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.

Triosephosphate isomerase catalysis is diffusion controlled. Appendix: Analysis of triose phosphate equilibria in aqueous solution by 31P NMR.
Authors: Authors: Blacklow SC, Raines RT, Lim WA, Zamore PD, Knowles JR.
Biochemistry
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The ectodomains determine ligand function in vivo and selectivity of DLL1 and DLL4 toward NOTCH1 and NOTCH2 in vitro.
Authors: Authors: Tveriakhina L, Schuster-Gossler K, Jarrett SM, Andrawes MB, Rohrbach M, Blacklow SC, Gossler A.
Elife
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Crystal Structure of a Full-Length Human Tetraspanin Reveals a Cholesterol-Binding Pocket.
Authors: Authors: Zimmerman B, Kelly B, McMillan BJ, Seegar TCM, Dror RO, Kruse AC, Blacklow SC.
Cell
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Refining a Jagged edge.
Authors: Authors: Blacklow SC.
Structure
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Structural and mechanistic insights into cooperative assembly of dimeric Notch transcription complexes.
Authors: Authors: Arnett KL, Hass M, McArthur DG, Ilagan MX, Aster JC, Kopan R, Blacklow SC.
Nat Struct Mol Biol
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Mutational and energetic studies of Notch 1 transcription complexes.
Authors: Authors: Del Bianco C, Aster JC, Blacklow SC.
J Mol Biol
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Phosphoinositide binding by the disabled-1 PTB domain is necessary for membrane localization and Reelin signal transduction.
Authors: Authors: Stolt PC, Chen Y, Liu P, Bock HH, Blacklow SC, Herz J.
J Biol Chem
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Origins of peptide selectivity and phosphoinositide binding revealed by structures of disabled-1 PTB domain complexes.
Authors: Authors: Stolt PC, Jeon H, Song HK, Herz J, Eck MJ, Blacklow SC.
Structure
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Calcium depletion dissociates and activates heterodimeric notch receptors.
Authors: Authors: Rand MD, Grimm LM, Artavanis-Tsakonas S, Patriub V, Blacklow SC, Sklar J, Aster JC.
Mol Cell Biol
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The development of enzyme catalytic efficiency: an experimental approach.
Authors: Authors: Hermes JD, Blacklow SC, Knowles JR.
Cold Spring Harb Symp Quant Biol
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