-
1
-
-
0028234529
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Jak-STAT pathways and transcriptional activation in response to IFNs and other extracellular signaling proteins
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Darnell JE Jr, Kerr IM, Stark GR. Jak-STAT pathways and transcriptional activation in response to IFNs and other extracellular signaling proteins. Science. 264:1994;1415-1421.
-
(1994)
Science
, vol.264
, pp. 1415-1421
-
-
Darnell J.E., Jr.1
Kerr, I.M.2
Stark, G.R.3
-
2
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0029655971
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Function of Stat2 protein in transcription activation by alpha interferon
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Qureshi SA, Leung S, Kerr IM, Stark GR, Darnell JJE. Function of Stat2 protein in transcription activation by alpha interferon. Mol Cell Biol. 16:1996;288-293.
-
(1996)
Mol Cell Biol
, vol.16
, pp. 288-293
-
-
Qureshi, S.A.1
Leung, S.2
Kerr, I.M.3
Stark, G.R.4
Darnell, J.J.E.5
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3
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0027327484
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JAK2 associates with the erythropoietin receptor and is tyrosine phosphorylated and activated following EPO stimulation
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Witthuhn B, Quelle FW, Silvennoinen O, Yi T, Tang B, Miura O, Ihle JN. JAK2 associates with the erythropoietin receptor and is tyrosine phosphorylated and activated following EPO stimulation. Cell. 74:1993;227-236.
-
(1993)
Cell
, vol.74
, pp. 227-236
-
-
Witthuhn, B.1
Quelle, F.W.2
Silvennoinen, O.3
Yi, T.4
Tang, B.5
Miura, O.6
Ihle, J.N.7
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4
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0029011115
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The amino-terminal portion of the JAK2 protein kinase is necessary for binding and phosphorylation of the granulocyte-macrophage colony-stimulating factor receptor βc chain
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Zhao Y, Wagner F, Franck SJ, Kraft AS. The amino-terminal portion of the JAK2 protein kinase is necessary for binding and phosphorylation of the granulocyte-macrophage colony-stimulating factor receptor βc chain. J Biol Chem. 270:1995;13814-13818.
-
(1995)
J Biol Chem
, vol.270
, pp. 13814-13818
-
-
Zhao, Y.1
Wagner, F.2
Franck, S.J.3
Kraft, A.S.4
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5
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0028180569
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JAK2 associates with the βc chain of the receptor for granulocyte-macrophage colony-stimulating factor, and its activation requires the membrane-proximal region
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Quelle FW, Sato N, Witthuhn BA, Inhorn RC, Eder M, Miyajima A, Griffin J, Ihle JN. JAK2 associates with the βc chain of the receptor for granulocyte-macrophage colony-stimulating factor, and its activation requires the membrane-proximal region. Mol Cell Biol. 14:1994;4335-4341.
-
(1994)
Mol Cell Biol
, vol.14
, pp. 4335-4341
-
-
Quelle, F.W.1
Sato, N.2
Witthuhn, B.A.3
Inhorn, R.C.4
Eder, M.5
Miyajima, A.6
Griffin, J.7
Ihle, J.N.8
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6
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0028957771
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The conserved box 1 motif of cytokine receptors is required for association with JAK kinases
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Tanner JW, Chen W, Young RL, Longmore GD, Shaw AS. The conserved box 1 motif of cytokine receptors is required for association with JAK kinases. J Biol Chem. 270:1995;6523-6530.
-
(1995)
J Biol Chem
, vol.270
, pp. 6523-6530
-
-
Tanner, J.W.1
Chen, W.2
Young, R.L.3
Longmore, G.D.4
Shaw, A.S.5
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7
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0029863420
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Molecular characterization of an alpha interferon receptor 1 subunit (IFNαR1) domain required for TYK2 binding and signal transduction
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Yan H, Krishnan K, Lim JTE, Contillo LG, Krolewski JJ. Molecular characterization of an alpha interferon receptor 1 subunit (IFNαR1) domain required for TYK2 binding and signal transduction. Mol Cell Biol. 16:1996;2074-2082.
-
(1996)
Mol Cell Biol
, vol.16
, pp. 2074-2082
-
-
Yan, H.1
Krishnan, K.2
Lim, J.T.E.3
Contillo, L.G.4
Krolewski, J.J.5
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8
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0028956353
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Specific recruitment of SH-PTP1 to the erythropoietin receptor causes inactivation of JAK2 and termination of proliferative signals
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of outstanding interest. This is the first demonstration that SHP-1 negatively regulates JAK. The authors also demonstrate the association of SHP-1, through its SH2 domain, with EPO receptor via its phosphorylated tyrosine residue. This model has now been extended to other cytokine receptors.
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Klingmuller U, Lorenz U, Cantley LC, Neel BG, Lodish HF. Specific recruitment of SH-PTP1 to the erythropoietin receptor causes inactivation of JAK2 and termination of proliferative signals. of outstanding interest Cell. 80:1995;729-738 This is the first demonstration that SHP-1 negatively regulates JAK. The authors also demonstrate the association of SHP-1, through its SH2 domain, with EPO receptor via its phosphorylated tyrosine residue. This model has now been extended to other cytokine receptors.
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(1995)
Cell
, vol.80
, pp. 729-738
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Klingmuller, U.1
Lorenz, U.2
Cantley, L.C.3
Neel, B.G.4
Lodish, H.F.5
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9
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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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of special interest. Complementation of SHP-1 to cells derived from an SHP-1 null mouse here shows that SHP-1 increases just the tyrosine phosphorylation of JAK1 and STAT1α but does not affect the activation of TYK2 and STAT2 as induced by IFNα. It appears that SHP-1 regulates the member of JAK and STAT differentially.
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David M, Chen H, 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. of special interest Mol Cell Biol. 15:1995;7050-7058 Complementation of SHP-1 to cells derived from an SHP-1 null mouse here shows that SHP-1 increases just the tyrosine phosphorylation of JAK1 and STAT1α but does not affect the activation of TYK2 and STAT2 as induced by IFNα. It appears that SHP-1 regulates the member of JAK and STAT differentially.
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(1995)
Mol Cell Biol
, vol.15
, pp. 7050-7058
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David, M.1
Chen, H.2
Goelz, S.3
Larner, A.C.4
Neel, B.G.5
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10
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0028074204
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Inhibition of erythropoietin-induced mitogenesis by a kinase-deficient form of Jak2
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Zhuang H, Patel SV, He T-C, Sonsteby SK, Niu Z, Wojchowski DM. Inhibition of erythropoietin-induced mitogenesis by a kinase-deficient form of Jak2. J Biol Chem. 269:1994;21411-21414.
-
(1994)
J Biol Chem
, vol.269
, pp. 21411-21414
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Zhuang, H.1
Patel, S.V.2
He T-C3
Sonsteby, S.K.4
Niu, Z.5
Wojchowski, D.M.6
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11
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15844389026
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JAK2 is essential for activation of c-fos and c-myc promoters and cell proliferation through the human granulocyte - Macrophage colony-stimulating factor receptor in BA/F3 cells
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of special interest. Experiments using dominant negative JAK2 show that all the known activities centering on c-fos gene activation and cell proliferation as induced by hGM - CSF are mediated by JAK2. JAK2 is also shown to mediate phosphorylation of tyrosine residues of the receptor.
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Watanabe S, Itoh T, Arai K. JAK2 is essential for activation of c-fos and c-myc promoters and cell proliferation through the human granulocyte - macrophage colony-stimulating factor receptor in BA/F3 cells. of special interest J Biol Chem. 271:1996;12681-12686 Experiments using dominant negative JAK2 show that all the known activities centering on c-fos gene activation and cell proliferation as induced by hGM - CSF are mediated by JAK2. JAK2 is also shown to mediate phosphorylation of tyrosine residues of the receptor.
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(1996)
J Biol Chem
, vol.271
, pp. 12681-12686
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Watanabe, S.1
Itoh, T.2
Arai, K.3
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12
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0030062769
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Kinase-negative mutants of JAK1 can sustain interferon-γ-inducible gene expression but not an antiviral state
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of outstanding interest. By complementing kinase negative JAK1 or JAK2 to cells lacking either JAK1 or JAK2, the authors show that the kinase activity of JAK1 is dispensable for IFNγ activity, even though JAK1 protein is essential for IFNγ signaling. This indicates that JAK1 plays a structural role in the correct assembly and function of receptors. This work provides an insight in the analysis of other cytokines which activate multiple JAKs.
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Briscoe J, Rogers NC, Witthuhn BA, Watling D, Harpur AG, Wilks AF, Stark GR, Ihle JN, Kerr IM. Kinase-negative mutants of JAK1 can sustain interferon-γ-inducible gene expression but not an antiviral state. of outstanding interest EMBO J. 15:1996;799-809 By complementing kinase negative JAK1 or JAK2 to cells lacking either JAK1 or JAK2, the authors show that the kinase activity of JAK1 is dispensable for IFNγ activity, even though JAK1 protein is essential for IFNγ signaling. This indicates that JAK1 plays a structural role in the correct assembly and function of receptors. This work provides an insight in the analysis of other cytokines which activate multiple JAKs.
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(1996)
EMBO J
, vol.15
, pp. 799-809
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Briscoe, J.1
Rogers, N.C.2
Witthuhn, B.A.3
Watling, D.4
Harpur, A.G.5
Wilks, A.F.6
Stark, G.R.7
Ihle, J.N.8
Kerr, I.M.9
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13
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0027993022
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Functional activation of Jak1 and Jak3 by selective associates with IL-2 receptor subunits
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Miyazaki T, Kawahara A, Fujii H, Nakagawa Y, Minami Y, Liu ZJ, Oishi I, Silvennoinen O, Witthuhn BA, Ihle JN, Taniguchi T. Functional activation of Jak1 and Jak3 by selective associates with IL-2 receptor subunits. Science. 266:1994;1045-1047.
-
(1994)
Science
, vol.266
, pp. 1045-1047
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Miyazaki, T.1
Kawahara, A.2
Fujii, H.3
Nakagawa, Y.4
Minami, Y.5
Liu, Z.J.6
Oishi, I.7
Silvennoinen, O.8
Witthuhn, B.A.9
Ihle, J.N.10
Taniguchi, T.11
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14
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0030046753
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STATs: Signal transducers and activators of transcription
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Ihle JN. STATs: signal transducers and activators of transcription. Cell. 84:1996;331-334.
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(1996)
Cell
, vol.84
, pp. 331-334
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Ihle, J.N.1
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15
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0029958784
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A novel STAT-like factor mediates lipopolysaccharide, interleukin 1 (IL-1), and IL-6 signaling and recognizes a gamma interferon activation site-like element in the IL1B gene
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Tsukada J, Waterman WR, Koyama Y, Webb AC, Auron PE. A novel STAT-like factor mediates lipopolysaccharide, interleukin 1 (IL-1), and IL-6 signaling and recognizes a gamma interferon activation site-like element in the IL1B gene. Mol Cell Biol. 16:1996;2183-2194.
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(1996)
Mol Cell Biol
, vol.16
, pp. 2183-2194
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Tsukada, J.1
Waterman, W.R.2
Koyama, Y.3
Webb, A.C.4
Auron, P.E.5
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16
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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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17
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0029869176
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The SH2 domains of Stat1 and Stat2 mediate multiple interactions in the transduction of IFN-α signals
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of special interest. The functions of the SH2 domains of STAT1 and STAT2 here have been analysed in vitro. The authors show that the SH2 domain plays a role in the formation of homodimerization and heterodimerization of STAT through its phosphotyrosine residue.
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Gupta S, Yan H, Wong LH, Ralph S, Krolewski J, Schindler C. The SH2 domains of Stat1 and Stat2 mediate multiple interactions in the transduction of IFN-α signals. of special interest EMBO J. 15:1996;1075-1084 The functions of the SH2 domains of STAT1 and STAT2 here have been analysed in vitro. The authors show that the SH2 domain plays a role in the formation of homodimerization and heterodimerization of STAT through its phosphotyrosine residue.
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(1996)
EMBO J
, vol.15
, pp. 1075-1084
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Gupta, S.1
Yan, H.2
Wong, L.H.3
Ralph, S.4
Krolewski, J.5
Schindler, C.6
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18
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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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of outstanding interest. Serine residue of STAT is phosphorylated following stimulation by a cytokine or growth factor. Reconstitution of STAT α-carrying mutation to the serine residue in cells lacking STAT1 shows that serine residues are required for maximal transcriptional activity but not for DNA binding.
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Wen Z, Zhong A, Darnell JE. Maximal activation of transcription by Stat1 and Stat3 requires both tyrosine and serine phosphorylation. of outstanding interest Cell. 82:1995;241-250 Serine residue of STAT is phosphorylated following stimulation by a cytokine or growth factor. Reconstitution of STAT α-carrying mutation to the serine residue in cells lacking STAT1 shows that serine residues are required for maximal transcriptional activity but not for DNA binding.
-
(1995)
Cell
, vol.82
, pp. 241-250
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Wen, Z.1
Zhong, A.2
Darnell, J.E.3
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19
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0029066128
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Differentiation-regulated serine phosphorylation of STAT1 promotes GAF activation in macrophages
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of special interest. Involvement of the JAK-STAT pathway in the differentiation of hematopoietic cells is an interesting issue. This report indicates that the increase in JAK-STAT activity is coincident with monocytic U937 differentiation. The authors also report that phosphorylation of the serine rather than tyrosine residue is responsible for augmentation of STAT activity.
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Eilers A, Georgellis D, Klose B, Schindler C, Ziemiecki A, Harpur AG, Wilks AF, Decker T. Differentiation-regulated serine phosphorylation of STAT1 promotes GAF activation in macrophages. of special interest Mol Cell Biol. 15:1995;3579-3586 Involvement of the JAK-STAT pathway in the differentiation of hematopoietic cells is an interesting issue. This report indicates that the increase in JAK-STAT activity is coincident with monocytic U937 differentiation. The authors also report that phosphorylation of the serine rather than tyrosine residue is responsible for augmentation of STAT activity.
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(1995)
Mol Cell Biol
, vol.15
, pp. 3579-3586
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-
Eilers, A.1
Georgellis, D.2
Klose, B.3
Schindler, C.4
Ziemiecki, A.5
Harpur, A.G.6
Wilks, A.F.7
Decker, T.8
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20
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0029133702
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Requirement for MAP kinase (ERK2) activity in interferon α- and interferon β-stimulated gene expression through STAT proteins
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of outstanding interest. The involvement of MAPK is suggested in phosphorylation of the critical serine residue of STAT, in response to IFNα/β. In addition, co-precipitation of MAPK with IFNα/β receptor was implicated. Further experiments are needed to confirm this report because activation of the MAPK cascade by IFN has not been describe before.
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David M, Petricoin E III, Benjamin C, Pine R, Weber MJ, Larner AC. Requirement for MAP kinase (ERK2) activity in interferon α- and interferon β-stimulated gene expression through STAT proteins. of outstanding interest Science. 269:1995;1721-1723 The involvement of MAPK is suggested in phosphorylation of the critical serine residue of STAT, in response to IFNα/β. In addition, co-precipitation of MAPK with IFNα/β receptor was implicated. Further experiments are needed to confirm this report because activation of the MAPK cascade by IFN has not been describe before.
-
(1995)
Science
, vol.269
, pp. 1721-1723
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David, M.1
Petricoin E. III2
Benjamin, C.3
Pine, R.4
Weber, M.J.5
Larner, A.C.6
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21
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0028798823
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Role of STAT2 in the alpha interferon signaling pathway
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Leung S, Oureshi SA, Kerr IM, Darnell JJE, Stark GR. Role of STAT2 in the alpha interferon signaling pathway. Mol Cell Biol. 15:1995;1312-1317.
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(1995)
Mol Cell Biol
, vol.15
, pp. 1312-1317
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Leung, S.1
Oureshi, S.A.2
Kerr, I.M.3
Darnell, J.J.E.4
Stark, G.R.5
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22
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0028857954
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Mutation of Jak3 in a patient with SCID: Essential role of Jak3 in lymphoid development
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of special interest. Certain mutations within the γ subunit cause SCID and JAK3 is known to associate with this; a JAK3 mutation has therefore been expected to cause a similar phenotype. The authors report SCID patients carrying a JAK3 mutation. It appears that a JAK3 mutation now accounts for the SCID phenotype of γ subunit mutants.
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Russell SM, Tayebi N, Nakajima H, Riedy MC, Roberts JL, Aman MJ, Migone T, Noguchi M, Markert ML, Buckley RH, et al. Mutation of Jak3 in a patient with SCID: essential role of Jak3 in lymphoid development. of special interest Science. 270:1995;797-800 Certain mutations within the γ subunit cause SCID and JAK3 is known to associate with this; a JAK3 mutation has therefore been expected to cause a similar phenotype. The authors report SCID patients carrying a JAK3 mutation. It appears that a JAK3 mutation now accounts for the SCID phenotype of γ subunit mutants.
-
(1995)
Science
, vol.270
, pp. 797-800
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Russell, S.M.1
Tayebi, N.2
Nakajima, H.3
Riedy, M.C.4
Roberts, J.L.5
Aman, M.J.6
Migone, T.7
Noguchi, M.8
Markert, M.L.9
Buckley, R.H.10
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23
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0029164841
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Mutations of Jak-3 gene in patients with autosomal severe combined immune deficiency (SCID)
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Macchi P, Villa A, Giliani S, Sacco MG, Frattini A, Porta F, Ugazio AG, Johnston JA, Candotti F, O'Shea JJ, Vezzoni P, Notarangelo LD. Mutations of Jak-3 gene in patients with autosomal severe combined immune deficiency (SCID). Nature. 377:1995;65-68.
-
(1995)
Nature
, vol.377
, pp. 65-68
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-
Macchi, P.1
Villa, A.2
Giliani, S.3
Sacco, M.G.4
Frattini, A.5
Porta, F.6
Ugazio, A.G.7
Johnston, J.A.8
Candotti, F.9
O'Shea, J.J.10
Vezzoni, P.11
Notarangelo, L.D.12
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24
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0028840706
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Defective lymphoid development in mice lacking Jak3
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Nosaka T, Van Deursen JMA, Tripp RA, Thierfelder WE, Witthuhn BA, McMickle AP, Doherty PC, Grosveld GC, Ihle JN. Defective lymphoid development in mice lacking Jak3. Science. 270:1995;800-802.
-
(1995)
Science
, vol.270
, pp. 800-802
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Nosaka, T.1
Van Deursen, J.M.A.2
Tripp, R.A.3
Thierfelder, W.E.4
Witthuhn, B.A.5
McMickle, A.P.6
Doherty, P.C.7
Grosveld, G.C.8
Ihle, J.N.9
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25
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0028799457
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Defects in B lymphocyte maturation and T lymphocyte activation in mice lacking Jak3
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Thomis DC, Gurniak CB, Tivol E, Sharpe AH, Berg LJ. Defects in B lymphocyte maturation and T lymphocyte activation in mice lacking Jak3. Science. 270:1995;794-797.
-
(1995)
Science
, vol.270
, pp. 794-797
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Thomis, D.C.1
Gurniak, C.B.2
Tivol, E.3
Sharpe, A.H.4
Berg, L.J.5
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26
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0028946158
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Contribution of STAT SH2 groups to specific interferon signaling by the Jak-STAT pathway
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Heim MH, Kerr IM, Stark GR, Darnell JJE. Contribution of STAT SH2 groups to specific interferon signaling by the Jak-STAT pathway. Science. 267:1995;1347-1349.
-
(1995)
Science
, vol.267
, pp. 1347-1349
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Heim, M.H.1
Kerr, I.M.2
Stark, G.R.3
Darnell, J.J.E.4
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27
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0028175454
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Ligand-induced IFNγ receptor tyrosine phosphorylation couples the receptor to its signal transduction system (p91)
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Greenlund AC, Farrar MA, Viviano BL, Schreiber RD. Ligand-induced IFNγ receptor tyrosine phosphorylation couples the receptor to its signal transduction system (p91). EMBO J. 13:1994;1591-1600.
-
(1994)
EMBO J
, vol.13
, pp. 1591-1600
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Greenlund, A.C.1
Farrar, M.A.2
Viviano, B.L.3
Schreiber, R.D.4
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28
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0027972046
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An interleukin-4-induced transcription factor: IL-4 Stat
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Hou J, Schindler U, Henzel WJ, Ho TC, Brasseur M, McKnight SL. An interleukin-4-induced transcription factor: IL-4 Stat. Science. 265:1994;1701-1706.
-
(1994)
Science
, vol.265
, pp. 1701-1706
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-
Hou, J.1
Schindler, U.2
Henzel, W.J.3
Ho, T.C.4
Brasseur, M.5
McKnight, S.L.6
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29
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0028228543
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Stat4, a novel gamma interferon activation site-binding protein expressed in early myeloid differentiation
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Yamamoto K, Quelli FW, Thierfelder WE, Kreider BL, Gilbert DJ, Jenkins NA, Copeland NG, Silvennoinen O, Ihle JN. Stat4, a novel gamma interferon activation site-binding protein expressed in early myeloid differentiation. Mol Cell Biol. 14:1994;4342-4349.
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(1994)
Mol Cell Biol
, vol.14
, pp. 4342-4349
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-
Yamamoto, K.1
Quelli, F.W.2
Thierfelder, W.E.3
Kreider, B.L.4
Gilbert, D.J.5
Jenkins, N.A.6
Copeland, N.G.7
Silvennoinen, O.8
Ihle, J.N.9
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30
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0028931604
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Choice of STATs and other substrates specified by modular tyrosine-based motifs in cytokine receptors
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of outstanding interest. This is the first demonstration of how to determine the specificity of STAT as activated by cytokine. Swapping of the region of the receptor containing tyrosine residue shows that choice of STAT for activation was determined by the tyrosine residue and the surrounding motif of the receptor.
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Stahl N, Farruggella TJ, Boulton TG, Zhong Z, Darnell JE Jr, Yancopoulos GD. Choice of STATs and other substrates specified by modular tyrosine-based motifs in cytokine receptors. of outstanding interest Science. 267:1995;1349-1353 This is the first demonstration of how to determine the specificity of STAT as activated by cytokine. Swapping of the region of the receptor containing tyrosine residue shows that choice of STAT for activation was determined by the tyrosine residue and the surrounding motif of the receptor.
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(1995)
Science
, vol.267
, pp. 1349-1353
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Stahl, N.1
Farruggella, T.J.2
Boulton, T.G.3
Zhong, Z.4
Darnell J.E., Jr.5
Yancopoulos, G.D.6
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31
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0013077966
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Identification of tyrosine residues within the intracellular domain of the erythropoietin receptor crucial for STAT5 activation
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Gobert S, Chretien S, Gouilleux F, Muller O, Pallard C, Dusanter-Fourt I, Groner B, Lacombe C, Gisselbrecht S, Mayeux P. Identification of tyrosine residues within the intracellular domain of the erythropoietin receptor crucial for STAT5 activation. EMBO J. 15:1996;2434-2441.
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(1996)
EMBO J
, vol.15
, pp. 2434-2441
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Gobert, S.1
Chretien, S.2
Gouilleux, F.3
Muller, O.4
Pallard, C.5
Dusanter-Fourt, I.6
Groner, B.7
Lacombe, C.8
Gisselbrecht, S.9
Mayeux, P.10
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32
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0029670220
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Phosphorylated interferon-α receptor 1 subunit (IFNaR1) acts as a docking site for the latent form of the 113 kDa STAT2 protein
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Yan H, Krishnan K, Greenlund AC, Gupta S, Lim JTE, Schreiber RD, Schindler CW, Krolewski JJ. Phosphorylated interferon-α receptor 1 subunit (IFNaR1) acts as a docking site for the latent form of the 113 kDa STAT2 protein. EMBO J. 15:1996;1064-1074.
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(1996)
EMBO J
, vol.15
, pp. 1064-1074
-
-
Yan, H.1
Krishnan, K.2
Greenlund, A.C.3
Gupta, S.4
Lim, J.T.E.5
Schreiber, R.D.6
Schindler, C.W.7
Krolewski, J.J.8
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33
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0028962572
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The role of shared receptor motifs and common Stat proteins in the generation of cytokine pleiotropy and redundancy by IL-2, IL-4, IL-7, IL-13, and IL-15
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of special interest. The γc subunit is shared by several cytokine receptors, yet JAK and STAT activated by these cytokines are not the same. After extensive analyses to understand this redundancy and pleiotropy, the authors found that there is a correlation between receptor motifs and activated STATs. This type of study may also provide information regarding redundancy and pleiotropy of the gp130-related cytokine system.
-
Lin J-X, Migone T-S, Tsang M, Friedmann M, Weatherbee JA, Zhou L, Yamauchi A, Bloom ET, Mietz J, John S, Leonard WJ. The role of shared receptor motifs and common Stat proteins in the generation of cytokine pleiotropy and redundancy by IL-2, IL-4, IL-7, IL-13, and IL-15. of special interest Immunity. 2:1995;331-339 The γc subunit is shared by several cytokine receptors, yet JAK and STAT activated by these cytokines are not the same. After extensive analyses to understand this redundancy and pleiotropy, the authors found that there is a correlation between receptor motifs and activated STATs. This type of study may also provide information regarding redundancy and pleiotropy of the gp130-related cytokine system.
-
(1995)
Immunity
, vol.2
, pp. 331-339
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-
Lin J-X1
Migone T-S2
Tsang, M.3
Friedmann, M.4
Weatherbee, J.A.5
Zhou, L.6
Yamauchi, A.7
Bloom, E.T.8
Mietz, J.9
John, S.10
Leonard, W.J.11
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34
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0029916933
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Activation and association of Stat3 with Src in v-Src-transformed cell lines
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of special interest. The role of JAK on STAT phosphorylation has become a widely accepted dogma. This study demonstrates the possibility that phosphorylation or activation of STAT may occur via Src tyrosine kinase. This study also implicates the role of STAT in transformation.
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Cao X, Tay A, Guy G, Tan YH. Activation and association of Stat3 with Src in v-Src-transformed cell lines. of special interest Mol Cell Biol. 16:1996;1595-1603 The role of JAK on STAT phosphorylation has become a widely accepted dogma. This study demonstrates the possibility that phosphorylation or activation of STAT may occur via Src tyrosine kinase. This study also implicates the role of STAT in transformation.
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(1996)
Mol Cell Biol
, vol.16
, pp. 1595-1603
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Cao, X.1
Tay, A.2
Guy, G.3
Tan, Y.H.4
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35
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0029069540
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Enhanced DNA-binding activity of a Stat3-related protein in cells transformed by the Src oncoprotein
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of special interest. This paper has a conclusion similar to that of [34]. The authors suggest an indirect mechanism for the interaction of Src and STAT because they observe JAK activation in Src transformed cells.
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Yu CL, Meyer DJ, Campbell GS, Lamar AC, Carter-Su C, Schwartz J, Jove R. Enhanced DNA-binding activity of a Stat3-related protein in cells transformed by the Src oncoprotein. of special interest Science. 269:1995;81-83 This paper has a conclusion similar to that of [34]. The authors suggest an indirect mechanism for the interaction of Src and STAT because they observe JAK activation in Src transformed cells.
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(1995)
Science
, vol.269
, pp. 81-83
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-
Yu, C.L.1
Meyer, D.J.2
Campbell, G.S.3
Lamar, A.C.4
Carter-Su, C.5
Schwartz, J.6
Jove, R.7
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36
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0028303977
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Molecular cloning of APRF, a novel ISGF3 p91-related transcription factor involved in the gp 130-mediated signaling pathway
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Akira S, Nishio Y, Inoue M, Wang X, Wei S, Matsusaka T, Yoshida K, Sudo T, Naruto M, Kishimoto T. Molecular cloning of APRF, a novel ISGF3 p91-related transcription factor involved in the gp 130-mediated signaling pathway. Cell. 77:1994;63-71.
-
(1994)
Cell
, vol.77
, pp. 63-71
-
-
Akira, S.1
Nishio, Y.2
Inoue, M.3
Wang, X.4
Wei, S.5
Matsusaka, T.6
Yoshida, K.7
Sudo, T.8
Naruto, M.9
Kishimoto, T.10
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37
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0028349735
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A stat family member activated by tyrosine phosphorylation in response to epidermal growth factor and interleukin-6
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Zhong Z, Wen Z, Darnell JE Jr. a stat family member activated by tyrosine phosphorylation in response to epidermal growth factor and interleukin-6. Science. 264:1994;95-98.
-
(1994)
Science
, vol.264
, pp. 95-98
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Zhong, Z.1
Wen, Z.2
Darnell J.E., Jr.3
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38
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0028217452
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Mammary gland factor (MGF) is a novel member of the cytokine regulated transcription factor gene family and confers the prolactin response
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Wakao H, Gouilleux F, Groner B. Mammary gland factor (MGF) is a novel member of the cytokine regulated transcription factor gene family and confers the prolactin response. EMBO J. 13:1994;2182-2191.
-
(1994)
EMBO J
, vol.13
, pp. 2182-2191
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-
Wakao, H.1
Gouilleux, F.2
Groner, B.3
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39
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0029952277
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The lipopolysaccharide-binding protein is a secretory class 1 acute-phase protein whose gene is transcriptionally activated by APRF/STAT-3 and other cytokine-inducible nuclear proteins
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Schumann RR, Kirschning CJ, Unbehaun A, Aberle H, Knopf H-P, Lamping N, Ulevitch RJ, Herrmann F. The lipopolysaccharide-binding protein is a secretory class 1 acute-phase protein whose gene is transcriptionally activated by APRF/STAT-3 and other cytokine-inducible nuclear proteins. Mol Cell Biol. 16:1996;3490-3503.
-
(1996)
Mol Cell Biol
, vol.16
, pp. 3490-3503
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Schumann, R.R.1
Kirschning, C.J.2
Unbehaun, A.3
Aberle, H.4
Knopf H-P5
Lamping, N.6
Ulevitch, R.J.7
Herrmann, F.8
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40
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0029892399
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Suppression of interleukin-3-induced gene expression by a C-terminal truncated Stat5: Role of Stat5 in proliferation
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Mui AL-F, Wakao H, Kinoshita T, Kitamura T, Miyajima A. Suppression of interleukin-3-induced gene expression by a C-terminal truncated Stat5: role of Stat5 in proliferation. EMBO J. 15:1996;2425-2433.
-
(1996)
EMBO J
, vol.15
, pp. 2425-2433
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Mui AL-F1
Wakao, H.2
Kinoshita, T.3
Kitamura, T.4
Miyajima, A.5
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41
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0029057858
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Cloning of murine stat6 and human stat6, stat proteins that are tyrosine phosphorylated in responses to IL-4 and IL-3 but are not required for mitogenesis
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Quelle FW, Shimoda K, Thierfelder W, Fischer C, Kim A, Ruben SM, Cleveland JL, Pierce JH, Keegan AD, Nelms K, et al. Cloning of murine stat6 and human stat6, stat proteins that are tyrosine phosphorylated in responses to IL-4 and IL-3 but are not required for mitogenesis. Mol Cell Biol. 15:1995;3336-3343.
-
(1995)
Mol Cell Biol
, vol.15
, pp. 3336-3343
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-
Quelle, F.W.1
Shimoda, K.2
Thierfelder, W.3
Fischer, C.4
Kim, A.5
Ruben, S.M.6
Cleveland, J.L.7
Pierce, J.H.8
Keegan, A.D.9
Nelms, K.10
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42
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0029866781
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Erythropoietin induces activation of Stat5 through association with specific tyrosines on the receptor that are not required for a mitogenic response
-
of outstanding interest. The authors describe the tyrosine residue of Epo receptor, which is required for activation of STAT5 by erythropoietin. As mutation of the tyrosine does not affect cell proliferation induced by Epo, the authors speculate that proliferation and STAT5 activation are separated in Epo signaling.
-
Quelle FW, Wang D, Nosaka T, Thierfelder WE, Stravopodis D, Weinstein Y, Ihle JN. Erythropoietin induces activation of Stat5 through association with specific tyrosines on the receptor that are not required for a mitogenic response. of outstanding interest Mol Cell Biol. 16:1996;1622-1631 The authors describe the tyrosine residue of Epo receptor, which is required for activation of STAT5 by erythropoietin. As mutation of the tyrosine does not affect cell proliferation induced by Epo, the authors speculate that proliferation and STAT5 activation are separated in Epo signaling.
-
(1996)
Mol Cell Biol
, vol.16
, pp. 1622-1631
-
-
Quelle, F.W.1
Wang, D.2
Nosaka, T.3
Thierfelder, W.E.4
Stravopodis, D.5
Weinstein, Y.6
Ihle, J.N.7
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43
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0029923780
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Cell growth arrest and induction of cyclin-dependent kinase inhibitor p21WAF1/CIP1 mediated by STAT1
-
of outstanding interest. This paper describes a relationship between STAT1 activation and the inhibition of cell growth by EGF and IFNγ. Inhibition is caused by recognition of the STAT binding site in the promoter region of cyclin-dependent kinase inhibitor p21 by activated STAT1. This is the first report describing both negative regulation via the JAK - STAT pathway and the relationship between cell cycle machinery and JAK - STAT signaling.
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Chin YE, Kitagawa M, Su W-CS, You A-H, Iwamoto Y, Fu X-Y. Cell growth arrest and induction of cyclin-dependent kinase inhibitor p21WAF1/CIP1 mediated by STAT1. of outstanding interest Science. 272:1996;719-721 This paper describes a relationship between STAT1 activation and the inhibition of cell growth by EGF and IFNγ. Inhibition is caused by recognition of the STAT binding site in the promoter region of cyclin-dependent kinase inhibitor p21 by activated STAT1. This is the first report describing both negative regulation via the JAK - STAT pathway and the relationship between cell cycle machinery and JAK - STAT signaling.
-
(1996)
Science
, vol.272
, pp. 719-721
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Chin, Y.E.1
Kitagawa, M.2
Su W-CS3
You A-H4
Iwamoto, Y.5
Fu X-Y6
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44
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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
-
of special interest. The authors here and in [45] arrive at the same conclusion that STAT1 is essential for IFNα/b and IFNγ signaling but not for other cytokines, such as IL-10, GH and EGF, which are known to activate STAT1.
-
Meraz MA, White JM, Sheehan KCF, Bach EA, Rodig SJ, Dighe AS, Kaplan DH, Riley JK, Greenlund AC, Campbell. Targeted disruption of the Stat1 gene in mice reveals unexpected physiologic specificity in the Jak-Stat signaling pathway. of special interest Cell. 84:1996;431-442 The authors here and in [45] arrive at the same conclusion that STAT1 is essential for IFNα/b and IFNγ signaling but not for other cytokines, such as IL-10, GH and EGF, which are known to activate STAT1.
-
(1996)
Cell
, vol.84
, pp. 431-442
-
-
Meraz, M.A.1
White, J.M.2
Sheehan, K.C.F.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
Campbell10
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45
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0030024563
-
Targeted disruption of the mouse Stat1 gene results in compromised innate immunity to viral disease
-
of special interest. The specific requirement of STAT1 for IFN activities but not for other cytokines is unexpected. It is of interest to examine whether or not other STATs, such as STAT3, can substitute STAT1 or has redundant activity of STAT1 in other cytokine signals.
-
Durbin JE, Hackenmiller R, Simon MC, Levy DE. Targeted disruption of the mouse Stat1 gene results in compromised innate immunity to viral disease. of special interest Cell. 84:1996;443-450 The specific requirement of STAT1 for IFN activities but not for other cytokines is unexpected. It is of interest to examine whether or not other STATs, such as STAT3, can substitute STAT1 or has redundant activity of STAT1 in other cytokine signals.
-
(1996)
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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46
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0029937270
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Impaired IL-12 responses and enhanced development of Th2 cells in Stat4-deficient mice
-
of special interest. IL-12 promotes Th1 development but the molecular mechanisms that regulate differentiation of Th1 and Th2 cells are largely unknown. IL - 12 is known to activate STAT4; this study and [47] reconfirms this at various levels. STAT4 knockout mice have an impaired development of Th1 cells in response to IL-12. This report provides an important clue regarding differentiation of Th1 cells.
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Kaplan MH, Sun Y-L, Hoey T, Grusby MJ. Impaired IL-12 responses and enhanced development of Th2 cells in Stat4-deficient mice. of special interest Nature. 382:1996;174-177 IL-12 promotes Th1 development but the molecular mechanisms that regulate differentiation of Th1 and Th2 cells are largely unknown. IL - 12 is known to activate STAT4; this study and [47] reconfirms this at various levels. STAT4 knockout mice have an impaired development of Th1 cells in response to IL-12. This report provides an important clue regarding differentiation of Th1 cells.
-
(1996)
Nature
, vol.382
, pp. 174-177
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-
Kaplan, M.H.1
Sun Y-L2
Hoey, T.3
Grusby, M.J.4
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47
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15844396183
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Requirement for Stat4 in interleukin-12 mediated responses of natural killer and T cells
-
of special interest. The conclusion of this paper is the same as that of [46] and also describes natural killer cell activity induced by IL-12. These reports show the primary and specific roles of STAT4 in all the known IL-12 activities tested. In addition, knockout of STAT1 and STAT6 implicate STAT protein specificity for particular cytokines.
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Thierfelder WE, Van Deursen JM, Yamamoto K, Tripp RA, Sarawar SR, Carson RT, Sangster MY, Vignali DAA, Doherty PC, Grosveld GC, Ihle JN. Requirement for Stat4 in interleukin-12 mediated responses of natural killer and T cells. of special interest Nature. 382:1996;171-174 The conclusion of this paper is the same as that of [46] and also describes natural killer cell activity induced by IL-12. These reports show the primary and specific roles of STAT4 in all the known IL-12 activities tested. In addition, knockout of STAT1 and STAT6 implicate STAT protein specificity for particular cytokines.
-
(1996)
Nature
, vol.382
, pp. 171-174
-
-
Thierfelder, W.E.1
Van Deursen, J.M.2
Yamamoto, K.3
Tripp, R.A.4
Sarawar, S.R.5
Carson, R.T.6
Sangster, M.Y.7
Vignali, D.A.A.8
Doherty, P.C.9
Grosveld, G.C.10
Ihle, J.N.11
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48
-
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15844404509
-
Essential role of Stat6 in IL-4 signalling
-
of special interest. Mice lacking STAT6 show defects in the IL-4 mediated response, such as expression of cell surface markers and B-cell proliferation co-stimulated by anti-IgM. These phenotypes were indistinguishable from those of IL-4 deficient mice. The authors conclude that - between two distinct signaling pathways mediated by STAT6 and 4PS described thus far - STAT6 plays a central role in exerting biological responses mediated by IL-4.
-
Takeda K, Tanaka T, Shi W, Matsumoto M, Minami M, Kashiwamura S, Nakanishi K, Yoshida N, Kishimoto T, Akira S. Essential role of Stat6 in IL-4 signalling. of special interest Nature. 380:1996;627-630 Mice lacking STAT6 show defects in the IL-4 mediated response, such as expression of cell surface markers and B-cell proliferation co-stimulated by anti-IgM. These phenotypes were indistinguishable from those of IL-4 deficient mice. The authors conclude that - between two distinct signaling pathways mediated by STAT6 and 4PS described thus far - STAT6 plays a central role in exerting biological responses mediated by IL-4.
-
(1996)
Nature
, vol.380
, pp. 627-630
-
-
Takeda, K.1
Tanaka, T.2
Shi, W.3
Matsumoto, M.4
Minami, M.5
Kashiwamura, S.6
Nakanishi, K.7
Yoshida, N.8
Kishimoto, T.9
Akira, S.10
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49
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15844374279
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Lack of IL-4-induced Th2 response and IgE class switching in mice with disrupted Stat6 gene
-
of special interest. This report also demonstrates impairment of various IL-4-mediated activities in STAT6 knockout mice. Interestingly, IL-4-mediated proliferation is only partially affected and this observation should be discussed in terms of involvement of STAT in cell proliferation.
-
Shimoda K, Van Deursen J, Sangster MY, Sarawar SR, Carson RT, Tripp RA, Chu C, Quelle FW, Nosaka T, Vignali DAA, et al. Lack of IL-4-induced Th2 response and IgE class switching in mice with disrupted Stat6 gene. of special interest Nature. 380:1996;630-633 This report also demonstrates impairment of various IL-4-mediated activities in STAT6 knockout mice. Interestingly, IL-4-mediated proliferation is only partially affected and this observation should be discussed in terms of involvement of STAT in cell proliferation.
-
(1996)
Nature
, vol.380
, pp. 630-633
-
-
Shimoda, K.1
Van Deursen, J.2
Sangster, M.Y.3
Sarawar, S.R.4
Carson, R.T.5
Tripp, R.A.6
Chu, C.7
Quelle, F.W.8
Nosaka, T.9
Vignali, D.A.A.10
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50
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0029876629
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Stat6 is required for mediating responses to IL-4 and for the development of Th2 cells
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of special interest. This paper describes an impairment of IL-13-induced cytokine production in T cells differentiated in vitro in addition to impairment of IL-4 activities in STAT6 knockout mice.
-
Kaplan MH, Schindler U, Smiley ST, Grusby MJ. Stat6 is required for mediating responses to IL-4 and for the development of Th2 cells. of special interest Immunity. 4:1996;313-319 This paper describes an impairment of IL-13-induced cytokine production in T cells differentiated in vitro in addition to impairment of IL-4 activities in STAT6 knockout mice.
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(1996)
Immunity
, vol.4
, pp. 313-319
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-
Kaplan, M.H.1
Schindler, U.2
Smiley, S.T.3
Grusby, M.J.4
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51
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0029005549
-
Constitutively activated Jak - STAT pathway in T cells transformed with HTLV-1
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of special interest. The mechanism of HTLV-1 transformation has long been studied and the role of Tax and other proteins encoded by the pX region is discussed. This report adds a new dimension to the study of the roles of the JAK-STAT pathway in cell transformation and proliferation.
-
Migone TS, Lin J-X, Cereseto A, Mulloy JC, O'Shea JJ, Franchini G, Leonard WJ. Constitutively activated Jak - STAT pathway in T cells transformed with HTLV-1. of special interest Science. 269:1995;79-81 The mechanism of HTLV-1 transformation has long been studied and the role of Tax and other proteins encoded by the pX region is discussed. This report adds a new dimension to the study of the roles of the JAK-STAT pathway in cell transformation and proliferation.
-
(1995)
Science
, vol.269
, pp. 79-81
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-
Migone, T.S.1
Lin J-X2
Cereseto, A.3
Mulloy, J.C.4
O'Shea, J.J.5
Franchini, G.6
Leonard, W.J.7
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52
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13344295097
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Inhibition of acute lymphoblastic leukaemia by a Jak-2 inhibitor
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Meydan N, Grunberger T, Dadi H, Shahar M, Arpaia E, Lapidot Z, Leeder JS, Freedman M, Cohen A, Gazit A, et al. Inhibition of acute lymphoblastic leukaemia by a Jak-2 inhibitor. Nature. 379:1996;645-648.
-
(1996)
Nature
, vol.379
, pp. 645-648
-
-
Meydan, N.1
Grunberger, T.2
Dadi, H.3
Shahar, M.4
Arpaia, E.5
Lapidot, Z.6
Leeder, J.S.7
Freedman, M.8
Cohen, A.9
Gazit, A.10
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53
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0029863169
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Tyrosyl phosphorylation and DNA binding activity of signal transducers and activators of transcription (STAT) proteins in hematopoietic cell lines transformed by Bcr/Abl
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Carlesso N, Frank DA, Griffin JD. Tyrosyl phosphorylation and DNA binding activity of signal transducers and activators of transcription (STAT) proteins in hematopoietic cell lines transformed by Bcr/Abl. J Exp Med. 183:1996;811-820.
-
(1996)
J Exp Med
, vol.183
, pp. 811-820
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Carlesso, N.1
Frank, D.A.2
Griffin, J.D.3
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54
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0030003920
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Lack of constitutive activation of Janus kinases and signal transduction and activation of transcription factors in philadelphia chromosome-positive acute lymphoblastic leukemia
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Kanwar VS, Witthuhn B, Campana D, Ihle JN. Lack of constitutive activation of Janus kinases and signal transduction and activation of transcription factors in philadelphia chromosome-positive acute lymphoblastic leukemia. Blood. 87:1996;4911-4912.
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(1996)
Blood
, vol.87
, pp. 4911-4912
-
-
Kanwar, V.S.1
Witthuhn, B.2
Campana, D.3
Ihle, J.N.4
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