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Darnell, J.E.1
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Cytokine receptor signal transduction and the control of hematopoietic cell development
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Interferon activation of the transcription factor Stat91 involves dimerization through SH2-phosphotyrosyl peptide interactions
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Extracellular signal-dependent nuclear import of Stat1 is mediated by nuclear pore-targeting complex formation with NPI-1, but not Rch1
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Sekimoto T, Imamoto N, Nakajima K, Hirano T, Yoneda Y. Extracellular signal-dependent nuclear import of Stat1 is mediated by nuclear pore-targeting complex formation with NPI-1, but not Rch1. EMBO J. 16:1997;7067-7077.
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0028916417
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Interleukin-3 signals through multiple forms of Stat5
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Azam M, Erdjument-Bromage H, Kreider BL, Xia M, Quelle F, Basu R, Saris C, Tempst P, Ihle JN, Schindler C. Interleukin-3 signals through multiple forms of Stat5. EMBO J. 14:1995;1402-1411.
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Basu, R.6
Saris, C.7
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7
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0028963550
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Interleukin-3, granulocyte-macrophage colony stimulating factor and interleukin-5 transduce signals through two STAT5 homologs
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Mui AL-F, Wakao H, O'Farrell A-M, Harada N, Miyajima A. Interleukin-3, granulocyte-macrophage colony stimulating factor and interleukin-5 transduce signals through two STAT5 homologs. EMBO J. 14:1995;1166-1175.
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Mui Al-F1
Wakao, H.2
O'Farrell A-M3
Harada, N.4
Miyajima, A.5
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0027772891
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Polypeptide signaling to the nucleus through tyrosine phosphorylation of Jak and Stat proteins
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Shuai K, Stark GR, Kerr IM, Darnell JE. Polypeptide signaling to the nucleus through tyrosine phosphorylation of Jak and Stat proteins. Nature. 366:1993;580-583.
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Shuai, K.1
Stark, G.R.2
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Darnell, J.E.4
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0027742729
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Interferon-induced nuclear signalling by Jak protein tyrosine kinases
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Silvennoinen O, Ihle JN, Schlessinger J, Levy DE. Interferon-induced nuclear signalling by Jak protein tyrosine kinases. Nature. 366:1993;583-585.
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Silvennoinen, O.1
Ihle, J.N.2
Schlessinger, J.3
Levy, D.E.4
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0027493650
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A single phosphotyrosine residue of Stat91 required for gene activation by inteferon-γ
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Shuai K, Stark GR, Kerr IM, Darnell JE. A single phosphotyrosine residue of Stat91 required for gene activation by inteferon-γ Science. 261:1993;1744-1746.
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Shuai, K.1
Stark, G.R.2
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Johnson LN, Noble ME, Owen DJ. Active and inactive protein kinases: structural basis for regulation. Cell. 85:1996;149-158.
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Johnson, L.N.1
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12
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0031282551
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Janus kinases in interleukin-2-mediated signaling: JAK1 and JAK3 are diffenentially regulated by tyrosine phosphorylation
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of special interest. This paper, together with Gauzzi et al., 1996 [13] and Feng et al., 1997 [14], defines the role of activation loop tyrosine residues in Janus kinases, with the surprising observation that, while Jak1, Jak2 and Tyk2 all require at least one of these residues for catalytic function, in Jak3 these residues are dispensable.
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Liu KD, Gaffen SL, Goldsmith MA, Greene WC. Janus kinases in interleukin-2-mediated signaling: JAK1 and JAK3 are diffenentially regulated by tyrosine phosphorylation. of special interest Curr Biol. 7:1997;817-826 This paper, together with Gauzzi et al., 1996 [13] and Feng et al., 1997 [14], defines the role of activation loop tyrosine residues in Janus kinases, with the surprising observation that, while Jak1, Jak2 and Tyk2 all require at least one of these residues for catalytic function, in Jak3 these residues are dispensable.
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Curr Biol
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Liu, K.D.1
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Goldsmith, M.A.3
Greene, W.C.4
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13
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0029786754
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Interferon-α-dependent activation of Tyk2 requires phosphorylation of positive regulatory tyrosines by another kinase
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of special interest. This paper, together with Liu et al., 1997 [12] and Feng et al., 1997 [14], defines the role of activation loop tyrosine residues in Janus kinases, with the surprising observation that, while Jak1, Jak2 and Tyk2 all require at least one of these residues for catalytic function, in Jak3 these residues are dispensable.
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Gauzzi MC, Velazquez L, McKendry R, Mogensen KE, Fellous M, Pellegrini S. Interferon-α-dependent activation of Tyk2 requires phosphorylation of positive regulatory tyrosines by another kinase. of special interest J Biol Chem. 271:1996;20494-20500 This paper, together with Liu et al., 1997 [12] and Feng et al., 1997 [14], defines the role of activation loop tyrosine residues in Janus kinases, with the surprising observation that, while Jak1, Jak2 and Tyk2 all require at least one of these residues for catalytic function, in Jak3 these residues are dispensable.
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J Biol Chem
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Gauzzi, M.C.1
Velazquez, L.2
McKendry, R.3
Mogensen, K.E.4
Fellous, M.5
Pellegrini, S.6
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14
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0030953469
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Activation of JAK2 catalytic activity requires phosphorylation of Y1007 in the kinase activation loop
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of special interest. This paper, together with Liu et al., 1997 [12] and Gauzzi et al., 1996 [13], defines the role of activation loop tyrosine residues in Janus kinases, with the surprising observation that, while Jak1, Jak2 and Tyk2 all require at least one of these residues for catalytic function, in Jak3 these residues are dispensable.
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Feng J, Witthuhn BA, Matsuda T, Kohlhuber F, Kerr IM, Ihle JN. Activation of JAK2 catalytic activity requires phosphorylation of Y1007 in the kinase activation loop. of special interest Mol Cell Biol. 17:1997;2497-2501 This paper, together with Liu et al., 1997 [12] and Gauzzi et al., 1996 [13], defines the role of activation loop tyrosine residues in Janus kinases, with the surprising observation that, while Jak1, Jak2 and Tyk2 all require at least one of these residues for catalytic function, in Jak3 these residues are dispensable.
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Mol Cell Biol
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Feng, J.1
Witthuhn, B.A.2
Matsuda, T.3
Kohlhuber, F.4
Kerr, I.M.5
Ihle, J.N.6
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Regulation of interferon-α responsiveness by the duration of Janus kinase activity
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Lee C-K, Bluyssen HAR, Levy DE. Regulation of interferon-α responsiveness by the duration of Janus kinase activity. J Biol Chem. 272:1997;21872-21877.
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Lee C-K1
Bluyssen, H.A.R.2
Levy, D.E.3
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16
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0029142798
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Signaling through the IL-2R β chain activates a STAT-5-like DNA binding activity
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Gaffen SL, Lai SY, Xu W, Gouilleux F, Groner B, Goldsmith MA, Greene WC. Signaling through the IL-2R β chain activates a STAT-5-like DNA binding activity. Proc Natl Acad Sci USA. 92:1995;7192-7196.
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Gaffen, S.L.1
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Xu, W.3
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Groner, B.5
Goldsmith, M.A.6
Greene, W.C.7
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17
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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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Jiao, H.1
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Platanias, L.C.5
Yi, T.6
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0031033714
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Molecular characterization of specific interactions between SHP-2 phosphatase and JAK tyrosine kinase
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Yin T, Shen R, Geng G-S, Yang Y-C. Molecular characterization of specific interactions between SHP-2 phosphatase and JAK tyrosine kinase. J Biol Chem. 272:1997;1032-1037.
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Yin, T.1
Shen, R.2
Geng G-S3
Yang Y-C4
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19
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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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of special interest. This is a particularly carefully performed study examining the turnover and nuclear import and export of Stat-1 in interferon-induced cells, in which the authors demonstrate convincingly that the majority of Stat-1 protein is recycled out of the nucleus rather than being degraded by proteasomes. Moreover, they perform a complete kinetic analysis of the duration of the interferon-induced response.
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Haspel RL, Salditt-Georgieff M, Darnell JE. The rapid inactivation of nuclear tyrosine phosphorylated STAT1 depends upon a protein tyrosine phosphatase. of special interest EMBO J. 15:1996;6262-6268 This is a particularly carefully performed study examining the turnover and nuclear import and export of Stat-1 in interferon-induced cells, in which the authors demonstrate convincingly that the majority of Stat-1 protein is recycled out of the nucleus rather than being degraded by proteasomes. Moreover, they perform a complete kinetic analysis of the duration of the interferon-induced response.
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(1996)
EMBO J
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Haspel, R.L.1
Salditt-Georgieff, M.2
Darnell, J.E.3
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20
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Regulation of interferon-γ-activated STAT1 by the ubiquitin-proteasome pathway
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Kim TK, Maniatis T. Regulation of interferon-γ-activated STAT1 by the ubiquitin-proteasome pathway. Science. 273:1996;1717-1719.
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Science
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Kim, T.K.1
Maniatis, T.2
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22
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0030792590
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A family of cytokine-inducible inhibitors of signalling
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of special interest. Collectively, Starr et al., Naka et al., 1997 [23], Endo et al., 1997 [24] and Chung et al., 1997 [26] provide the first evidence for a negative feedback loop controlling JAK/STAT responses, and identify new families of negative regulatory proteins involved in cytokine signaling.
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Starr R, Willson TA, Viney EM, Murray LJL, Rayner RR, 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 Collectively, Starr et al., Naka et al., 1997 [23], Endo et al., 1997 [24] and Chung et al., 1997 [26] provide the first evidence for a negative feedback loop controlling JAK/STAT responses, and identify new families of negative regulatory proteins involved in cytokine signaling.
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(1997)
Nature
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Starr, R.1
Willson, T.A.2
Viney, E.M.3
Murray, L.J.L.4
Rayner, R.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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23
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0030755934
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Structure and function of a new STAT-induced STAT inhibitor
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of special interest. Collectively, Naka et al., Starr et al., 1997 [22], Endo et al., 1997 [24] and Chung et al., 1997 [26] provide the first evidence for a negative feedback loop controlling JAK/STAT responses, and identify new families of negative regulatory proteins involved in cytokine signaling.
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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. of special interest Nature. 387:1997;924-928 Collectively, Naka et al., Starr et al., 1997 [22], Endo et al., 1997 [24] and Chung et al., 1997 [26] provide the first evidence for a negative feedback loop controlling JAK/STAT responses, and identify new families of negative regulatory proteins involved in cytokine signaling.
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(1997)
Nature
, vol.387
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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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24
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0030839112
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A new protein containing an SH2 domain that inhibits JAK kinases
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of special interest. Collectively, Endo et al., Starr et al., 1997 [22], Naka et al., 1997 [23] and Chung et al., 1997 [26] provide the first evidence for a negative feedback loop controlling JAK/STAT responses, and identify new families of negative regulatory proteins involved in cytokine signaling.
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Endo TA, Masahura M, Yokouchi M, Suzuki R, Sakamoto H, Mitsui K, Matsumoto A, Tanimura S, Ohtsubo M, Misawa H, et al. A new protein containing an SH2 domain that inhibits JAK kinases. of special interest Nature. 387:1997;921-924 Collectively, Endo et al., Starr et al., 1997 [22], Naka et al., 1997 [23] and Chung et al., 1997 [26] provide the first evidence for a negative feedback loop controlling JAK/STAT responses, and identify new families of negative regulatory proteins involved in cytokine signaling.
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(1997)
Nature
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Endo, T.A.1
Masahura, M.2
Yokouchi, M.3
Suzuki, R.4
Sakamoto, H.5
Mitsui, K.6
Matsumoto, A.7
Tanimura, S.8
Ohtsubo, M.9
Misawa, H.10
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25
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0029014206
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A novel cytokine-inducible gene CIS encodes and SH2-containing protein that binds to tyrosine-phosphorylated interleukin 2 and erythropoietin receptors
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Yoshimura A, Ohkubo T, Kiguchi T, Jenkins NA, Gilbert DJ, Copeland NG, Copeland NG, Hara T, Miyajima A. A novel cytokine-inducible gene CIS encodes and SH2-containing protein that binds to tyrosine-phosphorylated interleukin 2 and erythropoietin receptors. EMBO J. 14:1995;2816-2826.
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Yoshimura, A.1
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Gilbert, D.J.5
Copeland, N.G.6
Copeland, N.G.7
Hara, T.8
Miyajima, A.9
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26
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0030725378
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Specific inhibition of Stat3 signal transduction by PIAS3
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of special interest. Collectively, Chung et al., Starr et al., 197 [22], Naka et al., 1997 [23] and Endo et al., 1997 [24] provide the first evidence for a negative feedback loop controlling JAK/STAT responses, and identify new families of negative regulatory proteins involved in cytokine signaling.
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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 special interest Science. 278:1997;1803-1805 Collectively, Chung et al., Starr et al., 197 [22], Naka et al., 1997 [23] and Endo et al., 1997 [24] provide the first evidence for a negative feedback loop controlling JAK/STAT responses, and identify new families of negative regulatory proteins involved in cytokine signaling.
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Science
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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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27
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0028840706
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Defective lymphoid development in mice lacking Jack
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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 Jack. Science. 270:1995;800-802.
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Nosaka, T.1
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McMickle, A.P.6
Doherty, P.C.7
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Ihle, J.N.9
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28
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0029550822
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Park SY, Saijo K, Takahashi T, Osawa M, Arase H, Hirayama N, Miyakie K, Nakauchi H, Shirasawa T, Saito T. Developmental defects of lymphoid cells in JAK3 kinase-deficient mice. Immunity. 3:1995;771-782.
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Nakauchi, H.8
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Saito, T.10
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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.
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Defective lymphoid development in mice lacking expression of the common cytokine receptor γ chain
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Bloom, E.T.10
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Lymphoid development in mice with a targeted deletion of the interleukin 2 receptor γ chain
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Mutation of JAK3 gene in patients with autosomal severe iombined immune defiency (SCID)
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MacChi, P.1
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Mutation of Jak3 in a patient with SCID: Essential role of Jak3 in lymphoid development
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Russell, S.M.1
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Identification of a variable region within the cytoplasmic tail of the IL-2 receptor β chain that is required for growth signal transduction
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of special interest. The findings in this paper demonstrate that STATs may function not only as transcription factors but also as adaptor molecules. In this case, Stat-3 links phosphatidylinositol 3-kinase to the IFN receptor.
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Pfeffer LM, Mullersman JE, Pfeffer SR, Murti A, Yang CH. STAT3 as an adaptor to couple phosphatidylinositol 3-kinase to the IFNAR1 chain of the type I interferon receptor. of special interest Science. 276:1997;1418-1420 The findings in this paper demonstrate that STATs may function not only as transcription factors but also as adaptor molecules. In this case, Stat-3 links phosphatidylinositol 3-kinase to the IFN receptor.
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(1997)
Science
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Pfeffer, L.M.1
Mullersman, J.E.2
Pfeffer, S.R.3
Murti, A.4
Yang, C.H.5
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78
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8044231313
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An alternative pathway for STAT activation that is mediated by the direct interaction between JAK and STAT
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of special interest. While the predominant paradigm for STAT activation suggests that STATs bind to phosphorylated tyrosine residues on the activating receptor, this paper demonstrates that in some instances STATs may be delivered to the receptor complex by binding to JAKs instead. This explains some previous observations that certain receptors can activate STATs even in the absence of receptor tyrosine residues.
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Fujitani Y, Hibi M, Fukada T, Takahashi-Tezuka M, Yoshida H, Yamaguchi T, Sugiyama K, Yamanaka Y, Nakajima K, Hirano T. An alternative pathway for STAT activation that is mediated by the direct interaction between JAK and STAT. of special interest Oncogene. 14:1997;751-761 While the predominant paradigm for STAT activation suggests that STATs bind to phosphorylated tyrosine residues on the activating receptor, this paper demonstrates that in some instances STATs may be delivered to the receptor complex by binding to JAKs instead. This explains some previous observations that certain receptors can activate STATs even in the absence of receptor tyrosine residues.
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(1997)
Oncogene
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Fujitani, Y.1
Hibi, M.2
Fukada, T.3
Takahashi-Tezuka, M.4
Yoshida, H.5
Yamaguchi, T.6
Sugiyama, K.7
Yamanaka, Y.8
Nakajima, K.9
Hirano, T.10
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79
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Jak3 is associated with CD40 and is critical for CD40 induction of gene expression in B cells
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Hanissian SH, Geha RS. Jak3 is associated with CD40 and is critical for CD40 induction of gene expression in B cells. Immunity. 6:1997;379-387.
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(1997)
Immunity
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Hanissian, S.H.1
Geha, R.S.2
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80
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0030934461
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Interaction between Sam68 and src family tyrosine kinases, fyn and lck, in T cell receptor signaling
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Fusaki N, Iwamatsu A, Iwashima M, Fujisawa J-I. Interaction between Sam68 and src family tyrosine kinases, fyn and lck, in T cell receptor signaling. J Biol Chem. 272:1997;6214-6219.
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(1997)
J Biol Chem
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Fusaki, N.1
Iwamatsu, A.2
Iwashima, M.3
Fujisawa J-I4
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