Journal ArticleDOI
Jak-STAT pathways and transcriptional activation in response to IFNs and other extracellular signaling proteins
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TLDR
A previously unrecognized direct signal transduction pathway to the nucleus has been uncovered: IFN-receptor interaction at the cell surface leads to the activation of kinases of the Jak family that phosphorylate substrate proteins called STATs (signal transducers and activators of transcription).Abstract:
Through the study of transcriptional activation in response to interferon alpha (IFN-alpha) and interferon gamma (IFN-gamma), a previously unrecognized direct signal transduction pathway to the nucleus has been uncovered: IFN-receptor interaction at the cell surface leads to the activation of kinases of the Jak family that then phosphorylate substrate proteins called STATs (signal transducers and activators of transcription). The phosphorylated STAT proteins move to the nucleus, bind specific DNA elements, and direct transcription. Recognition of the molecules involved in the IFN-alpha and IFN-gamma pathway has led to discoveries that a number of STAT family members exist and that other polypeptide ligands also use the Jak-STAT molecules in signal transduction.read more
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The Receptor for Advanced Glycation End Products Is Induced by the Glycation Products Themselves and Tumor Necrosis Factor-α through Nuclear Factor-κB, and by 17β-Estradiol through Sp-1 in Human Vascular Endothelial Cells
Nobushige Tanaka,Hideto Yonekura,Sho-ichi Yamagishi,Hideki Fujimori,Yasuhiko Yamamoto,Hiroshi Yamamoto +5 more
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Cancer prevention with natural compounds.
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Constitutive activation of Stat3 in fibroblasts transformed by diverse oncoproteins and in breast carcinoma cells
R Garcia,CL Yu,A Hudnall,R Catlett,Kristie L. Nelson,Thomas E. Smithgall,Donald J. Fujita,Stephen P. Ethier,Richard Jove +8 more
TL;DR: Investigation of STAT activation in a panel of rodent fibroblast cell lines stably transformed by diverse viral oncoproteins demonstrates that selective activation of Stat3 is a common event during oncogenic transformation that directly or indirectly involves activation of specific tyrosine kinase signaling pathways.
Journal ArticleDOI
Synergy between Interferon-γ and Tumor Necrosis Factor-α in Transcriptional Activation Is Mediated by Cooperation between Signal Transducer and Activator of Transcription 1 and Nuclear Factor κB
TL;DR: In this paper, the authors demonstrate that a portion of this cooperativity is mediated by synergism between two distinct transcription factors: signal transducer and activator of transcription 1 (STAT1) and nuclear factor kappaB (NF-kappaB), which is most likely mediated by their independent interaction with one or more components of the basal transcription complex.
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Modulation of STAT signaling by STAT-interacting proteins
TL;DR: The roles of STAT-interacting proteins in the regulation of STAT signaling are reviewed, finding a number of proteins function to modulate STAT signaling at various steps and mediate the crosstalk of STATs with other cellular signaling pathways.
References
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Journal ArticleDOI
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TL;DR: Gel electrophoresis in studies of equilibrium binding, site distribution, and kinetics of protein-DNA interactions found that binding to the so-called third operator site (03) is 15-18 fold weaker than operator binding, and that the binding reactions with the first and third operators are uncoupled, implying that there is no communication between the sites.
Journal ArticleDOI
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Journal ArticleDOI
SH2 and SH3 Domains: Elements that Control Interactions of Cytoplasmic Signaling Proteins
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Journal ArticleDOI
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