Department of Internal Medicine

Cardiovascular Medicine Faculty


Paloma Giangrande, Ph.D.

Graduate School:
Duke University

Postdoctoral Fellowship:
Howard Hughes Medical Institute,
Duke University Medical School

Paloma H. Giangrande, Ph.D.
Assistant Professor

Dr. Giangrande's research interests include developing RNA-based therapeutics to modulate cellular pathways underlying pathological cell proliferation in the setting of cancer and cardiovascular disease. One area of Dr. Giangrande’s lab focuses on selecting RNA aptamers to receptors expressed on the surface of target-cells with SELEX (Systemic Evolution of Ligands by EXponential Enrichment) for the purpose of 1) modulating receptor function and/or 2) delivering therapeutic molecules (e.g. siRNAs, antagomirs, drugs) into specific cell types. A second interest of the Giangrande lab is to use genomic/proteomic methodologies to acquire important insights into the mechanisms of pathological cell proliferation. In addition to providing useful mechanistic information, this knowledge will be used to identify novel membrane proteins that can be targeted with therapeutic RNAs for treating cancer or pathological vascular hyperplasia.

Honors, Awards, and Organizations

Recent Publications

  1. McNamara, J.O. 2nd, Andrechek, E.R., Wang, Y., Viles, K.D., Rempel, R.E., Gilboa, E., Sullenger, B.A., Giangrande, P.H. Cell type-specific delivery of siRNAs with aptamer-siRNA chimeras. Nat Biotechnol. 24(8):1005-15, 2006.
  2. Mi, J., Zhang, X., Giangrande, P.H., McNamara, J.O. 2nd, Nimjee, S.M., Sarraf-Yazdi, S., Sullenger, B.A., Clary, B.M. Targeted inhibition of alphavbeta3 integrin with an RNA aptamer impairs endothelial cell growth and survival. Biochem Biophys Res Commun. 338(2):956-63, 2005.
  3. Zhu, W., Giangrande, P.H., Nevins, J.R.. Temporal control of cell cycle gene expression mediated by E2F transcription factors. Cell Cycle. 4(5):633-6, 2005.
  4. Giangrande, P.H., Zhu, W., Schlisio, S., Sun, X., Mori, S., Gaubatz, S., Nevins, J.R. A role for E2F6 in distinguishing G1/S- and G2/M-specific transcription. Genes Dev. 18(23):2941-51, 2004.
  5. Zhu, W., Giangrande, P.H., Nevins, J.R. E2Fs link the control of G1/S and G2/M transcription. EMBO J. 23(23):4615-26, 2004.
  6. Giangrande, P.H., Zhu, W., Rempel, R.E., Laakso, N., Nevins, J.R. Combinatorial gene control involving E2F and E Box family members. EMBO J. 23(6):1336-47, 2004.
  7. Giangrande, P.H., Hallstrom, T.C., Tunyaplin, C., Calame, K., Nevins, J.R. Identification of E-box factor TFE3 as a functional partner for the E2F3 transcription factor. Mol Cell Biol. 23(11):3707-20, 2003.
  8. Wu, L., Timmers, C., Maiti, B., Saavedra, H.I., Sang, L., Chong, G.T., Nuckolls, F., Giangrande, P., Wright, F.A., Field, S.J., Greenberg, M.E., Orkin, S., Nevins, J.R., Robinson, M.L., Leone, G. The E2F1-3 transcription factors are essential for cellular proliferation. Nature. 414(6862):457-62, 2001.
  9. Leone, G., Sears, R., Huang, E., Rempel, R., Nuckolls, F., Park, C.H., Giangrande, P., Wu, L., Saavedra, H.I., Field, S.J., Thompson, M.A., Yang, H., Fujiwara, Y., Greenberg, M.E., Orkin, S., Smith, C., Nevins, J.R. Myc requires distinct E2F activities to induce S phase and apoptosis. Mol Cell. 8(1):105-13, 2001.
  10. Giangrande, P.H., Kimbrel, E.A., Edwards, D.P., McDonnell, D.P. The opposing transcriptional activities of the two isoforms of the human progesterone receptor are due to differential cofactor binding. Mol Cell Biol. 20(9):3102-15, 2000.
  11. Giangrande, P.H., McDonnell, D.P. The A and B isoforms of the human progesterone receptor: two functionally different transcription factors encoded by a single gene. Recent Prog Horm Res. 54:291-313, 1999. Review.
  12. Tetel, M.J., Giangrande, P.H., Leonhardt, S.A., McDonnell, D.P., Edwards, D.P. Hormone-dependent interaction between the amino- and carboxyl-terminal domains of progesterone receptor in vitro and in vivo. Mol Endocrinol. 13(6):910-24, 1999.
  13. Giangrande, P.H., Pollio, G., McDonnell, D.P. Mapping and characterization of the functional domains responsible for the differential activity of the A and B isoforms of the human progesterone receptor. J Biol Chem. 272(52):32889-900, 1997.

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