Professor of Biological Chemistry and Molecular Pharmacology, Dana-Farber Cancer Institute
Pathology
Dr. Stephen C. Blacklow, MD
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Dr. Stephen C. Blacklow works in the field of Pathology. He studied medicine at Harvard Medical School. Harvard Medical School is a top medical college. Harvard Medical School has a rank of 1 in research and a 12 in primary care Doctor Stephen C. Blacklow, MD is a published MD as well. He has 61 publications published. The latest was: A tail of two sites: a bipartite mechanism for recognition of notch ligands by mind bomb e3 ligases.
Publications
- A tail of two sites: a bipartite mechanism for recognition of notch ligands by mind bomb e3 ligases.
- Biased multicomponent reactions to develop novel bromodomain inhibitors.
- NOTCH1-RBPJ complexes drive target gene expression through dynamic interactions with superenhancers.
- Insights into Notch3 Activation and Inhibition Mediated by Antibodies Directed against Its Negative Regulatory Region.
- Intrinsic Selectivity of Notch 1 for Delta-like 4 Over Delta-like 1.
- Complementary Genomic Screens Identify SERCA as a Therapeutic Target in NOTCH1 Mutated Cancer.
- T-cell factor 1 is a gatekeeper for T-cell specification in response to Notch signaling.
- Loss-of-function mutations in Notch receptors in cutaneous and lung squamous cell carcinoma.
- Epstein-Barr virus exploits intrinsic B-lymphocyte transcription programs to achieve immortal cell growth.
- Genome-wide analysis reveals conserved and divergent features of Notch1/RBPJ binding in human and murine T-lymphoblastic leukemia cells.
- Epstein-Barr virus nuclear protein 3C binds to the N-terminal (NTD) and beta trefoil domains (BTD) of RBP/CSL; Only the NTD interaction is essential for lymphoblastoid...
- Evidence for Increased Exposure of the Notch1 Metalloprotease Cleavage Site upon Conversion to an Activated Conformation.
- Notch ankyrin repeat domain variation influences leukemogenesis and Myc transactivation.
- Deletion-based mechanisms of Notch1 activation in T-ALL: key roles for RAG recombinase and a conserved internal translational start site in Notch1.
- Transformation by Tribbles homolog 2 (Trib2) requires both the Trib2 kinase domain and COP1 binding.
- Structural and mechanistic insights into cooperative assembly of dimeric Notch transcription complexes.
- Notch dimerization is required for leukemogenesis and T-cell development.
- Differential ability of Tribbles family members to promote degradation of C/EBPalpha and induce acute myelogenous leukemia.
- Characterization of Notch1 antibodies that inhibit signaling of both normal and mutated Notch1 receptors.
- Mechanistic insights into Notch receptor signaling from structural and biochemical studies.
- Notch and MAML-1 complexation do not detectably alter the DNA binding specificity of the transcription factor CSL.
- Pre-TCR signaling inactivates Notch1 transcription by antagonizing E2A.
- Structure of the Notch1-negative regulatory region: implications for normal activation and pathogenic signaling in T-ALL.
- Effects of S1 cleavage on the structure, surface export, and signaling activity of human Notch1 and Notch2.
- Modulation of Notch signaling by antibodies specific for the extracellular negative regulatory region of NOTCH3.
- Unfolding of the RAP-D3 helical bundle facilitates dissociation of RAP-receptor complexes.
- Notch signaling in leukemia.
- Notch directly regulates Gata3 expression during T helper 2 cell differentiation.
- Requirement for natively unstructured regions of mesoderm development candidate 2 in promoting low-density lipoprotein receptor-related protein 6 maturation.
- Structural basis for autoinhibition of Notch.
- Cooperative assembly of higher-order Notch complexes functions as a switch to induce transcription.
- c-Myc is an important direct target of Notch1 in T-cell acute lymphoblastic leukemia/lymphoma.
- Identification of a conserved negative regulatory sequence that influences the leukemogenic activity of NOTCH1.
- Leukemia-associated mutations within the NOTCH1 heterodimerization domain fall into at least two distinct mechanistic classes.
- Structure of an LDLR-RAP complex reveals a general mode for ligand recognition by lipoprotein receptors.
- Structural basis for cooperativity in recruitment of MAML coactivators to Notch transcription complexes.
- A new niche for Notch on Deltex?
- De novo genetic codes and pure translation display.
- Folding and binding integrity of variants of a prototype ligand-binding module from the LDL receptor possessing multiple alanine substitutions.
- Phosphoinositide binding by the disabled-1 PTB domain is necessary for membrane localization and Reelin signal transduction.
- Structure and physiologic function of the low-density lipoprotein receptor.
- Notch subunit heterodimerization and prevention of ligand-independent proteolytic activation depend, respectively, on a novel domain and the LNR repeats.
- Cooperation between fixed and low pH-inducible interfaces controls lipoprotein release by the LDL receptor.
- Pure translation display.
- Amino acid backbone specificity of the Escherichia coli translation machinery.
- Activating mutations of NOTCH1 in human T cell acute lymphoblastic leukemia.
- The dual-function disabled-1 PTB domain exhibits site independence in binding phosphoinositide and peptide ligands.
- Global defects in the expression and function of the low density lipoprotein receptor (LDLR) associated with two familial hypercholesterolemia mutations resulting in m...
- Catching the common cold.
- A two-module region of the low-density lipoprotein receptor sufficient for formation of complexes with apolipoprotein E ligands.
- The mature avian leukosis virus subgroup A envelope glycoprotein is metastable, and refolding induced by the synergistic effects of receptor binding and low pH is coup...
- A zinc clasp structure tethers Lck to T cell coreceptors CD4 and CD8.
- Nuclear magnetic resonance structure of a prototype Lin12-Notch repeat module from human Notch1.
- Structural requirements for assembly of the CSL.intracellular Notch1.Mastermind-like 1 transcriptional activation complex.
- Programming peptidomimetic syntheses by translating genetic codes designed de novo.
- Origins of peptide selectivity and phosphoinositide binding revealed by structures of disabled-1 PTB domain complexes.
- An intramolecular spin of the LDL receptor beta propeller.
- Growth suppression of pre-T acute lymphoblastic leukemia cells by inhibition of notch signaling.
- Cysteine-rich module structure reveals a fulcrum for integrin rearrangement upon activation.
- The SCAN domain of ZNF174 is a dimer.
Schools
Harvard Medical School
Brigham and Women39s Hospital
Doctors Specialties
- Clinical Pathology
- Pathology
Accepted Insurances
Education
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Brigham and Women's Hospital -
Harvard Medical School
Hospital
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Dana-Farber Cancer Institute
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