Stephen Blacklow

Stephen Blacklow, MD, PhD

Gustavus Adolphus Pfeiffer Professor of Biological Chemistry and Molecular Pharmacology, Harvard Medical School

Dr. Blacklow is currently the Gustavus Adolphus Pfeiffer Professor and Chair of the Department of Biological Chemistry and Molecular Pharmacology at Harvard Medical School, and a member of the Department of Cancer Biology at the Dana Farber Cancer Institute.

Research led by Dr. Blacklow’s team has shown how cell surface receptors can convey a developmental signal directly from one contacting cell surface to the next and then from the membrane to the nucleus. He has elucidated key molecular events in Notch signal transduction, a conserved cell-cell communication system that influences cell fate decisions in all metazoan organisms, and that is frequently hijacked as an oncogenic driver in human leukemia. His research on the Notch pathway has led to the development of new investigational therapies for hematologic malignancies such as T cell acute lymphocytic leukemia (ALL).

Dr. Blacklow was a recipient of the National Cancer Institute’s prestigious Outstanding Investigator Award in 2017, and elected to the Association of American Physicians in 2018. Dr. Blacklow directed the MD-PhD Program in Basic and Translational Sciences at Harvard Medical School and has served on Advisory Committees for pre-clinical departments, graduate programs, and MD-PhD programs at several major research universities and institutions, including Stanford, the University of Pennsylvania, and the Memorial Sloan Kettering Cancer Center.

Dr. Blacklow received his MD and PhD degrees from Harvard University in 1991, completed his residency in Clinical Pathology at Brigham and Women’s Hospital, and carried out postdoctoral research at the Whitehead Institute with Dr. Peter S. Kim.

Complementary genomic screens identify SERCA as a therapeutic target in NOTCH1 mutated cancer.
Authors: Authors: Roti G, Carlton A, Ross KN, Markstein M, Pajcini K, Su AH, Perrimon N, Pear WS, Kung AL, Blacklow SC, Aster JC, Stegmaier K.
Cancer Cell
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Transformation by Tribbles homolog 2 (Trib2) requires both the Trib2 kinase domain and COP1 binding.
Authors: Authors: Keeshan K, Bailis W, Dedhia PH, Vega ME, Shestova O, Xu L, Toscano K, Uljon SN, Blacklow SC, Pear WS.
Blood
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Structural basis for autoinhibition of Notch.
Authors: Authors: Gordon WR, Vardar-Ulu D, Histen G, Sanchez-Irizarry C, Aster JC, Blacklow SC.
Nat Struct Mol Biol
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Cooperation between fixed and low pH-inducible interfaces controls lipoprotein release by the LDL receptor.
Authors: Authors: Beglova N, Jeon H, Fisher C, Blacklow SC.
Mol Cell
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Notch signaling as a therapeutic target.
Authors: Authors: Nam Y, Aster JC, Blacklow SC.
Curr Opin Chem Biol
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Structural independence of ligand-binding modules five and six of the LDL receptor.
Authors: Authors: North CL, Blacklow SC.
Biochemistry
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MAFB enhances oncogenic Notch signaling in T cell acute lymphoblastic leukemia.
Authors: Authors: Pajcini KV, Xu L, Shao L, Petrovic J, Palasiewicz K, Ohtani Y, Bailis W, Lee C, Wertheim GB, Mani R, Muthusamy N, Li Y, Meijerink JPP, Blacklow SC, Faryabi RB, Cherry S, Pear WS.
Sci Signal
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Structural Basis for Substrate Selectivity of the E3 Ligase COP1.
Authors: Authors: Uljon S, Xu X, Durzynska I, Stein S, Adelmant G, Marto JA, Pear WS, Blacklow SC.
Structure
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Targeting the Notch pathway: twists and turns on the road to rational therapeutics.
Authors: Authors: Aster JC, Blacklow SC.
J Clin Oncol
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Differential ability of Tribbles family members to promote degradation of C/EBPalpha and induce acute myelogenous leukemia.
Authors: Authors: Dedhia PH, Keeshan K, Uljon S, Xu L, Vega ME, Shestova O, Zaks-Zilberman M, Romany C, Blacklow SC, Pear WS.
Blood
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