Sankar Ghosh
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Sankar Ghosh is a Professor of Immunobiology, Molecular Biophysics and Biochemistry, and Molecular, Cellular & Developmental Biology, and researcher working at Yale University.
[edit] Degrees
B.Sc., M.Sc., Calcutta University, India, 1981; M.S. Albert Einstein College of Medicine, New York, 1984; Ph.D., Albert Einstein College of Medicine, New York, 1988, Fellow of Irvington Institute for Medical Research; Whitehead Institute, Cambridge, 1989-1991; joined Yale faculty, 1991.
Dr. Ghosh worked in the lab of Nobel laureate David Baltimore.
[edit] Publications
Shim, J.H., et al. CHMP5 is essential for late endosome function and down-regulation of receptor signaling during mouse embryogenesis. J Cell Biol. 2006 Mar 27.
Shim, J.H., et al. TAK1, but not TAB1 or TAB2, plays an essential role in multiple signaling pathways in vivo. Genes Dev. 2005 Nov 15
Jimi, E. and S. Ghosh. Role of nuclear factor-kappaB in the immune system and bone. Immunol Rev. 2005 Dec.
Jimi, E. et al. Activation of NF-{kappa}B promotes the transition of large, CD43+ pre-B cells to small, CD43- pre-B cells. Int Immunol. 2005 May 20
Bailey ST, Ghosh S. 'PPAR'ting ways with inflammation. Nat Immunol., 2005 Oct 6
E. C. Ziegler, S. Ghosh, Regulating Inducible Transcription Through Controlled Localization. Sci. STKE 2005, re6 (2005).
di Meglio, P., A. Ianaro, and S. Ghosh, Amelioration of acute inflammation by systemic administration of a cell-permeable peptide inhibitor of NF-kappaB activation. Arthritis Rheum, 2005. 52(3): p. 951-8.
Lee, K.Y., et al., PDK1 nucleates T cell receptor-induced signaling complex for NF-kappaB activation. Science, 2005. 308(5718): p. 114-8.
Hayden, M.S. and S. Ghosh, Signaling to NF-kappaB. Genes Dev, 2004. 18(18): p. 2195-224.
Zhang, D., et al., A toll-like receptor that prevents infection by uropathogenic bacteria. Science, 2004. 303(5663): p. 1522-6.
Jimi, E., et al., Selective inhibition of NF-kappa B blocks osteoclastogenesis and prevents inflammatory bone destruction in vivo. Nat Med, 2004. 10(6): p. 617-24.
Marienfeld, R., et al., RelB forms transcriptionally inactive complexes with RelA/p65. J Biol Chem, 2003. 278(22): p. 19852-60.
Ma, X.Y., et al., The interferon-inducible p202a protein modulates NF-kappaB activity by inhibiting the binding to DNA of p50/p65 heterodimers and p65 homodimers while enhancing the binding of p50 homodimers. J Biol Chem, 2003. 278(25): p. 23008-19.
Wu, C. and S. Ghosh, Differential phosphorylation of the signal-responsive domain of I kappa B alpha and I kappa B beta by I kappa B kinases. J Biol Chem, 2003. 278(34): p. 31980-7.
May, M.J., R.B. Marienfeld, and S. Ghosh, Characterization of the Ikappa B-kinase NEMO binding domain. J Biol Chem, 2002. 277(48): p. 45992-6000.
Zhang, G. and S. Ghosh, Negative regulation of toll-like receptor-mediated signaling by Tollip. J Biol Chem, 2002. 277(9): p. 7059-65.
Zhong, H., et al., The phosphorylation status of nuclear NF-kappa B determines its association with CBP/p300 or HDAC-1. Mol Cell, 2002. 9(3): p. 625-36.
D'Acquisto, F., M.J. May, and S. Ghosh, Inhibition of Nuclear Factor Kappa B (NF-B):: An Emerging Theme in Anti-Inflammatory Therapies. Mol Interv, 2002. 2(1): p. 22-35.
Budde, L.M., et al., Regulation of IkappaBbeta expression in testis. Mol Biol Cell, 2002. 13(12): p. 4179-94.
Ghosh, S. and M. Karin, Missing pieces in the NF-kappaB puzzle. Cell, 2002. 109 Suppl: p. S81-96.
D'Acquisto, F. and S. Ghosh, PACT and PKR: turning on NF-kappa B in the absence of virus. Sci STKE, 2001. 2001(89): p. RE1.
Zhang, G. and S. Ghosh, Toll-like receptor-mediated NF-kappaB activation: a phylogenetically conserved paradigm in innate immunity. J Clin Invest, 2001. 107(1): p. 13-9.
May, M.J., et al., Selective inhibition of NF-kappaB activation by a peptide that blocks the interaction of NEMO with the IkappaB kinase complex. Science, 2000. 289(5484): p. 1550-4.
Voll, R.E., et al., NF-kappa B activation by the pre-T cell receptor serves as a selective survival signal in T lymphocyte development. Immunity, 2000. 13(5): p. 677-89.
Millet, I., et al., Inhibition of NF-kappaB activity and enhancement of apoptosis by the neuropeptide calcitonin gene-related peptide. J Biol Chem, 2000. 275(20): p. 15114-21.
Li, B., et al., Role of the guanosine triphosphatase Rac2 in T helper 1 cell differentiation. Science, 2000. 288(5474): p. 2219-22.
Fenwick, C., et al., A subclass of Ras proteins that regulate the degradation of IkappaB. Science, 2000. 287(5454): p. 869-73.
Budde, L.M. and S. Ghosh, Cloning and characterization of the gene encoding mouse IkappaBbeta. Gene, 2000. 247(1-2): p. 279-86.
Zhang, G. and S. Ghosh, Molecular mechanisms of NF-kappaB activation induced by bacterial lipopolysaccharide through Toll-like receptors. J Endotoxin Res, 2000. 6(6): p. 453-7.
Wu, C. and S. Ghosh, beta-TrCP mediates the signal-induced ubiquitination of IkappaBbeta. J Biol Chem, 1999. 274(42): p. 29591-4.
Kopp, E., et al., ECSIT is an evolutionarily conserved intermediate in the Toll/IL-1 signal transduction pathway. Genes Dev, 1999. 13(16): p. 2059-71.
May, M.J. and S. Ghosh, IkappaB kinases: kinsmen with different crafts. Science, 1999. 284(5412): p. 271-3.
Ghosh, S., Regulation of inducible gene expression by the transcription factor NF-kappaB. Immunol Res, 1999. 19(2-3): p. 183-9.
Voll, R.E. and S. Ghosh, Role of NF-kappa B in T-lymphocyte development. Cold Spring Harb Symp Quant Biol, 1999. 64: p. 485-90.
May, M.J. and S. Ghosh, Signal transduction through NF-kappa B. Immunol Today, 1998. 19(2): p. 80-8.
Medzhitov, R., et al., MyD88 is an adaptor protein in the hToll/IL-1 receptor family signaling pathways. Mol Cell, 1998. 2(2): p. 253-8.
Zhong, H., R.E. Voll, and S. Ghosh, Phosphorylation of NF-kappa B p65 by PKA stimulates transcriptional activity by promoting a novel bivalent interaction with the coactivator CBP/p300. Mol Cell, 1998. 1(5): p. 661-71.
Ghosh, S., M.J. May, and E.B. Kopp, NF-kappa B and Rel proteins: evolutionarily conserved mediators of immune responses. Annu Rev Immunol, 1998. 16: p. 225-60.
Zhong, H., et al., The transcriptional activity of NF-kappaB is regulated by the IkappaB-associated PKAc subunit through a cyclic AMP-independent mechanism. Cell, 1997. 89(3): p. 413-24.
Phillips, R.J. and S. Ghosh, Regulation of IkappaB beta in WEHI 231 mature B cells. Mol Cell Biol, 1997. 17(8): p. 4390-6.
May, M.J. and S. Ghosh, Rel/NF-kappa B and I kappa B proteins: an overview. Semin Cancer Biol, 1997. 8(2): p. 63-73.
Suyang, H., et al., Role of unphosphorylated, newly synthesized I kappa B beta in persistent activation of NF-kappa B. Mol Cell Biol, 1996. 16(10): p. 5444-9.
Johnson, D.R., et al., A sustained reduction in IkappaB-beta may contribute to persistent NF-kappaB activation in human endothelial cells. J Biol Chem, 1996. 271(27): p. 16317-22.
Phillips, R.J., S. Gustafson, and S. Ghosh, Identification of a novel NF-kappaB p50-related protein in B lymphocytes. Mol Cell Biol, 1996. 16(12): p. 7089-97.
Ghosh, G., et al., Structure of NF-kappa B p50 homodimer bound to a kappa B site. Nature, 1995. 373(6512): p. 303-10.
Thompson, J.E., et al., I kappa B-beta regulates the persistent response in a biphasic activation of NF-kappa B. Cell, 1995. 80(4): p. 573-82.
Kopp, E.B. and S. Ghosh, NF-kappa B and rel proteins in innate immunity. Adv Immunol, 1995. 58: p. 1-27.
Kopp, E. and S. Ghosh, Inhibition of NF-kappa B by sodium salicylate and aspirin. Science, 1994. 265(5174): p. 956-9.
Ghosh, S., et al., Cloning of the p50 DNA binding subunit of NF-kappa B: homology to rel and dorsal. Cell, 1990. 62(5): p. 1019-29.
Ghosh, S. and D. Baltimore, Activation in vitro of NF-kappa B by phosphorylation of its inhibitor I kappa B. Nature, 1990. 344(6267): p. 678-82.
