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Hagit Eldar-Finkelman

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Hagit Eldar-Finkelman
Prof. Hagit Eldar-Finkelman - Tel Aviv University - (August 2021)
Born1960
Jerusalem, Israel
CitizenshipIsraeli
Alma materHebrew University of Jerusalem, Weizmann Institute of Science
Known forThe pioneering work on the functions of GSK-3 and generation of novel GSK-3 inhibitors
AwardsBritish Council Award, American Heart Association award, Joslin Diabetes Center Fellowship
Scientific career
FieldsBiological NMR, Cellular signaling, Diabetes
InstitutionsTel Aviv University
Doctoral advisorEtta Livneh

Hagit Eldar-Finkelman (Hebrew: חגית אלדר-פינקלמן) is an Israeli scientist and a principal investigator of an active research laboratory at the Sackler School of Medicine at Tel Aviv University.[1][2] Eldar-Finkelman’s research is focused on the signal transduction field and drug development targeting protein kinases. She is well known for her pioneering work on the functions of GSK-3 and its contribution to diabetes[3][4] and other pathogenies, including depressive behavior,[5] Alzheimer’s diseases,[6][7] and Huntington’s diseases.[8] Novel findings also include the unique evolution of GSK-3 isozymes.[9] Eldar-Finkelman is a leading figure in developing novel substrate competitive inhibitors (SCIs) for GSK-3 with significant benefits as drug candidates.[10]

Biography

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Born in Jerusalem, Eldar-Finkelman obtained her BSc in Chemistry at the Hebrew University of Jerusalem and her MSc in Physical Chemistry and Ph.D. in Cellular Signaling at the Weizmann Institute of Science (1993). She did Post-doctorate at the University of Washington, working with Nobel Prize Laureate Edwin G. Krebs. She was then an Assistant Professor at Harvard Medical School for two years before joining Tel Aviv University in 2000. She received several awards, including the British Council Award, American Heart Association award, Joslin Diabetes Center Fellowship, Israeli Diabetes Association Award for distinguished Scientist, and the Lindner Prize of the Israel Endocrine Society. She is a Full Professor since 2012.[1][2]

Scientific interests and publications

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The research in Eldar-Finkelman’s laboratory studies the molecular mechanisms underlying human disease, focusing on cellular signaling networks. A particular emphasis is given to discovering and developing new chemical tools for regulating protein kinases- key elements in signal transduction networks. Eldar-Finkelman is well known for her pioneering work on the protein kinase function, glycogen synthase kinase-3 (GSK-3), revealing its contribution to pathological disorders. Her pioneering work showed that GSK-3 is a negative feedback regulator of the insulin signaling pathway and showed its contribution to type 2 diabetes.[3][11] She further presented novels mechanisms linking GSK-3 with neurodegeneration and cancer via autophagy/lysosome regulation.[12] Eldar-Finkelman develops a unique (SCI strategy) strategy in generating highly selective GSK-3 inhibitors that function as competitive substrate inhibitors (SCIs).[13][14] Accordingly, a novel class of cell-permeable peptide inhibitors was developed and provided proof of concept in treating in vivo models of diabetes[11] depressive behavior,[5] Alzheimer’s disease[6][7] and Huntington’s diseases.[8] A new modality of SCI called substrate converted into an inhibitor was discovered in her laboratory. The work was selected as a breakthrough of the year in drug discovery by Science Signaling.[7] A recent new development is the design of novel small molecules based on the SCI strategy.[15] Eldar-Finkelman published over 75 peer-reviewed articles (as Hagit Eldar 1986-1995).[2]

References

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  1. ^ a b Prof. Hagit Eldar-Finkelman - Homepage, Sackler Faculty of Medicine, Tel Aviv University
  2. ^ a b c ORCID - Hagit Eldar-Finkelman
  3. ^ a b Eldar-Finkelman, H.; Krebs, E. G. (1997). "Phosphorylation of insulin receptor substrate 1 by glycogen synthase kinase 3 impairs insulin action". Proceedings of the National Academy of Sciences. 94 (18): 9660–9664. Bibcode:1997PNAS...94.9660E. doi:10.1073/pnas.94.18.9660. ISSN 0027-8424. PMC 23245. PMID 9275179.
  4. ^ Eldar-Finkelman, H.; Schreyer, S. A.; Shinohara, M. M.; LeBoeuf, R. C.; Krebs, E. G. (1999). "Increased glycogen synthase kinase-3 activity in diabetes- and obesity-prone C57BL/6J mice". Diabetes. 48 (8): 1662–1666. doi:10.2337/diabetes.48.8.1662. ISSN 0012-1797. PMID 10426388.
  5. ^ a b Kaidanovich-Beilin, Oksana; Milman, Anat; Weizman, Abraham; Pick, Chaim G; Eldar-Finkelman, Hagit (2004). "Rapid antidepressive-like activity of specific glycogen synthase kinase-3 inhibitor and its effect on β-catenin in mouse hippocampus". Biological Psychiatry. 55 (8): 781–784. doi:10.1016/j.biopsych.2004.01.008. ISSN 0006-3223. PMID 15050857. S2CID 46559956.
  6. ^ a b Avrahami, Limor; Farfara, Dorit; Shaham-Kol, Maya; Vassar, Robert; Frenkel, Dan; Eldar-Finkelman, Hagit (2013). "Inhibition of Glycogen Synthase Kinase-3 Ameliorates β-Amyloid Pathology and Restores Lysosomal Acidification and Mammalian Target of Rapamycin Activity in the Alzheimer Disease Mouse Model". Journal of Biological Chemistry. 288 (2): 1295–1306. doi:10.1074/jbc.M112.409250. ISSN 0021-9258. PMC 3543013. PMID 23155049.
  7. ^ a b c Licht-Murava, A.; Paz, R.; Vaks, L.; Avrahami, L.; Plotkin, B.; Eisenstein, M.; Eldar-Finkelman, H. (2016). "A unique type of GSK-3 inhibitor brings new opportunities to the clinic". Science Signaling. 9 (454): ra110. doi:10.1126/scisignal.aah7102. ISSN 1945-0877. PMID 27902447. S2CID 34207388.
  8. ^ a b Rippin, Ido; Bonder, Katherina; Joseph, Shirley; Sarsor, Ammar; Vaks, Lilach; Eldar-Finkelman, Hagit (2021). "Inhibition of GSK-3 ameliorates the pathogenesis of Huntington's disease". Neurobiology of Disease. 154: 105336. doi:10.1016/j.nbd.2021.105336. ISSN 0969-9961. PMID 33753290.
  9. ^ Alon, Lina Tsaadon; Pietrokovski, Shmuel; Barkan, Shay; Avrahami, Limor; Kaidanovich-Beilin, Oksana; Woodgett, James R.; Barnea, Anat; Eldar-Finkelman, Hagit (2011). "Selective loss of glycogen synthase kinase-3α in birds reveals distinct roles for GSK-3 isozymes in tau phosphorylation". FEBS Letters. 585 (8): 1158–1162. doi:10.1016/j.febslet.2011.03.025. ISSN 0014-5793. PMID 21419127.
  10. ^ Avrahami, Limor; Licht-Murava, Avital; Eisenstein, Miriam; Eldar-Finkelman, Hagit (2013). "GSK-3 inhibition: Achieving moderate efficacy with high selectivity". Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1834 (7): 1410–1414. doi:10.1016/j.bbapap.2013.01.016. ISSN 1570-9639. PMID 23369789.
  11. ^ a b Kaidanovich-Beilin, Oksana; Eldar-Finkelman, Hagit (2006). "Long-Term Treatment with Novel Glycogen Synthase Kinase-3 Inhibitor Improves Glucose Homeostasis in ob/ob Mice: Molecular Characterization in Liver and Muscle". Journal of Pharmacology and Experimental Therapeutics. 316 (1): 17–24. doi:10.1124/jpet.105.090266. ISSN 0022-3565. PMID 16169938. S2CID 6425447.
  12. ^ Avrahami, Limor; Paz, Rom; Dominko, Kristina; Hecimovic, Silva; Bucci, Cecilia; Eldar-Finkelman, Hagit (2020). "GSK-3-TSC axis governs lysosomal acidification through autophagy and endocytic pathways". Cellular Signalling. 71: 109597. doi:10.1016/j.cellsig.2020.109597. ISSN 0898-6568. PMID 32173369.
  13. ^ Eldar-Finkelman, Hagit; Licht-Murava, Avital; Pietrokovski, Shmuel; Eisenstein, Miriam (2010). "Substrate Competitive GSK-3 Inhibitors strategy and Implications". Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1804 (3): 598–603. doi:10.1016/j.bbapap.2009.09.010. ISSN 1570-9639. PMID 19770076.
  14. ^ Licht-Murava, Avital; Plotkin, Batya; Eisenstein, Miriam; Eldar-Finkelman, Hagit (2011). "Elucidating Substrate and Inhibitor Binding Sites on the Surface of GSK-3β and the Refinement of a Competitive Inhibitor". Journal of Molecular Biology. 408 (2): 366–378. doi:10.1016/j.jmb.2011.02.036. ISSN 0022-2836. PMID 21354422.
  15. ^ Rippin, Ido; Khazanov, Netaly; Ben Joseph, Shirley; Kudinov, Tania; Berent, Eva; Arciniegas Ruiz, Sara Melisa; Marciano, Daniele; Levy, Laura; Gruzman, Arie; Senderowitz, Hanoch; Eldar-Finkelman, Hagit (2020). "Discovery and Design of Novel Small Molecule GSK-3 Inhibitors Targeting the Substrate Binding Site". International Journal of Molecular Sciences. 21 (22): 8709. doi:10.3390/ijms21228709. ISSN 1422-0067. PMC 7698860. PMID 33218072.
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