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1
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0028234529
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Jak-STAT pathways and transcriptional activation in response to interferons and other extracellular signaling proteins
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Darnell JE Jr, Kerr IA, Stark GR. Jak-STAT pathways and transcriptional activation in response to interferons and other extracellular signaling proteins. Science. 264:1994;1415-1421.
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(1994)
Science
, vol.264
, pp. 1415-1421
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Darnell J.E., Jr.1
Kerr, I.A.2
Stark, G.R.3
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2
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0030765924
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Jaks, STATs, cytokines, signal transduction, and immunoregulation: Are we there yet?
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O'Shea JJ. Jaks, STATs, cytokines, signal transduction, and immunoregulation: are we there yet? Immunity. 7:1997;1-11.
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(1997)
Immunity
, vol.7
, pp. 1-11
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O'Shea, J.J.1
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3
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0030807903
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SH2 signaling in a lower eukaryote: A Stat protein that regulates stalk cell differentiation in Dictyostelium
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of outstanding interest. This paper identifies a key transcriptional regulator that mediates cell - cell communication as a member of the STAT family. As Dictyosetelium is one of the most primitive multicellular organisms, it appears that STATs arose early in evolution as means of signal transduction. The most conserved regions between the Dictyostelium and mammalian STAT proteins are the DNA-binding domain and the SH2 domain.
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Kawata T, Shevchenko A, Fukuzawa M, Jermyn KA, Totty NF, Zhukovskaya NV, Sterling AE, Mann M, Williams JG. SH2 signaling in a lower eukaryote: a Stat protein that regulates stalk cell differentiation in Dictyostelium. of outstanding interest Cell. 89:1997;909-916 This paper identifies a key transcriptional regulator that mediates cell - cell communication as a member of the STAT family. As Dictyosetelium is one of the most primitive multicellular organisms, it appears that STATs arose early in evolution as means of signal transduction. The most conserved regions between the Dictyostelium and mammalian STAT proteins are the DNA-binding domain and the SH2 domain.
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(1997)
Cell
, vol.89
, pp. 909-916
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Kawata, T.1
Shevchenko, A.2
Fukuzawa, M.3
Jermyn, K.A.4
Totty, N.F.5
Zhukovskaya, N.V.6
Sterling, A.E.7
Mann, M.8
Williams, J.G.9
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4
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0001514956
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Identification of a STAT gene that functions in Drosophila development
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Yan R, Small S, Desplan C, Dearolf CR, Darnell JE Jr. Identification of a STAT gene that functions in Drosophila development. Cell. 84:1996;421-430.
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(1996)
Cell
, vol.84
, pp. 421-430
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Yan, R.1
Small, S.2
Desplan, C.3
Dearolf, C.R.4
Darnell J.E., Jr.5
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5
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0030040691
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Marelle acts downstream of the Drosophila HOP/Jak kinase and encodes a protein similar to the mammalian STATs
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Hou XS, Melnick MB, Perrimon N. marelle acts downstream of the Drosophila HOP/Jak kinase and encodes a protein similar to the mammalian STATs. Cell. 84:1996;411-419.
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(1996)
Cell
, vol.84
, pp. 411-419
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Hou, X.S.1
Melnick, M.B.2
Perrimon, N.3
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6
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0032504232
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Mutational analysis of the STAT6 SH2 domain
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of special interest. This paper reports a complete alanine-scanning mutagenesis of the STAT6 SH2 domain. Amino acids specifically required for cytokine receptor binding or dimerization are identified, providing a functional map of the STAT class of SH2 domain.
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Mikita T, Daniel C, Wu P, Schindler U. Mutational analysis of the STAT6 SH2 domain. of special interest J Biol Chem. 273:1998;17634-17642 This paper reports a complete alanine-scanning mutagenesis of the STAT6 SH2 domain. Amino acids specifically required for cytokine receptor binding or dimerization are identified, providing a functional map of the STAT class of SH2 domain.
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(1998)
J Biol Chem
, vol.273
, pp. 17634-17642
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Mikita, T.1
Daniel, C.2
Wu, P.3
Schindler, U.4
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7
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0032577678
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Crystal structure of a STAT-1 dimer bound to DNA
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of outstanding interest. This paper provides the first structural analysis of a STAT-DNA complex. The DNA-binding domain has the structure of the immunoglobulin fold, similar to NF-κB and p53. The SH2 domain is structurally very similar to src, despite the lack of sequence homology outside the phosphotyrosine-binding pocket.
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Chen X, Vinkemeir U, Zhao Y, Jeruzalmi D, Darnell JE Jr, Kuriyan J. Crystal structure of a STAT-1 dimer bound to DNA. of outstanding interest Cell. 93:1998;827-839 This paper provides the first structural analysis of a STAT-DNA complex. The DNA-binding domain has the structure of the immunoglobulin fold, similar to NF-κB and p53. The SH2 domain is structurally very similar to src, despite the lack of sequence homology outside the phosphotyrosine-binding pocket.
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(1998)
Cell
, vol.93
, pp. 827-839
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Chen, X.1
Vinkemeir, U.2
Zhao, Y.3
Jeruzalmi, D.4
Darnell J.E., Jr.5
Kuriyan, J.6
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8
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0028913109
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A STAT protein domain that determines DNA sequence recognition suggests a novel DNA-binding domain
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Horvath CM, Wen Z, Darnell JE Jr. A STAT protein domain that determines DNA sequence recognition suggests a novel DNA-binding domain. Genes Dev. 9:1995;984-994.
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(1995)
Genes Dev
, vol.9
, pp. 984-994
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Horvath, C.M.1
Wen, Z.2
Darnell J.E., Jr.3
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9
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0029001660
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Components of a Stat recognition code: Evidence for two layers of molecular selectivity
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Schindler U, Wu P, Rothe M, Brasseur M, McKnight SL. Components of a Stat recognition code: evidence for two layers of molecular selectivity. Immunity. 2:1995;689-697.
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(1995)
Immunity
, vol.2
, pp. 689-697
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Schindler, U.1
Wu, P.2
Rothe, M.3
Brasseur, M.4
McKnight, S.L.5
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10
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0029069145
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Transcriptional responses to polypeptide ligands: The JAK-STAT pathway
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Schindler C, Darnell JE Jr. Transcriptional responses to polypeptide ligands: the JAK-STAT pathway. Annu Rev Biochem. 64:1995;621-651.
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(1995)
Annu Rev Biochem
, vol.64
, pp. 621-651
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Schindler, C.1
Darnell J.E., Jr.2
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11
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0028937707
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Spacing of the palindromic half sites as a determinant of selective STAT (signal transducers and activators of transcription) DNA binding and transcriptional activity
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Seidel HM, Milocco LH, Lamb P, Darnell JE Jr, Stein RB, Rosen J. Spacing of the palindromic half sites as a determinant of selective STAT (signal transducers and activators of transcription) DNA binding and transcriptional activity. Proc Natl Acad Sci USA. 92:1995;3041-3045.
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(1995)
Proc Natl Acad Sci USA
, vol.92
, pp. 3041-3045
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Seidel, H.M.1
Milocco, L.H.2
Lamb, P.3
Darnell J.E., Jr.4
Stein, R.B.5
Rosen, J.6
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13
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0029739627
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Cooperative DNA binding and sequence-selective recognition conferred by the STAT amino terminal domain
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Xu X, Sun Y-L, Hoey T. Cooperative DNA binding and sequence-selective recognition conferred by the STAT amino terminal domain. Science. 273:1996;794-797.
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(1996)
Science
, vol.273
, pp. 794-797
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Xu, X.1
Sun, Y.-L.2
Hoey, T.3
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14
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0032512661
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Structure of the amino terminal protein interaction domain of STAT4
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of outstanding interest. The amino-terminal domain of STAT4 mediates dimer - dimer interactions and cooperative DNA binding to adjacent sites. This domain is composed of a series of helices that form a hook-like structure capable of dimerizing.
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Vinkemeier U, Moarefi I, Darnell JE, Kuriyan J. Structure of the amino terminal protein interaction domain of STAT4. of outstanding interest Science. 279:1998;1048-1052 The amino-terminal domain of STAT4 mediates dimer - dimer interactions and cooperative DNA binding to adjacent sites. This domain is composed of a series of helices that form a hook-like structure capable of dimerizing.
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(1998)
Science
, vol.279
, pp. 1048-1052
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Vinkemeier, U.1
Moarefi, I.2
Darnell, J.E.3
Kuriyan, J.4
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16
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0029826282
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Naturally occurring dominant negative variants of Stat5
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Wang D, Stravopodis D, Teglund S, Kitazawa J, Ihle JN. Naturally occurring dominant negative variants of Stat5. Mol Cell Biol. 16:1996;6141-6148.
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(1996)
Mol Cell Biol
, vol.16
, pp. 6141-6148
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Wang, D.1
Stravopodis, D.2
Teglund, S.3
Kitazawa, J.4
Ihle, J.N.5
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17
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0029117304
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Maximal activation of transcription by Stat1 and Stat3 requires both tyrosine and serine phosphorylation
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Wen Z, Zhong Z, Darnell JE Jr. Maximal activation of transcription by Stat1 and Stat3 requires both tyrosine and serine phosphorylation. Cell. 82:1995;241-250.
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(1995)
Cell
, vol.82
, pp. 241-250
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Wen, Z.1
Zhong, Z.2
Darnell J.E., Jr.3
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18
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0030792590
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A family of cytokine-inducible inhibitors of signalling
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of special interest. The authors use a retroviral gene transfer system to identify genes that inhibit IL-6 signaling, leading to the discovery of the SOCS family.
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Starr R, Willson TA, Viney EM, Murray LJL, Rayner JR, Jenkins BJ, Gonda TJ, Alexander WS, Metcalf D, Nicola NA, Hilton DJ. A family of cytokine-inducible inhibitors of signalling. of special interest Nature. 387:1997;917-921 The authors use a retroviral gene transfer system to identify genes that inhibit IL-6 signaling, leading to the discovery of the SOCS family.
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(1997)
Nature
, vol.387
, pp. 917-921
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Starr, R.1
Willson, T.A.2
Viney, E.M.3
Murray, L.J.L.4
Rayner, J.R.5
Jenkins, B.J.6
Gonda, T.J.7
Alexander, W.S.8
Metcalf, D.9
Nicola, N.A.10
Hilton, D.J.11
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19
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0030755934
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Structure and function of a new STAT-induced STAT inhibitor
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Naka T, Narazaki M, Hirata M, Matsumoto T, Minamoto S, Aono A, Nishimoto N, Kajita T, Taga T, Yoshizaki K, et al. Structure and function of a new STAT-induced STAT inhibitor. Nature. 387:1997;924-929.
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(1997)
Nature
, vol.387
, pp. 924-929
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-
Naka, T.1
Narazaki, M.2
Hirata, M.3
Matsumoto, T.4
Minamoto, S.5
Aono, A.6
Nishimoto, N.7
Kajita, T.8
Taga, T.9
Yoshizaki, K.10
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20
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0030839112
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A new protein containing an SH2 domain that inhibits JAK kinases
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Endo TA, Masuhara M, Yokouchi M, Suzuki R, Mitsui K, Sakamoto H, Ohtsubo M, Misawa H, Kanekura Y, Yoshimura A. A new protein containing an SH2 domain that inhibits JAK kinases. Nature. 387:1997;921-924.
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(1997)
Nature
, vol.387
, pp. 921-924
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Endo, T.A.1
Masuhara, M.2
Yokouchi, M.3
Suzuki, R.4
Mitsui, K.5
Sakamoto, H.6
Ohtsubo, M.7
Misawa, H.8
Kanekura, Y.9
Yoshimura, A.10
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21
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13144258732
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Twenty proteins containing a C-terminal SOCS box from five structural classes
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of special interest. This study identifies many new SOCS-box-containing proteins through database searching: several are similar to SOCS-1, containing an SH2 domain and a carboxy-terminal SOCs box; other members lack an SH2 domain but have other types of protein - protein interaction domains.
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Hilton DJ, Richardson RT, Alexander WS, Viney EM, Willson TA, Sprigg NS, Starr R, Nicholson SE, Metcalf D, Nicola NA. Twenty proteins containing a C-terminal SOCS box from five structural classes. of special interest Proc Natl Acad Sci USA. 95:1998;114-119 This study identifies many new SOCS-box-containing proteins through database searching: several are similar to SOCS-1, containing an SH2 domain and a carboxy-terminal SOCs box; other members lack an SH2 domain but have other types of protein - protein interaction domains.
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(1998)
Proc Natl Acad Sci USA
, vol.95
, pp. 114-119
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Hilton, D.J.1
Richardson, R.T.2
Alexander, W.S.3
Viney, E.M.4
Willson, T.A.5
Sprigg, N.S.6
Starr, R.7
Nicholson, S.E.8
Metcalf, D.9
Nicola, N.A.10
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22
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0028972719
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Differential regulation of the alpha/beta interferon-stimulated Jak/Stat pathway by the SH2 domain containing tyrosine phosphatase SHPTP1
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David M, Chen HE, Goelz S, Larner AC, Neel BG. Differential regulation of the alpha/beta interferon-stimulated Jak/Stat pathway by the SH2 domain containing tyrosine phosphatase SHPTP1. Mol Cell Biol. 15:1995;7050-7058.
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(1995)
Mol Cell Biol
, vol.15
, pp. 7050-7058
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David, M.1
Chen, H.E.2
Goelz, S.3
Larner, A.C.4
Neel, B.G.5
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23
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0029973560
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Direct association with and dephosphorylation of Jak2 kinase by the SH2-domain containing protein tyrosine phosphatase SHP-1
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Jiao H, Berrada K, Yang W, Tabrizi M, Platanias LC, Yi T. Direct association with and dephosphorylation of Jak2 kinase by the SH2-domain containing protein tyrosine phosphatase SHP-1. Mol Cell Biol. 16:1996;6985-6992.
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(1996)
Mol Cell Biol
, vol.16
, pp. 6985-6992
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Jiao, H.1
Berrada, K.2
Yang, W.3
Tabrizi, M.4
Platanias, L.C.5
Yi, T.6
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24
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0030945444
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Mapping of the cytoplasmic domain of the human growth hormone receptor that regulates rates of inactivation of Jak2 and Stat proteins
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Hackett RH, Wang YD, Switzer S, Feldman G, Wood WI, Larner AC. Mapping of the cytoplasmic domain of the human growth hormone receptor that regulates rates of inactivation of Jak2 and Stat proteins. J Biol Chem. 272:1997;11128-11132.
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(1997)
J Biol Chem
, vol.272
, pp. 11128-11132
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Hackett, R.H.1
Wang, Y.D.2
Switzer, S.3
Feldman, G.4
Wood, W.I.5
Larner, A.C.6
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25
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0030582671
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The emerging field of receptor-mediated inhibitory signaling: SHP or SHIP?
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Sharenberg AM, Kinet JP. The emerging field of receptor-mediated inhibitory signaling: SHP or SHIP? Cell. 87:1996;961-964.
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(1996)
Cell
, vol.87
, pp. 961-964
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Sharenberg, A.M.1
Kinet, J.P.2
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26
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0029972194
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The rapid inactivation of nuclear tyrosine phosphorylated Stat1 depends upon a protein tyrosine phosphatase
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Haspel RL, Salditt-Georgieff M, Darnell JE Jr. The rapid inactivation of nuclear tyrosine phosphorylated Stat1 depends upon a protein tyrosine phosphatase. EMBO J. 15:1996;6262-6268.
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(1996)
EMBO J
, vol.15
, pp. 6262-6268
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Haspel, R.L.1
Salditt-Georgieff, M.2
Darnell J.E., Jr.3
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27
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0029742102
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Enhancement of antiproliferative activity of gamma interferon by the specific inhibition of tyrosine dephosphorylation of Stat1
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Shuai K, Liao J, Song MM. Enhancement of antiproliferative activity of gamma interferon by the specific inhibition of tyrosine dephosphorylation of Stat1. Mol Cell Biol. 16:1996;4932-4941.
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(1996)
Mol Cell Biol
, vol.16
, pp. 4932-4941
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Shuai, K.1
Liao, J.2
Song, M.M.3
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28
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0000413462
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Regulation of interferon-gamma-activated STAT1 by the ubiquitin-proteasome pathway
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Kim TK, Maniatis T. Regulation of interferon-gamma-activated STAT1 by the ubiquitin-proteasome pathway. Science. 273:1996;1717-1719.
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(1996)
Science
, vol.273
, pp. 1717-1719
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Kim, T.K.1
Maniatis, T.2
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29
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0030725378
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Specific inhibition of Stat3 signal transduction by PIAS3
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of outstanding interest. An inhibitor of STAT3 DNA binding is identified. As PIAS3 is a member of a family of related proteins and does not interact with STAT1, it may be that specific PIAS proteins exist for each of the STATs. The exploration of how PIAS proteins inhibit STAT DNA binding and how their expression and activity is regulated will be hot topics in the field.
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Chung CD, Liao J, Liu B, Rao X, Jay P, Berta P, Shuai K. Specific inhibition of Stat3 signal transduction by PIAS3. of outstanding interest Science. 278:1997;1803-1805 An inhibitor of STAT3 DNA binding is identified. As PIAS3 is a member of a family of related proteins and does not interact with STAT1, it may be that specific PIAS proteins exist for each of the STATs. The exploration of how PIAS proteins inhibit STAT DNA binding and how their expression and activity is regulated will be hot topics in the field.
-
(1997)
Science
, vol.278
, pp. 1803-1805
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Chung, C.D.1
Liao, J.2
Liu, B.3
Rao, X.4
Jay, P.5
Berta, P.6
Shuai, K.7
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30
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0029557904
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Stat1 depends on transcriptional synergy with Sp1
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Look DC, Pelletier MR, Tidwell RM, Roswit WT, Holtzman MJ. Stat1 depends on transcriptional synergy with Sp1. J Biol Chem. 270:1995;30264-30267.
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(1995)
J Biol Chem
, vol.270
, pp. 30264-30267
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Look, D.C.1
Pelletier, M.R.2
Tidwell, R.M.3
Roswit, W.T.4
Holtzman, M.J.5
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31
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0031005027
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Synergy between interferon-γ and tumor necrosis factor-α in transcriptional activation is mediated by cooperation between signal tranducer and activator of transcription 1 and nuclear factor κB
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Ohmori Y, Schreiber RD, Hamilton TA. Synergy between interferon-γ and tumor necrosis factor-α in transcriptional activation is mediated by cooperation between signal tranducer and activator of transcription 1 and nuclear factor κB. J Biol Chem. 272:1997;14899-14907.
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J Biol Chem
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Ohmori, Y.1
Schreiber, R.D.2
Hamilton, T.A.3
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32
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0029075875
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Cooperative transcriptional of Jun and Stat3β, a short form of STAT3
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Shaefer TS, Sanders LK, Nathans D. Cooperative transcriptional of Jun and Stat3β, a short form of STAT3. Proc Natl Acad Sci USA. 92:1995;9097-9101.
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(1995)
Proc Natl Acad Sci USA
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Shaefer, T.S.1
Sanders, L.K.2
Nathans, D.3
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33
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0032513202
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Autoregulation of the Stat3 gene through cooperation with a cAMP-responsive element binding protein
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Ichiba M, Nakajima K, Yamnaka Y, Kiuchi N, Hirano T. Autoregulation of the Stat3 gene through cooperation with a cAMP-responsive element binding protein. J Biol Chem. 273:1998;6132-6138.
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(1998)
J Biol Chem
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Ichiba, M.1
Nakajima, K.2
Yamnaka, Y.3
Kiuchi, N.4
Hirano, T.5
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34
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0030667790
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STAT3 acts as a co-activator of glucocorticoid receptor signaling
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Zhang Z, Jones S, Hagood JS, Fuentes NL, Fuller GM. STAT3 acts as a co-activator of glucocorticoid receptor signaling. J Biol Chem. 272:1997;30607-30610.
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(1997)
J Biol Chem
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Zhang, Z.1
Jones, S.2
Hagood, J.S.3
Fuentes, N.L.4
Fuller, G.M.5
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35
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0029851231
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Functional interactions between STAT5 and the glucocorticoid receptor
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Stocklin E, Wissler M, Goilleux F, Groner B. Functional interactions between STAT5 and the glucocorticoid receptor. Nature. 383:1996;726-728.
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(1996)
Nature
, vol.383
, pp. 726-728
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Stocklin, E.1
Wissler, M.2
Goilleux, F.3
Groner, B.4
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36
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0032529415
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Synergistic activation of the germline epsilon promoter mediated by STAT6 and C/EBPβ
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Mikita T, Kurama M, Schnindler U. Synergistic activation of the germline epsilon promoter mediated by STAT6 and C/EBPβ J Immunol. 161:1998;1822-1828.
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(1998)
J Immunol
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Mikita, T.1
Kurama, M.2
Schnindler, U.3
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37
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0029767462
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Cooperation of Stat2 and p300/CBP in signalling induced by interferon α
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Bhattacharya S, Eckner R, Grossman S, Oldread E, Arany Z, D'Andrea A, Livingston DM. Cooperation of Stat2 and p300/CBP in signalling induced by interferon α Nature. 383:1996;344-347.
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(1996)
Nature
, vol.383
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Bhattacharya, S.1
Eckner, R.2
Grossman, S.3
Oldread, E.4
Arany, Z.5
D'Andrea, A.6
Livingston, D.M.7
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38
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0030449174
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Two contact regions between STAT1 and CBP/p300 ub interferon γ signaling
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Zhang JJ, Vinkemeier U, Gu W, Chakravarti D, Horvath CM, Darnell JE Jr. Two contact regions between STAT1 and CBP/p300 ub interferon γ signaling. Proc Natl Acad Sci USA. 93:1996;15092-15096.
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Proc Natl Acad Sci USA
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Zhang, J.J.1
Vinkemeier, U.2
Gu, W.3
Chakravarti, D.4
Horvath, C.M.5
Darnell J.E., Jr.6
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39
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0030024563
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Targeted disruption of the mouse Stat1 gene results in compromised innate immunity to viral disease
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Durbin JE, Hackenmiller R, Simon MC, Levy DE. Targeted disruption of the mouse Stat1 gene results in compromised innate immunity to viral disease. Cell. 84:1996;443-450.
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Cell
, vol.84
, pp. 443-450
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Durbin, J.E.1
Hackenmiller, R.2
Simon, M.C.3
Levy, D.E.4
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40
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13344282731
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Targeted disruption of the Stat1 gene in mice reveals unexpected physiologic specificity in the JAK-STAT signaling pathway
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Meraz MA, White JM, Sheehan KC, Bach EA, Rodig SJ, Dighe AS, Kaplan DH, Riley JK, Greenlund AC, Campbell D, et al. Targeted disruption of the Stat1 gene in mice reveals unexpected physiologic specificity in the JAK-STAT signaling pathway. Cell. 84:1996;431-442.
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Cell
, vol.84
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Meraz, M.A.1
White, J.M.2
Sheehan, K.C.3
Bach, E.A.4
Rodig, S.J.5
Dighe, A.S.6
Kaplan, D.H.7
Riley, J.K.8
Greenlund, A.C.9
Campbell, D.10
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41
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0030935260
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Targeted disruption of the mouse Stat3 gene leads to early embryonic lethality
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Takeda K, Noguchi K, Shi W, Tanaka T, Matsumoto M, Yoshida N, Kishimoto T, Akira S. Targeted disruption of the mouse Stat3 gene leads to early embryonic lethality. Proc Natl Acad Sci USA. 94:1997;3801-3804.
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Proc Natl Acad Sci USA
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Takeda, K.1
Noguchi, K.2
Shi, W.3
Tanaka, T.4
Matsumoto, M.5
Yoshida, N.6
Kishimoto, T.7
Akira, S.8
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42
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0029937270
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Impaired IL-12 responses and development of Th2 cells in STAT4-deficient mice
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Kaplan MH, Sun Y-L, Hoey T, Grusby MJ. Impaired IL-12 responses and development of Th2 cells in STAT4-deficient mice. Nature. 382:1996;174-177.
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(1996)
Nature
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Kaplan, M.H.1
Sun, Y.-L.2
Hoey, T.3
Grusby, M.J.4
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43
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15844396183
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