; Patel, MR.; Patel, PD.; Rodina, A.; Patel, Y.; Gozman, A.; Maharaj, R.; Clement, CC.; Lu, A.; Young, JC.; Chiosis, G. Heat shock protein 70 inhibitors. 2. 2,5’-thiodipyrimidines, 5-(phenylthio)pyrimidines, 2-(pyridin-3-ylthio)pyrimidines, and 3-(phenylthio)pyridines as reversible binders to an allosteric site on heat shock protein 70. J Med Chem. 2014, 57(4):1208-24.
  6. Kang, Y.; Taldone, T.; Patel, HJ.; Patel, PD.; Rodina, A.; Gozman, A.; Maharaj, R.; Clement, CC.; Patel, MR.; Brodsky, JL.; Young, JC.; Chiosis, G. Heat shock protein 70 inhibitors. 1. 2,5’-thiodipyrimidine and 5-(phenylthio)pyrimidine acrylamides as irreversible binders to an allosteric site on heat shock protein 70. J Med Chem. 2014, 57(4):1188-207.
  7. Rodina, A.; Patel, PD.; Kang, Y.; Patel, Y.; Baaklini, I.; Wong, M.; Taldone, T.; Yan, P.; Yang, C.; Maharaj, R.; Gozman, A.; Patel, M.; Patel, H.;  Erdjument-Bromage, H.; Talele, T.; Young, JC.; and Chiosis, G. Identification of an allosteric pocket on human Hsp70 reveals a novel mode of inhibition of this therapeutically important protein . Chemistry and Biology 2013, 20(12):1469-80.
  8. Nayar, U.; Lu, P.; Goldstein, RL.; Vider, J.; Ballon, G.; Rodina, A.; Taldone, T.; Erdjument-Bromage, H.; Chomet, M.; Blasberg, R.; Melnick, A.; Cerchietti, L.; Chiosis, G.; Wang, YL.; Cesarman E. Targeting the Hsp90-associated viral oncoproteome in gammaherpesvirus-associated malignancies. Blood. 2013, 122(16):2837-47.
  9. Taldone, T.; Rodina, A.; Dagama Gomes, EM.; Riolo, M.; Patel, HJ.; Alonso-Sabadell, R.; Zatorska, D.; Patel, MR.; Kishinevsky, S.; Chiosis, G. Synthesis and evaluation of cell-permeable biotinylated PU-H71 derivatives as tumor Hsp90 probes. Beilstein J Org Chem. 2013, 9:544-56.
  10. Moulick, K.; Ahn, JH.; Zong, H.; Rodina, A.; Cerchietti, L.; Gomes DaGama, E.; Caldas-Lopes, E.; Beebe, K.; Perna, F.; Hatzi, K.; Vu, LP.; Zhao, X.; Zatorska, D.; Taldone, T.; Smith-Jones, P.; Alpaugh, M.; Gross, SS.; Pillarsetty, N.; Ku, T.; Lewis, JS.; Larson, SM.; Levine, R.; Erdjument-Bromage, H.; Guzman, M.; Nimer, SD.; Melnick, A.; Neckers, L.; Chiosis, G. Affinity-based proteomics reveal cancer-specific networks coordinated by Hsp90. Nature Chem Biol 2011, 7(11):818-26.
  11. Marubayashi, S.; Koppikar, P.; Taldone, T.; Abdel-Wahab, O.; West, N.; Bhagwat, N.; Caldas-Lopes, E.; Ross, KN.; Gönen, M.; Gozman, A.; Ahn, JH.; Rodina, A.; Ouerfelli, O.; Yang, G.; Hedvat, C.; Bradner, JE.; Chiosis, G.; Levine, RL. HSP90 is a therapeutic target in JAK2-dependent myeloproliferative neoplasms in mice and humans. J Clin Invest. 2010, 120(10):3578-93.
  12. Caldas-Lopes, E.; Cerchietti, L.; Ahn, JH.; Clement, CC.; Robles, AI.; Rodina, A.; Moulick, K.; Taldone, T.; Gozman, A.; Guo, Y.; Wu, N.; de Stanchina, E.; White, J.; Gross, SS.; Ma, Y.; Varticovski, L.; Melnick, A.; Chiosis, G. Hsp90 inhibitor PU-H71, a multimodal inhibitor of malignancy, induces complete responses in triple-negative breast cancer models. PNAS 2009, 106(20):8368-8373.
  13. Luo, W.; Dou, F.; Rodina, A.; Chip, S.; Kim, J.; Zhao, Q.; Moulick, K.; Aguirre, J.; Wu, N.; Greengard, P. and Chiosis, G. Roles of heat-shock protein 90 in maintaining and facilitating the neurodegenerative phenotype in tauopathies. PNAS 2007, 104(22):9511-9516.
  14. Rodina, A.; Vilenchik, M.; Moulick, K.; Aguirre, J.; Kim, J.; Chiang, A.; Litz, J.; Clement, C.; Kang, Y.; She, Y.; Wu, N.; Felts, S.; Wipf, P.; Massague, J.; Jiang, X.; Brodsky, J.; Krystal, G. and Chiosis, G. Selective compounds define Hsp90 as a major inhibitor of apoptosis in small-cell lung cancer. Nature Chem Biol 2007, 3(8):498-507.