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Volumn 118, Issue , 2019, Pages 48-63

The regulation of JAKs in cytokine signaling and its breakdown in disease

Author keywords

Cancer; Cytokine signaling; Janus kinase (JAK); Mutation; Myeloproliferative neoplasm (MPN)

Indexed keywords

CYTOKINE RECEPTOR; JANUS KINASE; STAT PROTEIN; CYTOKINE;

EID: 85045840532     PISSN: 10434666     EISSN: 10960023     Source Type: Journal    
DOI: 10.1016/j.cyto.2018.03.041     Document Type: Review
Times cited : (154)

References (257)
  • 1
    • 15444339209 scopus 로고    scopus 로고
    • A TEL-JAK2 fusion protein with constitutive kinase activity in human leukemia
    • Lacronique, V., Boureux, A., Valle, V.D., Poirel, H., Quang, C.T., Mauchauffe, M., et al. A TEL-JAK2 fusion protein with constitutive kinase activity in human leukemia. Science 278:5341 (1997), 1309–1312.
    • (1997) Science , vol.278 , Issue.5341 , pp. 1309-1312
    • Lacronique, V.1    Boureux, A.2    Valle, V.D.3    Poirel, H.4    Quang, C.T.5    Mauchauffe, M.6
  • 2
    • 79954606783 scopus 로고    scopus 로고
    • JAK2 rearrangements, including the novel SEC31A-JAK2 fusion, are recurrent in classical hodgkin lymphoma
    • Van Roosbroeck, K., Cox, L., Tousseyn, T., Lahortiga, I., Gielen, O., Cauwelier, B., et al. JAK2 rearrangements, including the novel SEC31A-JAK2 fusion, are recurrent in classical hodgkin lymphoma. Blood 117:15 (2011), 4056–4064.
    • (2011) Blood , vol.117 , Issue.15 , pp. 4056-4064
    • Van Roosbroeck, K.1    Cox, L.2    Tousseyn, T.3    Lahortiga, I.4    Gielen, O.5    Cauwelier, B.6
  • 4
    • 84963819722 scopus 로고    scopus 로고
    • Triple-negative breast cancers with amplification of JAK2 at the 9p24 locus demonstrate JAK2-specific dependence
    • Balko, J.M., Schwarz, L.J., Luo, N., Estrada, M.V., Giltnane, J.M., Davila-Gonzalez, D., et al. Triple-negative breast cancers with amplification of JAK2 at the 9p24 locus demonstrate JAK2-specific dependence. Sci. Transl. Med., 8(334), 2016, 334ra53.
    • (2016) Sci. Transl. Med. , vol.8 , Issue.334 , pp. 334ra53
    • Balko, J.M.1    Schwarz, L.J.2    Luo, N.3    Estrada, M.V.4    Giltnane, J.M.5    Davila-Gonzalez, D.6
  • 5
    • 84878232331 scopus 로고    scopus 로고
    • JAK/STAT signaling in hematological malignancies
    • Vainchenker, W., Constantinescu, S., JAK/STAT signaling in hematological malignancies. Oncogene 32 (2013), 2601–2613.
    • (2013) Oncogene , vol.32 , pp. 2601-2613
    • Vainchenker, W.1    Constantinescu, S.2
  • 6
    • 84939162798 scopus 로고    scopus 로고
    • Pathogenesis of myeloproliferative neoplasms
    • Skoda, R.C., Duek, A., Grisouard, J., Pathogenesis of myeloproliferative neoplasms. Exp. Hematol. 43:8 (2015), 599–608.
    • (2015) Exp. Hematol. , vol.43 , Issue.8 , pp. 599-608
    • Skoda, R.C.1    Duek, A.2    Grisouard, J.3
  • 7
    • 84938415522 scopus 로고    scopus 로고
    • The role of JAK/STAT signalling in the pathogenesis, prognosis and treatment of solid tumours
    • Thomas, S., Snowden, J., Zeidler, M., Danson, S., The role of JAK/STAT signalling in the pathogenesis, prognosis and treatment of solid tumours. Br. J. Cancer 113:3 (2015), 365–371.
    • (2015) Br. J. Cancer , vol.113 , Issue.3 , pp. 365-371
    • Thomas, S.1    Snowden, J.2    Zeidler, M.3    Danson, S.4
  • 8
    • 70949094349 scopus 로고    scopus 로고
    • The JAK2 inhibitor AZD1480 potently blocks Stat3 signaling and oncogenesis in solid tumors
    • Hedvat, M., Huszar, D., Herrmann, A., Gozgit, J.M., Schroeder, A., Sheehy, A., et al. The JAK2 inhibitor AZD1480 potently blocks Stat3 signaling and oncogenesis in solid tumors. Cancer Cell 16:6 (2009), 487–497.
    • (2009) Cancer Cell , vol.16 , Issue.6 , pp. 487-497
    • Hedvat, M.1    Huszar, D.2    Herrmann, A.3    Gozgit, J.M.4    Schroeder, A.5    Sheehy, A.6
  • 9
    • 84962750039 scopus 로고    scopus 로고
    • JAK2 inhibition sensitizes resistant EGFR-mutant lung adenocarcinoma to tyrosine kinase inhibitors
    • Gao, S.P., Chang, Q., Mao, N., Daly, L.A., Vogel, R., Chan, T., et al. JAK2 inhibition sensitizes resistant EGFR-mutant lung adenocarcinoma to tyrosine kinase inhibitors. Sci. Signal, 9(421), 2016, ra33.
    • (2016) Sci. Signal , vol.9 , Issue.421 , pp. ra33
    • Gao, S.P.1    Chang, Q.2    Mao, N.3    Daly, L.A.4    Vogel, R.5    Chan, T.6
  • 10
    • 85012885394 scopus 로고    scopus 로고
    • JAK-STAT signaling in the therapeutic landscape of myeloproliferative neoplasms
    • O'Sullivan, J.M., Harrison, C.N., JAK-STAT signaling in the therapeutic landscape of myeloproliferative neoplasms. Mol. Cell Endocrinol. 451 (2017), 71–79.
    • (2017) Mol. Cell Endocrinol. , vol.451 , pp. 71-79
    • O'Sullivan, J.M.1    Harrison, C.N.2
  • 11
    • 84960894417 scopus 로고    scopus 로고
    • Janus kinase inhibitors for rheumatoid arthritis
    • Yamaoka, K., Janus kinase inhibitors for rheumatoid arthritis. Curr. Opin. Chem. Biol. 32 (2016), 29–33.
    • (2016) Curr. Opin. Chem. Biol. , vol.32 , pp. 29-33
    • Yamaoka, K.1
  • 12
    • 85014062632 scopus 로고    scopus 로고
    • JAK–STAT signaling as a target for inflammatory and autoimmune diseases: Current and future prospects
    • Banerjee, S., Biehl, A., Gadina, M., Hasni, S., Schwartz, D.M., JAK–STAT signaling as a target for inflammatory and autoimmune diseases: Current and future prospects. Drugs 77:5 (2017), 521–546.
    • (2017) Drugs , vol.77 , Issue.5 , pp. 521-546
    • Banerjee, S.1    Biehl, A.2    Gadina, M.3    Hasni, S.4    Schwartz, D.M.5
  • 13
    • 84951828799 scopus 로고    scopus 로고
    • Randomized, double-blind, phase II study of ruxolitinib or placebo in combination with capecitabine in patients with metastatic pancreatic cancer for whom therapy with gemcitabine has failed
    • Hurwitz, H.I., Uppal, N., Wagner, S.A., Bendell, J.C., Beck, J.T., Wade, S.M. III, et al. Randomized, double-blind, phase II study of ruxolitinib or placebo in combination with capecitabine in patients with metastatic pancreatic cancer for whom therapy with gemcitabine has failed. J. Clin. Oncol. 33:34 (2015), 4039–4047.
    • (2015) J. Clin. Oncol. , vol.33 , Issue.34 , pp. 4039-4047
    • Hurwitz, H.I.1    Uppal, N.2    Wagner, S.A.3    Bendell, J.C.4    Beck, J.T.5    Wade, S.M.6
  • 14
    • 0035694582 scopus 로고    scopus 로고
    • The N-terminal domain of janus kinase 2 is required for golgi processing and cell surface expression of erythropoietin receptor
    • Huang, L.J., Constantinescu, S.N., Lodish, H.F., The N-terminal domain of janus kinase 2 is required for golgi processing and cell surface expression of erythropoietin receptor. Mol. Cell. 8:6 (2001), 1327–1338.
    • (2001) Mol. Cell. , vol.8 , Issue.6 , pp. 1327-1338
    • Huang, L.J.1    Constantinescu, S.N.2    Lodish, H.F.3
  • 15
    • 0141866643 scopus 로고    scopus 로고
    • Long term association of the cytokine receptor gp130 and the janus kinase Jak1 revealed by FRAP analysis
    • Giese, B., Au-Yeung, C., Herrmann, A., Diefenbach, S., Haan, C., Küster, A., et al. Long term association of the cytokine receptor gp130 and the janus kinase Jak1 revealed by FRAP analysis. J. Biol. Chem. 278:40 (2003), 39205–39213.
    • (2003) J. Biol. Chem. , vol.278 , Issue.40 , pp. 39205-39213
    • Giese, B.1    Au-Yeung, C.2    Herrmann, A.3    Diefenbach, S.4    Haan, C.5    Küster, A.6
  • 16
    • 33750522675 scopus 로고    scopus 로고
    • Jaks and cytokine receptors—an intimate relationship
    • Haan, C., Kreis, S., Margue, C., Behrmann, I., Jaks and cytokine receptors—an intimate relationship. Biochem. Pharmacol. 72:11 (2006), 1538–1546.
    • (2006) Biochem. Pharmacol. , vol.72 , Issue.11 , pp. 1538-1546
    • Haan, C.1    Kreis, S.2    Margue, C.3    Behrmann, I.4
  • 18
    • 21844460518 scopus 로고    scopus 로고
    • The Jak1 SH2 domain does not fulfill a classical SH2 function in jak/STAT signaling but plays a structural role for receptor interaction and up-regulation of receptor surface expression
    • Radtke, S., Haan, S., Jörissen, A., Hermanns, H.M., Diefenbach, S., Smyczek, T., et al. The Jak1 SH2 domain does not fulfill a classical SH2 function in jak/STAT signaling but plays a structural role for receptor interaction and up-regulation of receptor surface expression. J. Biol. Chem. 280:27 (2005), 25760–25768.
    • (2005) J. Biol. Chem. , vol.280 , Issue.27 , pp. 25760-25768
    • Radtke, S.1    Haan, S.2    Jörissen, A.3    Hermanns, H.M.4    Diefenbach, S.5    Smyczek, T.6
  • 19
    • 70350351539 scopus 로고    scopus 로고
    • A JAK2 interdomain linker relays epo receptor engagement signals to kinase activation
    • Zhao, L., Dong, H., Zhang, C.C., Kinch, L., Osawa, M., Iacovino, M., et al. A JAK2 interdomain linker relays epo receptor engagement signals to kinase activation. J. Biol. Chem., 284(39), 2009, 26988.
    • (2009) J. Biol. Chem. , vol.284 , Issue.39 , pp. 26988
    • Zhao, L.1    Dong, H.2    Zhang, C.C.3    Kinch, L.4    Osawa, M.5    Iacovino, M.6
  • 20
    • 18244393495 scopus 로고    scopus 로고
    • Unexpected effects of FERM domain mutations on catalytic activity of Jak3: Structural implication for janus kinases
    • Zhou, Y.J., Chen, M., Cusack, N.A., Kimmel, L.H., Magnuson, K.S., Boyd, J.G., et al. Unexpected effects of FERM domain mutations on catalytic activity of Jak3: Structural implication for janus kinases. Mol. Cell. 8:5 (2001), 959–969.
    • (2001) Mol. Cell. , vol.8 , Issue.5 , pp. 959-969
    • Zhou, Y.J.1    Chen, M.2    Cusack, N.A.3    Kimmel, L.H.4    Magnuson, K.S.5    Boyd, J.G.6
  • 21
    • 76549088588 scopus 로고    scopus 로고
    • A regulating role of the JAK2 FERM domain in hyperactivation of JAK2 (V617F)
    • Zhao, L., Ma, Y., Seemann, J., Huang, L., A regulating role of the JAK2 FERM domain in hyperactivation of JAK2 (V617F). Biochem. J. 426 (2010), 91–98.
    • (2010) Biochem. J. , vol.426 , pp. 91-98
    • Zhao, L.1    Ma, Y.2    Seemann, J.3    Huang, L.4
  • 23
    • 84964679935 scopus 로고    scopus 로고
    • The structural basis for class II cytokine receptor recognition by JAK1
    • Ferrao, R., Wallweber, H.J., Ho, H., Tam, C., Franke, Y., Quinn, J., et al. The structural basis for class II cytokine receptor recognition by JAK1. Structure 24:6 (2016), 897–905.
    • (2016) Structure , vol.24 , Issue.6 , pp. 897-905
    • Ferrao, R.1    Wallweber, H.J.2    Ho, H.3    Tam, C.4    Franke, Y.5    Quinn, J.6
  • 24
    • 84971463428 scopus 로고    scopus 로고
    • Crystal structure of the FERM-SH2 module of human Jak2
    • McNally, R., Toms, A.V., Eck, M.J., Crystal structure of the FERM-SH2 module of human Jak2. PLoS One, 11(5), 2016, e0156218.
    • (2016) PLoS One , vol.11 , Issue.5 , pp. e0156218
    • McNally, R.1    Toms, A.V.2    Eck, M.J.3
  • 25
    • 84995549478 scopus 로고    scopus 로고
    • Crystal structure of a complex of the intracellular domain of interferon λ receptor 1 (IFNLR1) and the FERM/SH2 domains of human JAK1
    • Zhang, D., Wlodawer, A., Lubkowski, J., Crystal structure of a complex of the intracellular domain of interferon λ receptor 1 (IFNLR1) and the FERM/SH2 domains of human JAK1. J. Mol. Biol. 428:23 (2016), 4651–4668.
    • (2016) J. Mol. Biol. , vol.428 , Issue.23 , pp. 4651-4668
    • Zhang, D.1    Wlodawer, A.2    Lubkowski, J.3
  • 28
    • 84956893891 scopus 로고    scopus 로고
    • Nucleotide-binding mechanisms in pseudokinases
    • Hammarén, H.M., Virtanen, A.T., Silvennoinen, O., Nucleotide-binding mechanisms in pseudokinases. Biosci. Rep., 36(1), 2015, e00282.
    • (2015) Biosci. Rep. , vol.36 , Issue.1 , pp. e00282
    • Hammarén, H.M.1    Virtanen, A.T.2    Silvennoinen, O.3
  • 29
    • 0036107253 scopus 로고    scopus 로고
    • Evolutionary analysis for functional divergence of jak protein kinase domains and tissue-specific genes
    • Gu, J., Wang, Y., Gu, X., Evolutionary analysis for functional divergence of jak protein kinase domains and tissue-specific genes. J. Mol. Evol. 54:6 (2002), 725–733.
    • (2002) J. Mol. Evol. , vol.54 , Issue.6 , pp. 725-733
    • Gu, J.1    Wang, Y.2    Gu, X.3
  • 30
    • 84859972127 scopus 로고    scopus 로고
    • JAK and STAT signaling molecules in immunoregulation and immune-mediated disease
    • O'Shea, J.J., Plenge, R., JAK and STAT signaling molecules in immunoregulation and immune-mediated disease. Immunity 36:4 (2012), 542–550.
    • (2012) Immunity , vol.36 , Issue.4 , pp. 542-550
    • O'Shea, J.J.1    Plenge, R.2
  • 32
    • 0030953469 scopus 로고    scopus 로고
    • Activation of Jak2 catalytic activity requires phosphorylation of Y1007 in the kinase activation loop
    • Feng, J., Witthuhn, B.A., Matsuda, T., Kohlhuber, F., Kerr, I.M., Ihle, J.N., Activation of Jak2 catalytic activity requires phosphorylation of Y1007 in the kinase activation loop. Mol. Cell. Biol. 17:5 (1997), 2497–2501.
    • (1997) Mol. Cell. Biol. , vol.17 , Issue.5 , pp. 2497-2501
    • Feng, J.1    Witthuhn, B.A.2    Matsuda, T.3    Kohlhuber, F.4    Kerr, I.M.5    Ihle, J.N.6
  • 33
    • 1842479256 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of the janus kinase 2 activation loop is essential for a high-activity catalytic state but dispensable for a basal catalytic state
    • Chatti, K., Farrar, W.L., Duhé, R.J., Tyrosine phosphorylation of the janus kinase 2 activation loop is essential for a high-activity catalytic state but dispensable for a basal catalytic state. Biochemistry (N Y) 43:14 (2004), 4272–4283.
    • (2004) Biochemistry (N Y) , vol.43 , Issue.14 , pp. 4272-4283
    • Chatti, K.1    Farrar, W.L.2    Duhé, R.J.3
  • 35
    • 0030840464 scopus 로고    scopus 로고
    • STATs and gene regulation
    • Darnell, J.E. Jr., STATs and gene regulation. Science 277:5332 (1997), 1630–1635.
    • (1997) Science , vol.277 , Issue.5332 , pp. 1630-1635
    • Darnell, J.E.1
  • 36
    • 0032499801 scopus 로고    scopus 로고
    • Three-dimensional structure of the Stat3β homodimer bound to DNA
    • Becker, S., Groner, B., Müller, C.W., Three-dimensional structure of the Stat3β homodimer bound to DNA. Nature 394:6689 (1998), 145–151.
    • (1998) Nature , vol.394 , Issue.6689 , pp. 145-151
    • Becker, S.1    Groner, B.2    Müller, C.W.3
  • 37
    • 0032577678 scopus 로고    scopus 로고
    • Crystal structure of a tyrosine phosphorylated STAT-1 dimer bound to DNA
    • Chen, X., Vinkemeier, U., Zhao, Y., Jeruzalmi, D., Darnell, J.E., Kuriyan, J., Crystal structure of a tyrosine phosphorylated STAT-1 dimer bound to DNA. Cell 93:5 (1998), 827–839.
    • (1998) Cell , vol.93 , Issue.5 , pp. 827-839
    • Chen, X.1    Vinkemeier, U.2    Zhao, Y.3    Jeruzalmi, D.4    Darnell, J.E.5    Kuriyan, J.6
  • 38
    • 85016307327 scopus 로고    scopus 로고
    • Mechanisms and consequences of jak-STAT signaling in the immune system
    • Villarino, A.V., Kanno, Y., O'Shea, J.J., Mechanisms and consequences of jak-STAT signaling in the immune system. Nat. Immunol. 18:4 (2017), 374–384.
    • (2017) Nat. Immunol. , vol.18 , Issue.4 , pp. 374-384
    • Villarino, A.V.1    Kanno, Y.2    O'Shea, J.J.3
  • 39
    • 84975318343 scopus 로고    scopus 로고
    • Evolution of cytokine receptor signaling
    • Liongue, C., Sertori, R., Ward, A.C., Evolution of cytokine receptor signaling. J. Immunol. 197:1 (2016), 11–18.
    • (2016) J. Immunol. , vol.197 , Issue.1 , pp. 11-18
    • Liongue, C.1    Sertori, R.2    Ward, A.C.3
  • 40
    • 79955136973 scopus 로고    scopus 로고
    • Analysis of Jak2 catalytic function by peptide microarrays: the role of the JH2 domain and V617F mutation
    • Sanz, A., Ungureanu, D., Pekkala, T., Ruijtenbeek, R., Touw, I.P., Hilhorst, R., et al. Analysis of Jak2 catalytic function by peptide microarrays: the role of the JH2 domain and V617F mutation. PLoS One, 6(4), 2011, e18522.
    • (2011) PLoS One , vol.6 , Issue.4 , pp. e18522
    • Sanz, A.1    Ungureanu, D.2    Pekkala, T.3    Ruijtenbeek, R.4    Touw, I.P.5    Hilhorst, R.6
  • 41
    • 84901840527 scopus 로고    scopus 로고
    • Structure of the pseudokinase–kinase domains from protein kinase TYK2 reveals a mechanism for janus kinase (JAK) autoinhibition
    • Lupardus, P.J., Ultsch, M., Wallweber, H., Bir Kohli, P., Johnson, A.R., Eigenbrot, C., Structure of the pseudokinase–kinase domains from protein kinase TYK2 reveals a mechanism for janus kinase (JAK) autoinhibition. Proc. Natl. Acad. Sci. U. S. A. 111:22 (2014), 8025–8030.
    • (2014) Proc. Natl. Acad. Sci. U. S. A. , vol.111 , Issue.22 , pp. 8025-8030
    • Lupardus, P.J.1    Ultsch, M.2    Wallweber, H.3    Bir Kohli, P.4    Johnson, A.R.5    Eigenbrot, C.6
  • 42
    • 84861859600 scopus 로고    scopus 로고
    • The structural basis for control of eukaryotic protein kinases
    • Endicott, J.A., Noble, M.E., Johnson, L.N., The structural basis for control of eukaryotic protein kinases. Annu. Rev. Biochem. 81 (2012), 587–613.
    • (2012) Annu. Rev. Biochem. , vol.81 , pp. 587-613
    • Endicott, J.A.1    Noble, M.E.2    Johnson, L.N.3
  • 43
    • 84878764309 scopus 로고    scopus 로고
    • Production and crystallization of recombinant JAK proteins
    • Springer
    • Lucet, I.S., Bamert, R., Production and crystallization of recombinant JAK proteins. JAK-STAT Signalling, 2013, Springer, 275–300.
    • (2013) JAK-STAT Signalling , pp. 275-300
    • Lucet, I.S.1    Bamert, R.2
  • 45
    • 0028835347 scopus 로고
    • Distinct domains of the protein tyrosine kinase tyk2 required for binding of interferon-/and for signal transduction
    • Velazquez, L., Mogensen, K.E., Barbieri, G., Fellous, M., Uzé, G., Pellegrini, S., Distinct domains of the protein tyrosine kinase tyk2 required for binding of interferon-/and for signal transduction. J. Biol. Chem. 270:7 (1995), 3327–3334.
    • (1995) J. Biol. Chem. , vol.270 , Issue.7 , pp. 3327-3334
    • Velazquez, L.1    Mogensen, K.E.2    Barbieri, G.3    Fellous, M.4    Uzé, G.5    Pellegrini, S.6
  • 46
    • 0031017533 scopus 로고    scopus 로고
    • Mutation in the jak kinase JH2 domain hyperactivates drosophila and mammalian jak-stat pathways
    • Luo, H., Rose, P., Barber, D., Hanratty, W.P., Lee, S., Roberts, T.M., et al. Mutation in the jak kinase JH2 domain hyperactivates drosophila and mammalian jak-stat pathways. Mol. Cell. Biol. 17:3 (1997), 1562–1571.
    • (1997) Mol. Cell. Biol. , vol.17 , Issue.3 , pp. 1562-1571
    • Luo, H.1    Rose, P.2    Barber, D.3    Hanratty, W.P.4    Lee, S.5    Roberts, T.M.6
  • 47
    • 0034012330 scopus 로고    scopus 로고
    • Regulation of the Jak2 tyrosine kinase by its pseudokinase domain
    • Saharinen, P., Takaluoma, K., Silvennoinen, O., Regulation of the Jak2 tyrosine kinase by its pseudokinase domain. Mol. Cell. Biol. 20:10 (2000), 3387–3395.
    • (2000) Mol. Cell. Biol. , vol.20 , Issue.10 , pp. 3387-3395
    • Saharinen, P.1    Takaluoma, K.2    Silvennoinen, O.3
  • 48
    • 0037033012 scopus 로고    scopus 로고
    • The pseudokinase domain is required for suppression of basal activity of Jak2 and Jak3 tyrosine kinases and for cytokine-inducible activation of signal transduction
    • Saharinen, P., Silvennoinen, O., The pseudokinase domain is required for suppression of basal activity of Jak2 and Jak3 tyrosine kinases and for cytokine-inducible activation of signal transduction. J. Biol. Chem. 277:49 (2002), 47954–47963.
    • (2002) J. Biol. Chem. , vol.277 , Issue.49 , pp. 47954-47963
    • Saharinen, P.1    Silvennoinen, O.2
  • 49
    • 0033965488 scopus 로고    scopus 로고
    • Complex effects of naturally occurring mutations in the JAK3 pseudokinase domain: Evidence for interactions between the kinase and pseudokinase domains
    • Chen, M., Cheng, A., Candotti, F., Zhou, Y.J., Hymel, A., Fasth, A., et al. Complex effects of naturally occurring mutations in the JAK3 pseudokinase domain: Evidence for interactions between the kinase and pseudokinase domains. Mol. Cell. Biol. 20:3 (2000), 947–956.
    • (2000) Mol. Cell. Biol. , vol.20 , Issue.3 , pp. 947-956
    • Chen, M.1    Cheng, A.2    Candotti, F.3    Zhou, Y.J.4    Hymel, A.5    Fasth, A.6
  • 50
    • 0034255258 scopus 로고    scopus 로고
    • A dual role for the kinase-like domain of the tyrosine kinase Tyk2 in interferon-α signaling
    • Yeh, T.C., Dondi, E., Uzé, G., Pellegrini, S., A dual role for the kinase-like domain of the tyrosine kinase Tyk2 in interferon-α signaling. Proc. Natl. Acad. Sci. U. S. A. 97:16 (2000), 8991–8996.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , Issue.16 , pp. 8991-8996
    • Yeh, T.C.1    Dondi, E.2    Uzé, G.3    Pellegrini, S.4
  • 51
    • 77952299611 scopus 로고    scopus 로고
    • The src, syk, and tec family kinases: Distinct types of molecular switches
    • Bradshaw, J.M., The src, syk, and tec family kinases: Distinct types of molecular switches. Cell. Signal 22:8 (2010), 1175–1184.
    • (2010) Cell. Signal , vol.22 , Issue.8 , pp. 1175-1184
    • Bradshaw, J.M.1
  • 53
    • 2442642830 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of Jak2 in the JH2 domain inhibits cytokine signaling
    • Feener, E.P., Rosario, F., Dunn, S.L., Stancheva, Z., Myers, M.G. Jr, Tyrosine phosphorylation of Jak2 in the JH2 domain inhibits cytokine signaling. Mol. Cell. Biol. 24:11 (2004), 4968–4978.
    • (2004) Mol. Cell. Biol. , vol.24 , Issue.11 , pp. 4968-4978
    • Feener, E.P.1    Rosario, F.2    Dunn, S.L.3    Stancheva, Z.4    Myers, M.G.5
  • 54
    • 33646865516 scopus 로고    scopus 로고
    • Phosphorylation of Jak2 on Ser523 inhibits Jak2-dependent leptin receptor signaling
    • Ishida-Takahashi, R., Rosario, F., Gong, Y., Kopp, K., Stancheva, Z., Chen, X., et al. Phosphorylation of Jak2 on Ser523 inhibits Jak2-dependent leptin receptor signaling. Mol. Cell. Biol. 26:11 (2006), 4063–4073.
    • (2006) Mol. Cell. Biol. , vol.26 , Issue.11 , pp. 4063-4073
    • Ishida-Takahashi, R.1    Rosario, F.2    Gong, Y.3    Kopp, K.4    Stancheva, Z.5    Chen, X.6
  • 55
    • 33646864349 scopus 로고    scopus 로고
    • Phosphorylation of JAK2 at serine 523: A negative regulator of JAK2 that is stimulated by growth hormone and epidermal growth factor
    • Mazurkiewicz-Munoz, A.M., Argetsinger, L.S., Kouadio, J.K., Stensballe, A., Jensen, O.N., Cline, J.M., et al. Phosphorylation of JAK2 at serine 523: A negative regulator of JAK2 that is stimulated by growth hormone and epidermal growth factor. Mol. Cell. Biol. 26:11 (2006), 4052–4062.
    • (2006) Mol. Cell. Biol. , vol.26 , Issue.11 , pp. 4052-4062
    • Mazurkiewicz-Munoz, A.M.1    Argetsinger, L.S.2    Kouadio, J.K.3    Stensballe, A.4    Jensen, O.N.5    Cline, J.M.6
  • 56
    • 84928102345 scopus 로고    scopus 로고
    • The JH2 domain and SH2-JH2 linker regulate JAK2 activity: A detailed kinetic analysis of wild type and V617F mutant kinase domains
    • Sanz, A.S., Niranjan, Y., Hammarén, H., Ungureanu, D., Ruijtenbeek, R., Touw, I.P., et al. The JH2 domain and SH2-JH2 linker regulate JAK2 activity: A detailed kinetic analysis of wild type and V617F mutant kinase domains. BBA Proteins Proteomics 1844:10 (2014), 1835–1841.
    • (2014) BBA Proteins Proteomics , vol.1844 , Issue.10 , pp. 1835-1841
    • Sanz, A.S.1    Niranjan, Y.2    Hammarén, H.3    Ungureanu, D.4    Ruijtenbeek, R.5    Touw, I.P.6
  • 57
    • 78649458601 scopus 로고    scopus 로고
    • Oncogenic JAK2V617F requires an intact SH2-like domain for constitutive activation and induction of a myeloproliferative disease in mice
    • Gorantla, S.P., Dechow, T.N., Grundler, R., Illert zum, A.L., Büschenfelde, C.M., Kremer, M., et al. Oncogenic JAK2V617F requires an intact SH2-like domain for constitutive activation and induction of a myeloproliferative disease in mice. Blood 116:22 (2010), 4600–4611.
    • (2010) Blood , vol.116 , Issue.22 , pp. 4600-4611
    • Gorantla, S.P.1    Dechow, T.N.2    Grundler, R.3    Illert zum, A.L.4    Büschenfelde, C.M.5    Kremer, M.6
  • 58
    • 84930965814 scopus 로고    scopus 로고
    • Molecular insights into regulation of JAK2 in myeloproliferative neoplasms
    • Silvennoinen, O., Hubbard, S.R., Molecular insights into regulation of JAK2 in myeloproliferative neoplasms. Blood 125:22 (2015), 3388–3392.
    • (2015) Blood , vol.125 , Issue.22 , pp. 3388-3392
    • Silvennoinen, O.1    Hubbard, S.R.2
  • 59
    • 41949118675 scopus 로고    scopus 로고
    • Dimerization by a cytokine receptor is necessary for constitutive activation of JAK2V617F
    • Lu, X., Huang, L.J.S., Lodish, H.F., Dimerization by a cytokine receptor is necessary for constitutive activation of JAK2V617F. J. Biol. Chem. 283:9 (2008), 5258–5266.
    • (2008) J. Biol. Chem. , vol.283 , Issue.9 , pp. 5258-5266
    • Lu, X.1    Huang, L.J.S.2    Lodish, H.F.3
  • 60
    • 43549109620 scopus 로고    scopus 로고
    • The Jak2V617F oncogene associated with myeloproliferative diseases requires a functional FERM domain for transformation and for expression of the myc and pim proto-oncogenes
    • Wernig, G., Gonneville, J.R., Crowley, B.J., Rodrigues, M.S., Reddy, M.M., Hudon, H.E., et al. The Jak2V617F oncogene associated with myeloproliferative diseases requires a functional FERM domain for transformation and for expression of the myc and pim proto-oncogenes. Blood 111:7 (2008), 3751–3759.
    • (2008) Blood , vol.111 , Issue.7 , pp. 3751-3759
    • Wernig, G.1    Gonneville, J.R.2    Crowley, B.J.3    Rodrigues, M.S.4    Reddy, M.M.5    Hudon, H.E.6
  • 61
    • 85011004567 scopus 로고    scopus 로고
    • Activating JAK2 mutants reveal cytokine receptor coupling differences that impact outcomes in myeloproliferative neoplasm
    • Yao, H., Ma, Y., Hong, Z., Zhao, L., Monaghan, S.A., Hu, M.C., et al. Activating JAK2 mutants reveal cytokine receptor coupling differences that impact outcomes in myeloproliferative neoplasm. Leukemia 31:10 (2017), 2122–2131.
    • (2017) Leukemia , vol.31 , Issue.10 , pp. 2122-2131
    • Yao, H.1    Ma, Y.2    Hong, Z.3    Zhao, L.4    Monaghan, S.A.5    Hu, M.C.6
  • 62
    • 77955299093 scopus 로고    scopus 로고
    • JAK2 V617F constitutive activation requires JH2 residue F595: a pseudokinase domain target for specific inhibitors
    • Dusa, A., Mouton, C., Pecquet, C., Herman, M., Constantinescu, S.N., JAK2 V617F constitutive activation requires JH2 residue F595: a pseudokinase domain target for specific inhibitors. PLoS One 5:6 (2010), 207–212.
    • (2010) PLoS One , vol.5 , Issue.6 , pp. 207-212
    • Dusa, A.1    Mouton, C.2    Pecquet, C.3    Herman, M.4    Constantinescu, S.N.5
  • 63
    • 84885418884 scopus 로고    scopus 로고
    • Structure of a pseudokinase-domain switch that controls oncogenic activation of jak kinases
    • Toms, A.V., Deshpande, A., McNally, R., Jeong, Y., Rogers, J.M., Kim, C.U., et al. Structure of a pseudokinase-domain switch that controls oncogenic activation of jak kinases. Nat. Struct. Mol. Biol. 20:10 (2013), 1221–1223.
    • (2013) Nat. Struct. Mol. Biol. , vol.20 , Issue.10 , pp. 1221-1223
    • Toms, A.V.1    Deshpande, A.2    McNally, R.3    Jeong, Y.4    Rogers, J.M.5    Kim, C.U.6
  • 65
    • 78649289718 scopus 로고    scopus 로고
    • The constitutive activation of Jak2-V617F is mediated by a π stacking mechanism involving phenylalanines 595 and 617
    • Gnanasambandan, K., Magis, A., Sayeski, P.P., The constitutive activation of Jak2-V617F is mediated by a π stacking mechanism involving phenylalanines 595 and 617. Biochemistry 49:46 (2010), 9972–9984.
    • (2010) Biochemistry , vol.49 , Issue.46 , pp. 9972-9984
    • Gnanasambandan, K.1    Magis, A.2    Sayeski, P.P.3
  • 66
    • 84975109095 scopus 로고    scopus 로고
    • Uncoupling JAK2 V617F activation from cytokine-induced signalling by modulation of JH2 alphaC helix
    • Leroy, E., Dusa, A., Colau, D., Motamedi, A., Cahu, X., Mouton, C., et al. Uncoupling JAK2 V617F activation from cytokine-induced signalling by modulation of JH2 alphaC helix. Biochem. J. 473:11 (2016), 1579–1591.
    • (2016) Biochem. J. , vol.473 , Issue.11 , pp. 1579-1591
    • Leroy, E.1    Dusa, A.2    Colau, D.3    Motamedi, A.4    Cahu, X.5    Mouton, C.6
  • 68
    • 80052492285 scopus 로고    scopus 로고
    • The pseudokinase domain of JAK2 is a dual-specificity protein kinase that negatively regulates cytokine signaling
    • Ungureanu, D., Wu, J., Pekkala, T., Niranjan, Y., Young, C., Jensen, O.N., et al. The pseudokinase domain of JAK2 is a dual-specificity protein kinase that negatively regulates cytokine signaling. Nat. Struct. Mol. Biol. 18:9 (2011), 971–976.
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , Issue.9 , pp. 971-976
    • Ungureanu, D.1    Wu, J.2    Pekkala, T.3    Niranjan, Y.4    Young, C.5    Jensen, O.N.6
  • 69
    • 67649183002 scopus 로고    scopus 로고
    • Regulation of Jak2 function by phosphorylation of Tyr317 and Tyr637 during cytokine signaling
    • Robertson, S.A., Koleva, R.I., Argetsinger, L.S., Carter-Su, C., Marto, J.A., Feener, E.P., et al. Regulation of Jak2 function by phosphorylation of Tyr317 and Tyr637 during cytokine signaling. Mol. Cell. Biol. 29:12 (2009), 3367–3378.
    • (2009) Mol. Cell. Biol. , vol.29 , Issue.12 , pp. 3367-3378
    • Robertson, S.A.1    Koleva, R.I.2    Argetsinger, L.S.3    Carter-Su, C.4    Marto, J.A.5    Feener, E.P.6
  • 70
    • 33750221616 scopus 로고    scopus 로고
    • Receptor specific downregulation of cytokine signaling by autophosphorylation in the FERM domain of Jak2
    • Funakoshi-Tago, M., Pelletier, S., Matsuda, T., Parganas, E., Ihle, J.N., Receptor specific downregulation of cytokine signaling by autophosphorylation in the FERM domain of Jak2. EMBO J. 25:20 (2006), 4763–4772.
    • (2006) EMBO J. , vol.25 , Issue.20 , pp. 4763-4772
    • Funakoshi-Tago, M.1    Pelletier, S.2    Matsuda, T.3    Parganas, E.4    Ihle, J.N.5
  • 71
    • 42649118836 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases in the JAK/STAT pathway
    • Xu, D., Qu, C.K., Protein tyrosine phosphatases in the JAK/STAT pathway. Front Biosci. 13 (2008), 4925–4932.
    • (2008) Front Biosci. , vol.13 , pp. 4925-4932
    • Xu, D.1    Qu, C.K.2
  • 72
    • 85035008860 scopus 로고    scopus 로고
    • Therapeutic targeting of oncogenic tyrosine phosphatases
    • Frankson, R., Yu, Z.H., Bai, Y., Li, Q., Zhang, R.Y., Zhang, Z.Y., Therapeutic targeting of oncogenic tyrosine phosphatases. Cancer Res. 77:21 (2017), 5701–5705.
    • (2017) Cancer Res. , vol.77 , Issue.21 , pp. 5701-5705
    • Frankson, R.1    Yu, Z.H.2    Bai, Y.3    Li, Q.4    Zhang, R.Y.5    Zhang, Z.Y.6
  • 74
    • 84857414096 scopus 로고    scopus 로고
    • Suppression of cytokine signaling by SOCS3: Characterization of the mode of inhibition and the basis of its specificity
    • Babon, J.J., Kershaw, N.J., Murphy, J.M., Varghese, L.N., Laktyushin, A., Young, S.N., et al. Suppression of cytokine signaling by SOCS3: Characterization of the mode of inhibition and the basis of its specificity. Immunity 36:2 (2012), 239–250.
    • (2012) Immunity , vol.36 , Issue.2 , pp. 239-250
    • Babon, J.J.1    Kershaw, N.J.2    Murphy, J.M.3    Varghese, L.N.4    Laktyushin, A.5    Young, S.N.6
  • 75
    • 84876183232 scopus 로고    scopus 로고
    • SOCS3 binds specific receptor–JAK complexes to control cytokine signaling by direct kinase inhibition
    • Kershaw, N.J., Murphy, J.M., Liau, N.P., Varghese, L.N., Laktyushin, A., Whitlock, E.L., et al. SOCS3 binds specific receptor–JAK complexes to control cytokine signaling by direct kinase inhibition. Nat. Struct. Mol. Biol. 20:4 (2013), 469–476.
    • (2013) Nat. Struct. Mol. Biol. , vol.20 , Issue.4 , pp. 469-476
    • Kershaw, N.J.1    Murphy, J.M.2    Liau, N.P.3    Varghese, L.N.4    Laktyushin, A.5    Whitlock, E.L.6
  • 76
    • 33747748126 scopus 로고    scopus 로고
    • Binding of SH2-B family members within a potential negative regulatory region maintains JAK2 in an active state
    • Kurzer, J.H., Saharinen, P., Silvennoinen, O., Carter-Su, C., Binding of SH2-B family members within a potential negative regulatory region maintains JAK2 in an active state. Mol. Cell. Biol. 26:17 (2006), 6381–6394.
    • (2006) Mol. Cell. Biol. , vol.26 , Issue.17 , pp. 6381-6394
    • Kurzer, J.H.1    Saharinen, P.2    Silvennoinen, O.3    Carter-Su, C.4
  • 77
    • 34548370733 scopus 로고    scopus 로고
    • SH2B1 enhances leptin signaling by both janus kinase 2 Tyr813 phosphorylation-dependent and-independent mechanisms
    • Li, Z., Zhou, Y., Carter-Su, C., Myers, M.G. Jr, Rui, L., SH2B1 enhances leptin signaling by both janus kinase 2 Tyr813 phosphorylation-dependent and-independent mechanisms. Mol. Endocrinol. 21:9 (2007), 2270–2281.
    • (2007) Mol. Endocrinol. , vol.21 , Issue.9 , pp. 2270-2281
    • Li, Z.1    Zhou, Y.2    Carter-Su, C.3    Myers, M.G.4    Rui, L.5
  • 78
    • 77954894901 scopus 로고    scopus 로고
    • Critical role of the src homology 2 (SH2) domain of neuronal SH2B1 in the regulation of body weight and glucose homeostasis in mice
    • Morris, D.L., Cho, K.W., Rui, L., Critical role of the src homology 2 (SH2) domain of neuronal SH2B1 in the regulation of body weight and glucose homeostasis in mice. Endocrinology 151:8 (2010), 3643–3651.
    • (2010) Endocrinology , vol.151 , Issue.8 , pp. 3643-3651
    • Morris, D.L.1    Cho, K.W.2    Rui, L.3
  • 79
    • 85026654141 scopus 로고    scopus 로고
    • The role of LNK/SH2B3 genetic alterations in myeloproliferative neoplasms and other hematological disorders
    • Maslah, N., Cassinat, B., Verger, E., Kiladjian, J., Velazquez, L., The role of LNK/SH2B3 genetic alterations in myeloproliferative neoplasms and other hematological disorders. Leukemia, 2017.
    • (2017) Leukemia
    • Maslah, N.1    Cassinat, B.2    Verger, E.3    Kiladjian, J.4    Velazquez, L.5
  • 81
    • 25144523930 scopus 로고    scopus 로고
    • Identification of SH2-B as a key regulator of leptin sensitivity, energy balance, and body weight in mice
    • Ren, D., Li, M., Duan, C., Rui, L., Identification of SH2-B as a key regulator of leptin sensitivity, energy balance, and body weight in mice. Cell Metab. 2:2 (2005), 95–104.
    • (2005) Cell Metab. , vol.2 , Issue.2 , pp. 95-104
    • Ren, D.1    Li, M.2    Duan, C.3    Rui, L.4
  • 82
    • 84864386268 scopus 로고    scopus 로고
    • The SH2B1 adaptor protein associates with a proximal region of the erythropoietin receptor
    • Javadi, M., Hofstatter, E., Stickle, N., Beattie, B.K., Jaster, R., Carter-Su, C., et al. The SH2B1 adaptor protein associates with a proximal region of the erythropoietin receptor. J. Biol. Chem. 287:31 (2012), 26223–26234.
    • (2012) J. Biol. Chem. , vol.287 , Issue.31 , pp. 26223-26234
    • Javadi, M.1    Hofstatter, E.2    Stickle, N.3    Beattie, B.K.4    Jaster, R.5    Carter-Su, C.6
  • 83
    • 84878944582 scopus 로고    scopus 로고
    • Sumoylation: A regulatory protein modification in health and disease
    • Flotho, A., Melchior, F., Sumoylation: A regulatory protein modification in health and disease. Annu. Rev. Biochem. 82 (2013), 357–385.
    • (2013) Annu. Rev. Biochem. , vol.82 , pp. 357-385
    • Flotho, A.1    Melchior, F.2
  • 84
    • 0030725378 scopus 로고    scopus 로고
    • Specific inhibition of Stat3 signal transduction by PIAS3
    • Chung, C.D., Liao, J., Liu, B., Rao, X., Jay, P., Berta, P., et al. Specific inhibition of Stat3 signal transduction by PIAS3. Science 278:5344 (1997), 1803–1805.
    • (1997) Science , vol.278 , Issue.5344 , pp. 1803-1805
    • Chung, C.D.1    Liao, J.2    Liu, B.3    Rao, X.4    Jay, P.5    Berta, P.6
  • 86
    • 85017337605 scopus 로고    scopus 로고
    • The role of PIAS SUMO E3-ligases in cancer
    • Rabellino, A., Andreani, C., Scaglioni, P.P., The role of PIAS SUMO E3-ligases in cancer. Cancer Res. 77:7 (2017), 1542–1547.
    • (2017) Cancer Res. , vol.77 , Issue.7 , pp. 1542-1547
    • Rabellino, A.1    Andreani, C.2    Scaglioni, P.P.3
  • 87
    • 32644459132 scopus 로고    scopus 로고
    • Regulation of cytokine signaling pathways by PIAS proteins
    • Shuai, K., Regulation of cytokine signaling pathways by PIAS proteins. Cell Res. 16:2 (2006), 196–202.
    • (2006) Cell Res. , vol.16 , Issue.2 , pp. 196-202
    • Shuai, K.1
  • 88
    • 22444442637 scopus 로고    scopus 로고
    • Signaling conformations of the tall cytokine receptor gp130 when in complex with IL-6 and IL-6 receptor
    • Skiniotis, G., Boulanger, M.J., Garcia, K.C., Walz, T., Signaling conformations of the tall cytokine receptor gp130 when in complex with IL-6 and IL-6 receptor. Nat. Struct. Mol. Biol. 12:6 (2005), 545–551.
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , Issue.6 , pp. 545-551
    • Skiniotis, G.1    Boulanger, M.J.2    Garcia, K.C.3    Walz, T.4
  • 89
    • 34047263587 scopus 로고    scopus 로고
    • The dynamics of signal triggering in a gp130-receptor complex
    • Matadeen, R., Hon, W., Heath, J.K., Jones, E.Y., Fuller, S., The dynamics of signal triggering in a gp130-receptor complex. Structure 15:4 (2007), 441–448.
    • (2007) Structure , vol.15 , Issue.4 , pp. 441-448
    • Matadeen, R.1    Hon, W.2    Heath, J.K.3    Jones, E.Y.4    Fuller, S.5
  • 91
    • 84925518929 scopus 로고    scopus 로고
    • Insights into cytokine–receptor interactions from cytokine engineering
    • Spangler, J.B., Moraga, I., Mendoza, J.L., Garcia, K.C., Insights into cytokine–receptor interactions from cytokine engineering. Annu. Rev. Immunol. 33 (2015), 139–167.
    • (2015) Annu. Rev. Immunol. , vol.33 , pp. 139-167
    • Spangler, J.B.1    Moraga, I.2    Mendoza, J.L.3    Garcia, K.C.4
  • 92
    • 33847696075 scopus 로고    scopus 로고
    • Receptor tyrosine kinases: Mechanisms of activation and signaling
    • Hubbard, S.R., Miller, W.T., Receptor tyrosine kinases: Mechanisms of activation and signaling. Curr. Opin. Cell Biol. 19:2 (2007), 117–123.
    • (2007) Curr. Opin. Cell Biol. , vol.19 , Issue.2 , pp. 117-123
    • Hubbard, S.R.1    Miller, W.T.2
  • 93
    • 77953896432 scopus 로고    scopus 로고
    • Cell signaling by receptor-tyrosine kinases
    • Lemmon, M.A., Schlessinger, J., Cell signaling by receptor-tyrosine kinases. Cell, 141(7), 2010, 1117.
    • (2010) Cell , vol.141 , Issue.7 , pp. 1117
    • Lemmon, M.A.1    Schlessinger, J.2
  • 95
    • 84859885294 scopus 로고    scopus 로고
    • Activation of target signal transducers utilizing chimeric receptors with signaling-molecule binding motifs
    • Saka, K., Kawahara, M., Ueda, H., Nagamune, T., Activation of target signal transducers utilizing chimeric receptors with signaling-molecule binding motifs. Biotechnol. Bioeng. 109:6 (2012), 1528–1537.
    • (2012) Biotechnol. Bioeng. , vol.109 , Issue.6 , pp. 1528-1537
    • Saka, K.1    Kawahara, M.2    Ueda, H.3    Nagamune, T.4
  • 96
    • 0035836645 scopus 로고    scopus 로고
    • Ligand-independent oligomerization of cell-surface erythropoietin receptor is mediated by the transmembrane domain
    • Constantinescu, S.N., Keren, T., Socolovsky, M., Nam, H., Henis, Y.I., Lodish, H.F., Ligand-independent oligomerization of cell-surface erythropoietin receptor is mediated by the transmembrane domain. Proc. Natl. Acad. Sci. U. S. A. 98:8 (2001), 4379–4384.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , Issue.8 , pp. 4379-4384
    • Constantinescu, S.N.1    Keren, T.2    Socolovsky, M.3    Nam, H.4    Henis, Y.I.5    Lodish, H.F.6
  • 97
    • 26944493862 scopus 로고    scopus 로고
    • Model for growth hormone receptor activation based on subunit rotation within a receptor dimer
    • Brown, R.J., Adams, J.J., Pelekanos, R.A., Wan, Y., McKinstry, W.J., Palethorpe, K., et al. Model for growth hormone receptor activation based on subunit rotation within a receptor dimer. Nat. Struct. Mol. Biol. 12:9 (2005), 814–821.
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , Issue.9 , pp. 814-821
    • Brown, R.J.1    Adams, J.J.2    Pelekanos, R.A.3    Wan, Y.4    McKinstry, W.J.5    Palethorpe, K.6
  • 98
    • 78651254183 scopus 로고    scopus 로고
    • Structural snapshots of full-length Jak1, a transmembrane gp130/IL-6/IL-6Rα cytokine receptor complex, and the receptor-Jak1 holocomplex
    • Lupardus, P.J., Skiniotis, G., Rice, A.J., Thomas, C., Fischer, S., Walz, T., et al. Structural snapshots of full-length Jak1, a transmembrane gp130/IL-6/IL-6Rα cytokine receptor complex, and the receptor-Jak1 holocomplex. Structure 19:1 (2011), 45–55.
    • (2011) Structure , vol.19 , Issue.1 , pp. 45-55
    • Lupardus, P.J.1    Skiniotis, G.2    Rice, A.J.3    Thomas, C.4    Fischer, S.5    Walz, T.6
  • 99
    • 0038374250 scopus 로고    scopus 로고
    • Activation of the leptin receptor by a ligand-induced conformational change of constitutive receptor dimers
    • Couturier, C., Jockers, R., Activation of the leptin receptor by a ligand-induced conformational change of constitutive receptor dimers. J. Biol. Chem. 278:29 (2003), 26604–26611.
    • (2003) J. Biol. Chem. , vol.278 , Issue.29 , pp. 26604-26611
    • Couturier, C.1    Jockers, R.2
  • 100
    • 57749119532 scopus 로고    scopus 로고
    • Ligand-independent homomeric and heteromeric complexes between interleukin-2 or -9 receptor subunits and the gamma chain
    • Malka, Y., Hornakova, T., Royer, Y., Knoops, L., Renauld, J.C., Constantinescu, S.N., et al. Ligand-independent homomeric and heteromeric complexes between interleukin-2 or -9 receptor subunits and the gamma chain. J. Biol. Chem. 283:48 (2008), 33569–33577.
    • (2008) J. Biol. Chem. , vol.283 , Issue.48 , pp. 33569-33577
    • Malka, Y.1    Hornakova, T.2    Royer, Y.3    Knoops, L.4    Renauld, J.C.5    Constantinescu, S.N.6
  • 101
    • 0344413478 scopus 로고    scopus 로고
    • Active and inactive orientations of the transmembrane and cytosolic domains of the erythropoietin receptor dimer
    • Seubert, N., Royer, Y., Staerk, J., Kubatzky, K.F., Moucadel, V., Krishnakumar, S., et al. Active and inactive orientations of the transmembrane and cytosolic domains of the erythropoietin receptor dimer. Mol. Cell 12:5 (2003), 1239–1250.
    • (2003) Mol. Cell , vol.12 , Issue.5 , pp. 1239-1250
    • Seubert, N.1    Royer, Y.2    Staerk, J.3    Kubatzky, K.F.4    Moucadel, V.5    Krishnakumar, S.6
  • 102
    • 33646381647 scopus 로고    scopus 로고
    • Active conformation of the erythropoietin receptor: Random and cysteine-scanning mutagenesis of the extracellular juxtamembrane and transmembrane domains
    • Lu, X., Gross, A.W., Lodish, H.F., Active conformation of the erythropoietin receptor: Random and cysteine-scanning mutagenesis of the extracellular juxtamembrane and transmembrane domains. J. Biol. Chem. 281:11 (2006), 7002–7011.
    • (2006) J. Biol. Chem. , vol.281 , Issue.11 , pp. 7002-7011
    • Lu, X.1    Gross, A.W.2    Lodish, H.F.3
  • 103
    • 80455174620 scopus 로고    scopus 로고
    • Orientation-specific signalling by thrombopoietin receptor dimers
    • Staerk, J., Defour, J., Pecquet, C., Leroy, E., Antoine-Poirel, H., Brett, I., et al. Orientation-specific signalling by thrombopoietin receptor dimers. EMBO J. 30:21 (2011), 4398–4413.
    • (2011) EMBO J. , vol.30 , Issue.21 , pp. 4398-4413
    • Staerk, J.1    Defour, J.2    Pecquet, C.3    Leroy, E.4    Antoine-Poirel, H.5    Brett, I.6
  • 104
    • 84900432315 scopus 로고    scopus 로고
    • Mechanism of activation of protein kinase JAK2 by the growth hormone receptor
    • Brooks, A.J., Dai, W., O'Mara, M.L., Abankwa, D., Chhabra, Y., Pelekanos, R.A., et al. Mechanism of activation of protein kinase JAK2 by the growth hormone receptor. Science, 344(6185), 2014, 1249783.
    • (2014) Science , vol.344 , Issue.6185 , pp. 1249783
    • Brooks, A.J.1    Dai, W.2    O'Mara, M.L.3    Abankwa, D.4    Chhabra, Y.5    Pelekanos, R.A.6
  • 105
    • 84925535544 scopus 로고    scopus 로고
    • Tuning cytokine receptor signaling by re-orienting dimer geometry with surrogate ligands
    • Moraga, I., Wernig, G., Wilmes, S., Gryshkova, V., Richter, C.P., Hong, W., et al. Tuning cytokine receptor signaling by re-orienting dimer geometry with surrogate ligands. Cell 160:6 (2015), 1196–1208.
    • (2015) Cell , vol.160 , Issue.6 , pp. 1196-1208
    • Moraga, I.1    Wernig, G.2    Wilmes, S.3    Gryshkova, V.4    Richter, C.P.5    Hong, W.6
  • 106
    • 84949507084 scopus 로고    scopus 로고
    • Tyrosine kinase 2–Surveillant of tumours and bona fide oncogene
    • Leitner, N.R., Witalisz-Siepracka, A., Strobl, B., Müller, M., Tyrosine kinase 2–Surveillant of tumours and bona fide oncogene. Cytokine 89 (2017), 209–218.
    • (2017) Cytokine , vol.89 , pp. 209-218
    • Leitner, N.R.1    Witalisz-Siepracka, A.2    Strobl, B.3    Müller, M.4
  • 107
    • 0029164841 scopus 로고
    • Mutations of jak-3 gene in patients with autosomal severe combined immune deficiency (SCID)
    • Macchi, P., Villa, A., Giliani, S., Sacco, M.G., Frattini, A., Porta, F., et al. Mutations of jak-3 gene in patients with autosomal severe combined immune deficiency (SCID). Nature 377:6544 (1995), 65–68.
    • (1995) Nature , vol.377 , Issue.6544 , pp. 65-68
    • Macchi, P.1    Villa, A.2    Giliani, S.3    Sacco, M.G.4    Frattini, A.5    Porta, F.6
  • 108
    • 0028857954 scopus 로고
    • Mutation of Jak3 in a patient with SCID: Essential role of Jak3 in lymphoid development
    • Russell, S.M., Tayebi, N., Nakajima, H., Riedy, M.C., Roberts, J.L., Aman, M.J., et al. Mutation of Jak3 in a patient with SCID: Essential role of Jak3 in lymphoid development. Science 270:5237 (1995), 797–800.
    • (1995) Science , vol.270 , Issue.5237 , pp. 797-800
    • Russell, S.M.1    Tayebi, N.2    Nakajima, H.3    Riedy, M.C.4    Roberts, J.L.5    Aman, M.J.6
  • 109
    • 13344295097 scopus 로고    scopus 로고
    • Inhibition of acute lymphoblastic leukaemia by a jak-2 inhibitor
    • Meydan, N., Grunberger, T., Dadi, H., Shahar, M., Arpaia, E., Lapidot, Z., et al. Inhibition of acute lymphoblastic leukaemia by a jak-2 inhibitor. Nature 379:6566 (1996), 645–648.
    • (1996) Nature , vol.379 , Issue.6566 , pp. 645-648
    • Meydan, N.1    Grunberger, T.2    Dadi, H.3    Shahar, M.4    Arpaia, E.5    Lapidot, Z.6
  • 110
    • 0030852328 scopus 로고    scopus 로고
    • Fusion of TEL, the ETS-variant gene 6 (ETV6), to the receptor-associated kinase JAK2 as a result of t(9;12) in a lymphoid and t(9;15;12) in a myeloid leukemia
    • Peeters, P., Raynaud, S.D., Cools, J., Wlodarska, I., Grosgeorge, J., Philip, P., et al. Fusion of TEL, the ETS-variant gene 6 (ETV6), to the receptor-associated kinase JAK2 as a result of t(9;12) in a lymphoid and t(9;15;12) in a myeloid leukemia. Blood 90:7 (1997), 2535–2540.
    • (1997) Blood , vol.90 , Issue.7 , pp. 2535-2540
    • Peeters, P.1    Raynaud, S.D.2    Cools, J.3    Wlodarska, I.4    Grosgeorge, J.5    Philip, P.6
  • 111
    • 27944481825 scopus 로고    scopus 로고
    • The t (8; 9)(p22; p24) translocation in atypical chronic myeloid leukaemia yields a new PCM1-JAK2 fusion gene
    • Bousquet, M., Quelen, C., De Mas, V., Duchayne, E., Roquefeuil, B., Delsol, G., et al. The t (8; 9)(p22; p24) translocation in atypical chronic myeloid leukaemia yields a new PCM1-JAK2 fusion gene. Oncogene 24:48 (2005), 7248–7252.
    • (2005) Oncogene , vol.24 , Issue.48 , pp. 7248-7252
    • Bousquet, M.1    Quelen, C.2    De Mas, V.3    Duchayne, E.4    Roquefeuil, B.5    Delsol, G.6
  • 112
    • 20144389913 scopus 로고    scopus 로고
    • The t(8;9)(p22;p24) is a recurrent abnormality in chronic and acute leukemia that fuses PCM1 to JAK2
    • Reiter, A., Walz, C., Watmore, A., Schoch, C., Blau, I., Schlegelberger, B., et al. The t(8;9)(p22;p24) is a recurrent abnormality in chronic and acute leukemia that fuses PCM1 to JAK2. Cancer Res. 65:7 (2005), 2662–2667.
    • (2005) Cancer Res. , vol.65 , Issue.7 , pp. 2662-2667
    • Reiter, A.1    Walz, C.2    Watmore, A.3    Schoch, C.4    Blau, I.5    Schlegelberger, B.6
  • 113
    • 77952614673 scopus 로고    scopus 로고
    • Chromosome 9p24 abnormalities: Prevalence, description of novel JAK2 translocations, JAK2V617F mutation analysis and clinicopathologic correlates
    • Patnaik, M.M., Knudson, R.A., Gangat, N., Hanson, C.A., Pardanani, A., Tefferi, A., et al. Chromosome 9p24 abnormalities: Prevalence, description of novel JAK2 translocations, JAK2V617F mutation analysis and clinicopathologic correlates. Eur. J. Haematol. 84:6 (2010), 518–524.
    • (2010) Eur. J. Haematol. , vol.84 , Issue.6 , pp. 518-524
    • Patnaik, M.M.1    Knudson, R.A.2    Gangat, N.3    Hanson, C.A.4    Pardanani, A.5    Tefferi, A.6
  • 114
    • 84929606569 scopus 로고    scopus 로고
    • Identification of SPAG9 as a novel JAK2 fusion partner gene in pediatric acute lymphoblastic leukemia with t (9; 17)(p24; q21)
    • Kawamura, M., Taki, T., Kaku, H., Ohki, K., Hayashi, Y., Identification of SPAG9 as a novel JAK2 fusion partner gene in pediatric acute lymphoblastic leukemia with t (9; 17)(p24; q21). Genes Chromosomes Cancer 54:7 (2015), 401–408.
    • (2015) Genes Chromosomes Cancer , vol.54 , Issue.7 , pp. 401-408
    • Kawamura, M.1    Taki, T.2    Kaku, H.3    Ohki, K.4    Hayashi, Y.5
  • 115
    • 25844469587 scopus 로고    scopus 로고
    • A BCR–JAK2 fusion gene as the result of at (9; 22)(p24; q11. 2) translocation in a patient with a clinically typical chronic myeloid leukemia
    • Griesinger, F., Hennig, H., Hillmer, F., Podleschny, M., Steffens, R., Pies, A., et al. A BCR–JAK2 fusion gene as the result of at (9; 22)(p24; q11. 2) translocation in a patient with a clinically typical chronic myeloid leukemia. Genes Chromosomes Cancer 44:3 (2005), 329–333.
    • (2005) Genes Chromosomes Cancer , vol.44 , Issue.3 , pp. 329-333
    • Griesinger, F.1    Hennig, H.2    Hillmer, F.3    Podleschny, M.4    Steffens, R.5    Pies, A.6
  • 116
    • 20144363192 scopus 로고    scopus 로고
    • Acquired mutation of the tyrosine kinase JAK2 in human myeloproliferative disorders
    • Baxter, E.J., Scott, L.M., Campbell, P.J., East, C., Fourouclas, N., Swanton, S., et al. Acquired mutation of the tyrosine kinase JAK2 in human myeloproliferative disorders. Lancet 365:9464 (2005), 1054–1061.
    • (2005) Lancet , vol.365 , Issue.9464 , pp. 1054-1061
    • Baxter, E.J.1    Scott, L.M.2    Campbell, P.J.3    East, C.4    Fourouclas, N.5    Swanton, S.6
  • 117
    • 17844383458 scopus 로고    scopus 로고
    • A unique clonal JAK2 mutation leading to constitutive signalling causes polycythaemia vera
    • James, C., Ugo, V., Le Couédic, J.P., Staerk, J., Delhommeau, F., Lacout, C., et al. A unique clonal JAK2 mutation leading to constitutive signalling causes polycythaemia vera. Nature 434:7037 (2005), 1144–1148.
    • (2005) Nature , vol.434 , Issue.7037 , pp. 1144-1148
    • James, C.1    Ugo, V.2    Le Couédic, J.P.3    Staerk, J.4    Delhommeau, F.5    Lacout, C.6
  • 119
    • 20244369569 scopus 로고    scopus 로고
    • Activating mutation in the tyrosine kinase JAK2 in polycythemia vera, essential thrombocythemia, and myeloid metaplasia with myelofibrosis
    • Levine, R.L., Wadleigh, M., Cools, J., Ebert, B.L., Wernig, G., Huntly, B.J.P., et al. Activating mutation in the tyrosine kinase JAK2 in polycythemia vera, essential thrombocythemia, and myeloid metaplasia with myelofibrosis. Cancer Cell 7:4 (2005), 387–397.
    • (2005) Cancer Cell , vol.7 , Issue.4 , pp. 387-397
    • Levine, R.L.1    Wadleigh, M.2    Cools, J.3    Ebert, B.L.4    Wernig, G.5    Huntly, B.J.P.6
  • 120
    • 36248991883 scopus 로고    scopus 로고
    • The JAK2 V617F allele burden in essential thrombocythemia, polycythemia vera and primary myelofibrosis–impact on disease phenotype
    • Larsen, T.S., Pallisgaard, N., Møller, M.B., Hasselbalch, H.C., The JAK2 V617F allele burden in essential thrombocythemia, polycythemia vera and primary myelofibrosis–impact on disease phenotype. Eur. J. Haematol. 79:6 (2007), 508–515.
    • (2007) Eur. J. Haematol. , vol.79 , Issue.6 , pp. 508-515
    • Larsen, T.S.1    Pallisgaard, N.2    Møller, M.B.3    Hasselbalch, H.C.4
  • 121
    • 34347385613 scopus 로고    scopus 로고
    • Different STAT-3 and STAT-5 phosphorylation discriminates among ph-negative chronic myeloproliferative diseases and is independent of the V617F JAK-2 mutation
    • Teofili, L., Martini, M., Cenci, T., Petrucci, G., Torti, L., Storti, S., et al. Different STAT-3 and STAT-5 phosphorylation discriminates among ph-negative chronic myeloproliferative diseases and is independent of the V617F JAK-2 mutation. Blood 110:1 (2007), 354–359.
    • (2007) Blood , vol.110 , Issue.1 , pp. 354-359
    • Teofili, L.1    Martini, M.2    Cenci, T.3    Petrucci, G.4    Torti, L.5    Storti, S.6
  • 122
    • 35648996038 scopus 로고    scopus 로고
    • JAK2-V617F activating mutation in acute myeloid leukemia: Prognostic impact and association with other molecular markers
    • Vicente, C., Vázquez, I., Marcotegui, N., Conchillo, A., Carranza, C., Rivell, G., et al. JAK2-V617F activating mutation in acute myeloid leukemia: Prognostic impact and association with other molecular markers. Leukemia 21:11 (2007), 2386–2391.
    • (2007) Leukemia , vol.21 , Issue.11 , pp. 2386-2391
    • Vicente, C.1    Vázquez, I.2    Marcotegui, N.3    Conchillo, A.4    Carranza, C.5    Rivell, G.6
  • 123
    • 65649096940 scopus 로고    scopus 로고
    • Mutational analysis of JAK1 gene in human hepatocellular carcinoma
    • Xie, H.J., Bae, H.J., Noh, J.H., Eun, J.W., Kim, J.K., Jung, K.H., et al. Mutational analysis of JAK1 gene in human hepatocellular carcinoma. Neoplasma 56:2 (2009), 136–140.
    • (2009) Neoplasma , vol.56 , Issue.2 , pp. 136-140
    • Xie, H.J.1    Bae, H.J.2    Noh, J.H.3    Eun, J.W.4    Kim, J.K.5    Jung, K.H.6
  • 124
    • 50949127379 scopus 로고    scopus 로고
    • Characteristics and clinical correlates of MPL 515W>L/K mutation in essential thrombocythemia
    • Vannucchi, A.M., Antonioli, E., Guglielmelli, P., Pancrazzi, A., Guerini, V., Barosi, G., et al. Characteristics and clinical correlates of MPL 515W>L/K mutation in essential thrombocythemia. Blood 112:3 (2008), 844–847.
    • (2008) Blood , vol.112 , Issue.3 , pp. 844-847
    • Vannucchi, A.M.1    Antonioli, E.2    Guglielmelli, P.3    Pancrazzi, A.4    Guerini, V.5    Barosi, G.6
  • 125
    • 84873726286 scopus 로고    scopus 로고
    • Tryptophan at the transmembrane–cytosolic junction modulates thrombopoietin receptor dimerization and activation
    • Defour, J., Itaya, M., Gryshkova, V., Brett, I.C., Pecquet, C., Sato, T., et al. Tryptophan at the transmembrane–cytosolic junction modulates thrombopoietin receptor dimerization and activation. Proc. Natl. Acad. Sci. U. S. A., 2013.
    • (2013) Proc. Natl. Acad. Sci. U. S. A.
    • Defour, J.1    Itaya, M.2    Gryshkova, V.3    Brett, I.C.4    Pecquet, C.5    Sato, T.6
  • 126
    • 84958019754 scopus 로고    scopus 로고
    • His499 regulates dimerization and prevents oncogenic activation by asparagine mutations of the human thrombopoietin receptor
    • jbc. M115. 696534
    • Leroy, E., Defour, J., Sato, T., Dass, S., Gryshkova, V., Marlar, S.M., et al. His499 regulates dimerization and prevents oncogenic activation by asparagine mutations of the human thrombopoietin receptor. J. Biol. Chem., 2015 jbc. M115. 696534.
    • (2015) J. Biol. Chem.
    • Leroy, E.1    Defour, J.2    Sato, T.3    Dass, S.4    Gryshkova, V.5    Marlar, S.M.6
  • 127
    • 84960906311 scopus 로고    scopus 로고
    • Activation of the thrombopoietin receptor by mutant calreticulin in CALR-mutant myeloproliferative neoplasms
    • Araki, M., Yang, Y., Masubuchi, N., Hironaka, Y., Takei, H., Morishita, S., et al. Activation of the thrombopoietin receptor by mutant calreticulin in CALR-mutant myeloproliferative neoplasms. Blood 127:10 (2016), 1307–1316.
    • (2016) Blood , vol.127 , Issue.10 , pp. 1307-1316
    • Araki, M.1    Yang, Y.2    Masubuchi, N.3    Hironaka, Y.4    Takei, H.5    Morishita, S.6
  • 128
    • 84962360217 scopus 로고    scopus 로고
    • Mutant calreticulin requires both its mutant C-terminus and the thrombopoietin receptor for oncogenic transformation
    • Elf, S., Abdelfattah, N.S., Chen, E., Perales-Paton, J., Rosen, E.A., Ko, A., et al. Mutant calreticulin requires both its mutant C-terminus and the thrombopoietin receptor for oncogenic transformation. Cancer Discov. 6:4 (2016), 368–381.
    • (2016) Cancer Discov. , vol.6 , Issue.4 , pp. 368-381
    • Elf, S.1    Abdelfattah, N.S.2    Chen, E.3    Perales-Paton, J.4    Rosen, E.A.5    Ko, A.6
  • 129
    • 77953529304 scopus 로고    scopus 로고
    • JAK2 V617F and beyond: Role of genetics and aberrant signaling in the pathogenesis of myeloproliferative neoplasms
    • Oh, S.T., Gotlib, J., JAK2 V617F and beyond: Role of genetics and aberrant signaling in the pathogenesis of myeloproliferative neoplasms. Expert. Rev. Hematol. 3:3 (2010), 323–337.
    • (2010) Expert. Rev. Hematol. , vol.3 , Issue.3 , pp. 323-337
    • Oh, S.T.1    Gotlib, J.2
  • 130
    • 84956556396 scopus 로고    scopus 로고
    • LNK mutations and myeloproliferative disorders
    • McMullin, M.F., Cario, H., LNK mutations and myeloproliferative disorders. Am. J. Hematol. 91:2 (2016), 248–251.
    • (2016) Am. J. Hematol. , vol.91 , Issue.2 , pp. 248-251
    • McMullin, M.F.1    Cario, H.2
  • 131
  • 132
    • 33845897463 scopus 로고    scopus 로고
    • Human tyrosine kinase 2 deficiency reveals its requisite roles in multiple cytokine signals involved in innate and acquired immunity
    • Minegishi, Y., Saito, M., Morio, T., Watanabe, K., Agematsu, K., Tsuchiya, S., et al. Human tyrosine kinase 2 deficiency reveals its requisite roles in multiple cytokine signals involved in innate and acquired immunity. Immunity 25:5 (2006), 745–755.
    • (2006) Immunity , vol.25 , Issue.5 , pp. 745-755
    • Minegishi, Y.1    Saito, M.2    Morio, T.3    Watanabe, K.4    Agematsu, K.5    Tsuchiya, S.6
  • 134
    • 84877595634 scopus 로고    scopus 로고
    • TYK2-STAT1-BCL2 pathway dependence in T-cell acute lymphoblastic leukemia
    • Sanda, T., Tyner, J.W., Gutierrez, A., Ngo, V.N., Glover, J., Chang, B.H., et al. TYK2-STAT1-BCL2 pathway dependence in T-cell acute lymphoblastic leukemia. Cancer Discov 3:5 (2013), 564–577.
    • (2013) Cancer Discov , vol.3 , Issue.5 , pp. 564-577
    • Sanda, T.1    Tyner, J.W.2    Gutierrez, A.3    Ngo, V.N.4    Glover, J.5    Chang, B.H.6
  • 135
    • 84996802211 scopus 로고    scopus 로고
    • Germline activating TYK2 mutations in pediatric patients with two primary acute lymphoblastic leukemia occurrences
    • Waanders, E., Scheijen, B., Jongmans, M., Venselaar, H., van Reijmersdal, S., van Dijk, A., et al. Germline activating TYK2 mutations in pediatric patients with two primary acute lymphoblastic leukemia occurrences. Leukemia, 31(4), 2017, 821.
    • (2017) Leukemia , vol.31 , Issue.4 , pp. 821
    • Waanders, E.1    Scheijen, B.2    Jongmans, M.3    Venselaar, H.4    van Reijmersdal, S.5    van Dijk, A.6
  • 136
    • 84886611381 scopus 로고    scopus 로고
    • SOCS proteins in development and disease
    • Trengove, M.C., Ward, A.C., SOCS proteins in development and disease. Am J Clin Exp Immunol 2:1 (2013), 1–29.
    • (2013) Am J Clin Exp Immunol , vol.2 , Issue.1 , pp. 1-29
    • Trengove, M.C.1    Ward, A.C.2
  • 137
    • 84899547538 scopus 로고    scopus 로고
    • SOCS signaling in autoimmune diseases: Molecular mechanisms and therapeutic implications
    • Liang, Y., Xu, W., Peng, H., Pan, H., Ye, D., SOCS signaling in autoimmune diseases: Molecular mechanisms and therapeutic implications. Eur. J. Immunol. 44:5 (2014), 1265–1275.
    • (2014) Eur. J. Immunol. , vol.44 , Issue.5 , pp. 1265-1275
    • Liang, Y.1    Xu, W.2    Peng, H.3    Pan, H.4    Ye, D.5
  • 138
    • 38749118957 scopus 로고    scopus 로고
    • Decreased expression of SOCS-3 mRNA in breast cancer with lymph node metastasis
    • Nakagawa, T., Iida, S., Osanai, T., Uetake, H., Aruga, T., Toriya, Y., et al. Decreased expression of SOCS-3 mRNA in breast cancer with lymph node metastasis. Oncol. Rep. 19:1 (2008), 33–39.
    • (2008) Oncol. Rep. , vol.19 , Issue.1 , pp. 33-39
    • Nakagawa, T.1    Iida, S.2    Osanai, T.3    Uetake, H.4    Aruga, T.5    Toriya, Y.6
  • 139
    • 34247265510 scopus 로고    scopus 로고
    • Functional polymorphism in the suppressor of cytokine signaling 1 gene associated with adult asthma
    • Harada, M., Nakashima, K., Hirota, T., Shimizu, M., Doi, S., Fujita, K., et al. Functional polymorphism in the suppressor of cytokine signaling 1 gene associated with adult asthma. Am. J. Respir. Cell Mol. Biol. 36:4 (2007), 491–496.
    • (2007) Am. J. Respir. Cell Mol. Biol. , vol.36 , Issue.4 , pp. 491-496
    • Harada, M.1    Nakashima, K.2    Hirota, T.3    Shimizu, M.4    Doi, S.5    Fujita, K.6
  • 141
    • 38849121220 scopus 로고    scopus 로고
    • Association between suppressors of cytokine signalling, t-helper type 1/t-helper type 2 balance and allergic sensitization in children
    • Daegelmann, C., Herberth, G., Röder, S., Herbarth, O., Giese, T., Krämer, U., et al. Association between suppressors of cytokine signalling, t-helper type 1/t-helper type 2 balance and allergic sensitization in children. Clin. Exp. Allergy 38:3 (2008), 438–448.
    • (2008) Clin. Exp. Allergy , vol.38 , Issue.3 , pp. 438-448
    • Daegelmann, C.1    Herberth, G.2    Röder, S.3    Herbarth, O.4    Giese, T.5    Krämer, U.6
  • 143
    • 84919684042 scopus 로고    scopus 로고
    • Mechanisms of jak/STAT signaling in immunity and disease
    • Villarino, A.V., Kanno, Y., Ferdinand, J.R., O'Shea, J.J., Mechanisms of jak/STAT signaling in immunity and disease. J. Immunol. 194:1 (2015), 21–27.
    • (2015) J. Immunol. , vol.194 , Issue.1 , pp. 21-27
    • Villarino, A.V.1    Kanno, Y.2    Ferdinand, J.R.3    O'Shea, J.J.4
  • 145
    • 84928387908 scopus 로고    scopus 로고
    • Tyrosine kinase 2-mediated signal transduction in T lymphocytes is blocked by pharmacological stabilization of its pseudokinase domain
    • Tokarski, J.S., Zupa-Fernandez, A., Tredup, J.A., Pike, K., Chang, C., Xie, D., et al. Tyrosine kinase 2-mediated signal transduction in T lymphocytes is blocked by pharmacological stabilization of its pseudokinase domain. J. Biol. Chem. 290:17 (2015), 11061–11074.
    • (2015) J. Biol. Chem. , vol.290 , Issue.17 , pp. 11061-11074
    • Tokarski, J.S.1    Zupa-Fernandez, A.2    Tredup, J.A.3    Pike, K.4    Chang, C.5    Xie, D.6
  • 146
    • 85018510428 scopus 로고    scopus 로고
    • Identification of imidazo [1, 2-b] pyridazine TYK2 pseudokinase ligands as potent and selective allosteric inhibitors of TYK2 signalling
    • Moslin, R., Gardner, D., Santella, J., Zhang, Y., Duncia, J., Liu, C., et al. Identification of imidazo [1, 2-b] pyridazine TYK2 pseudokinase ligands as potent and selective allosteric inhibitors of TYK2 signalling. Med. Chem. Commun. 8:4 (2017), 700–712.
    • (2017) Med. Chem. Commun. , vol.8 , Issue.4 , pp. 700-712
    • Moslin, R.1    Gardner, D.2    Santella, J.3    Zhang, Y.4    Duncia, J.5    Liu, C.6
  • 147
    • 85020403925 scopus 로고    scopus 로고
    • JAK2 JH2 fluorescence polarization assay and crystal structures for complexes with three small molecules
    • Newton, A.S., Deiana, L., Puleo, D., Cisneros, J.A., Cutrona, K.J., Schlessinger, J., et al. JAK2 JH2 fluorescence polarization assay and crystal structures for complexes with three small molecules. ACS Med. Chem. Lett. 8:6 (2017), 614–617.
    • (2017) ACS Med. Chem. Lett. , vol.8 , Issue.6 , pp. 614-617
    • Newton, A.S.1    Deiana, L.2    Puleo, D.3    Cisneros, J.A.4    Cutrona, K.J.5    Schlessinger, J.6
  • 148
    • 85020466558 scopus 로고    scopus 로고
    • Identification and characterization of JAK2 pseudokinase domain small molecule binders
    • Puleo, D., Kucera, K., Hammaren, H., Ungureanu, D., Newton, A., Silvennoinen, O., et al. Identification and characterization of JAK2 pseudokinase domain small molecule binders. ACS Med. Chem. Lett. 8:6 (2017), 618–621.
    • (2017) ACS Med. Chem. Lett. , vol.8 , Issue.6 , pp. 618-621
    • Puleo, D.1    Kucera, K.2    Hammaren, H.3    Ungureanu, D.4    Newton, A.5    Silvennoinen, O.6
  • 149
    • 85013106430 scopus 로고    scopus 로고
    • Rethinking JAK2 inhibition: Towards novel strategies of more specific and versatile janus kinase inhibition
    • Leroy, E., Constantinescu, S.N., Rethinking JAK2 inhibition: Towards novel strategies of more specific and versatile janus kinase inhibition. Leukemia 31:5 (2017), 1023–1038.
    • (2017) Leukemia , vol.31 , Issue.5 , pp. 1023-1038
    • Leroy, E.1    Constantinescu, S.N.2
  • 150
    • 0141720769 scopus 로고    scopus 로고
    • Class II cytokine receptors and their ligands: Key antiviral and inflammatory modulators
    • Renauld, J., Class II cytokine receptors and their ligands: Key antiviral and inflammatory modulators. Nat. Rev. Immunol. 3:8 (2003), 667–676.
    • (2003) Nat. Rev. Immunol. , vol.3 , Issue.8 , pp. 667-676
    • Renauld, J.1
  • 151
    • 84922479625 scopus 로고    scopus 로고
    • The IL-20 subfamily of cytokines—from host defence to tissue homeostasis
    • Rutz, S., Wang, X., Ouyang, W., The IL-20 subfamily of cytokines—from host defence to tissue homeostasis. Nat. Rev. Immunol. 14:12 (2014), 783–795.
    • (2014) Nat. Rev. Immunol. , vol.14 , Issue.12 , pp. 783-795
    • Rutz, S.1    Wang, X.2    Ouyang, W.3
  • 152
    • 84941941096 scopus 로고    scopus 로고
    • The biology of interleukin-27 reveals unique pro-and anti-inflammatory functions in immunity
    • Aparicio-Siegmund, S., Garbers, C., The biology of interleukin-27 reveals unique pro-and anti-inflammatory functions in immunity. Cytokine Growth Factor Rev. 26:5 (2015), 579–586.
    • (2015) Cytokine Growth Factor Rev. , vol.26 , Issue.5 , pp. 579-586
    • Aparicio-Siegmund, S.1    Garbers, C.2
  • 153
    • 84864124859 scopus 로고    scopus 로고
    • IL-12 family cytokines: Immunological playmakers
    • Vignali, D.A., Kuchroo, V.K., IL-12 family cytokines: Immunological playmakers. Nat. Immunol. 13:8 (2012), 722–728.
    • (2012) Nat. Immunol. , vol.13 , Issue.8 , pp. 722-728
    • Vignali, D.A.1    Kuchroo, V.K.2
  • 154
    • 52949111844 scopus 로고    scopus 로고
    • Inteferons pen the JAK–STAT pathway
    • Schindler, C., Plumlee, C., Inteferons pen the JAK–STAT pathway. Semin. Cell Dev. Biol. 19:4 (2008), 311–318.
    • (2008) Semin. Cell Dev. Biol. , vol.19 , Issue.4 , pp. 311-318
    • Schindler, C.1    Plumlee, C.2
  • 155
    • 35348850734 scopus 로고    scopus 로고
    • Hematopoietic cytokine receptor signaling
    • Baker, S., Rane, S., Reddy, E., Hematopoietic cytokine receptor signaling. Oncogene 26:47 (2007), 6724–6737.
    • (2007) Oncogene , vol.26 , Issue.47 , pp. 6724-6737
    • Baker, S.1    Rane, S.2    Reddy, E.3
  • 156
    • 42749087384 scopus 로고    scopus 로고
    • The extended IL-10 superfamily: IL-10, IL-19, IL-20, IL-22, IL-24, IL-26, IL-28, and IL-29
    • Commins, S., Steinke, J.W., Borish, L., The extended IL-10 superfamily: IL-10, IL-19, IL-20, IL-22, IL-24, IL-26, IL-28, and IL-29. J. Allergy Clin. Immunol. 121:5 (2008), 1108–1111.
    • (2008) J. Allergy Clin. Immunol. , vol.121 , Issue.5 , pp. 1108-1111
    • Commins, S.1    Steinke, J.W.2    Borish, L.3
  • 157
    • 79551575494 scopus 로고    scopus 로고
    • Janus kinase inhibitors for the treatment of myeloproliferative neoplasias and beyond
    • Quintás-Cardama, A., Kantarjian, H., Cortes, J., Verstovsek, S., Janus kinase inhibitors for the treatment of myeloproliferative neoplasias and beyond. Nat. Rev. Drug Discov. 10:2 (2011), 127–140.
    • (2011) Nat. Rev. Drug Discov. , vol.10 , Issue.2 , pp. 127-140
    • Quintás-Cardama, A.1    Kantarjian, H.2    Cortes, J.3    Verstovsek, S.4
  • 160
    • 84941943727 scopus 로고    scopus 로고
    • Cardiotrophin-like cytokine factor 1 (CLCF1) and neuropoietin (NP) signalling and their roles in development, adulthood, cancer and degenerative disorders
    • Sims, N.A., Cardiotrophin-like cytokine factor 1 (CLCF1) and neuropoietin (NP) signalling and their roles in development, adulthood, cancer and degenerative disorders. Cytokine Growth Factor Rev. 26:5 (2015), 517–522.
    • (2015) Cytokine Growth Factor Rev. , vol.26 , Issue.5 , pp. 517-522
    • Sims, N.A.1
  • 161
    • 57049124847 scopus 로고    scopus 로고
    • Structures and biological functions of IL-31 and IL-31 receptors
    • Zhang, Q., Putheti, P., Zhou, Q., Liu, Q., Gao, W., Structures and biological functions of IL-31 and IL-31 receptors. Cytokine Growth Factor Rev. 19:5 (2008), 347–356.
    • (2008) Cytokine Growth Factor Rev. , vol.19 , Issue.5 , pp. 347-356
    • Zhang, Q.1    Putheti, P.2    Zhou, Q.3    Liu, Q.4    Gao, W.5
  • 162
    • 9644295710 scopus 로고    scopus 로고
    • Cytokines and immunodeficiency diseases: Critical roles of the γc-dependent cytokines interleukins 2, 4, 7, 9, 15, and 21, and their signaling pathways
    • Kovanen, P.E., Leonard, W.J., Cytokines and immunodeficiency diseases: Critical roles of the γc-dependent cytokines interleukins 2, 4, 7, 9, 15, and 21, and their signaling pathways. Immunol. Rev. 202:1 (2004), 67–83.
    • (2004) Immunol. Rev. , vol.202 , Issue.1 , pp. 67-83
    • Kovanen, P.E.1    Leonard, W.J.2
  • 163
    • 84906655742 scopus 로고    scopus 로고
    • TSLP signaling pathway map: A platform for analysis of TSLP-mediated signaling
    • Zhong, J., Sharma, J., Raju, R., Palapetta, S.M., Prasad, T., Huang, T., et al. TSLP signaling pathway map: A platform for analysis of TSLP-mediated signaling. Database (Oxford), 2014, 2014, bau007.
    • (2014) Database (Oxford) , vol.2014 , pp. bau007
    • Zhong, J.1    Sharma, J.2    Raju, R.3    Palapetta, S.M.4    Prasad, T.5    Huang, T.6
  • 164
    • 0032076183 scopus 로고    scopus 로고
    • Disruption of the Jak1 gene demonstrates obligatory and nonredundant roles of the jaks in cytokine-induced biologic responses
    • Rodig, S.J., Meraz, M.A., White, J.M., Lampe, P.A., Riley, J.K., Arthur, C.D., et al. Disruption of the Jak1 gene demonstrates obligatory and nonredundant roles of the jaks in cytokine-induced biologic responses. Cell 93:3 (1998), 373–383.
    • (1998) Cell , vol.93 , Issue.3 , pp. 373-383
    • Rodig, S.J.1    Meraz, M.A.2    White, J.M.3    Lampe, P.A.4    Riley, J.K.5    Arthur, C.D.6
  • 165
    • 0034804745 scopus 로고    scopus 로고
    • Mutations in severe combined immune deficiency (SCID) due to JAK3 deficiency
    • Notarangelo, L.D., Mella, P., Jones, A., de Saint, Basile G, Savoldi, G., Cranston, T., et al. Mutations in severe combined immune deficiency (SCID) due to JAK3 deficiency. Hum. Mutat. 18:4 (2001), 255–263.
    • (2001) Hum. Mutat. , vol.18 , Issue.4 , pp. 255-263
    • Notarangelo, L.D.1    Mella, P.2    Jones, A.3    de Saint, B.G.4    Savoldi, G.5    Cranston, T.6
  • 166
    • 80053499723 scopus 로고    scopus 로고
    • A structure-function perspective of jak2 mutations and implications for alternate drug design strategies: The road not taken
    • Gnanasambandan, K., Sayeski, P., A structure-function perspective of jak2 mutations and implications for alternate drug design strategies: The road not taken. Curr. Med. Chem. 18:30 (2011), 4659–4673.
    • (2011) Curr. Med. Chem. , vol.18 , Issue.30 , pp. 4659-4673
    • Gnanasambandan, K.1    Sayeski, P.2
  • 167
    • 84895910321 scopus 로고    scopus 로고
    • JAK1 truncating mutations in gynecologic cancer define new role of cancer-associated protein tyrosine kinase aberrations
    • Ren, Y., Zhang, Y., Liu, R.Z., Fenstermacher, D.A., Wright, K.L., Teer, J.K., et al. JAK1 truncating mutations in gynecologic cancer define new role of cancer-associated protein tyrosine kinase aberrations. Sci. Rep., 3, 2013, 3042.
    • (2013) Sci. Rep. , vol.3 , pp. 3042
    • Ren, Y.1    Zhang, Y.2    Liu, R.Z.3    Fenstermacher, D.A.4    Wright, K.L.5    Teer, J.K.6
  • 168
    • 42249091014 scopus 로고    scopus 로고
    • Somatically acquired JAK1 mutations in adult acute lymphoblastic leukemia
    • Flex, E., Petrangeli, V., Stella, L., Chiaretti, S., Hornakova, T., Knoops, L., et al. Somatically acquired JAK1 mutations in adult acute lymphoblastic leukemia. J. Exp. Med. 205:4 (2008), 751–758.
    • (2008) J. Exp. Med. , vol.205 , Issue.4 , pp. 751-758
    • Flex, E.1    Petrangeli, V.2    Stella, L.3    Chiaretti, S.4    Hornakova, T.5    Knoops, L.6
  • 169
    • 84881041250 scopus 로고    scopus 로고
    • Whole-exome sequencing in adult ETP-ALL reveals a high rate of DNMT3A mutations
    • Neumann, M., Heesch, S., Schlee, C., Schwartz, S., Gokbuget, N., Hoelzer, D., et al. Whole-exome sequencing in adult ETP-ALL reveals a high rate of DNMT3A mutations. Blood 121:23 (2013), 4749–4752.
    • (2013) Blood , vol.121 , Issue.23 , pp. 4749-4752
    • Neumann, M.1    Heesch, S.2    Schlee, C.3    Schwartz, S.4    Gokbuget, N.5    Hoelzer, D.6
  • 170
    • 0035813208 scopus 로고    scopus 로고
    • Mapping of a region within the N terminus of Jak1 involved in cytokine receptor interaction
    • Haan, C., Is'harc, H., Hermanns, H.M., Schmitz-Van De Leur, H., Kerr, I.M., Heinrich, P.C., et al. Mapping of a region within the N terminus of Jak1 involved in cytokine receptor interaction. J. Biol. Chem. 276:40 (2001), 37451–37458.
    • (2001) J. Biol. Chem. , vol.276 , Issue.40 , pp. 37451-37458
    • Haan, C.1    Is'harc, H.2    Hermanns, H.M.3    Schmitz-Van De Leur, H.4    Kerr, I.M.5    Heinrich, P.C.6
  • 171
    • 84964787419 scopus 로고    scopus 로고
    • Structural modeling of JAK1 mutations in T-cell acute lymphoblastic leukemia reveals a second contact site between pseudokinase and kinase domains
    • Cante-Barrett, K., Uitdehaag, J.C., Meijerink, J.P., Structural modeling of JAK1 mutations in T-cell acute lymphoblastic leukemia reveals a second contact site between pseudokinase and kinase domains. Haematologica 101:5 (2016), e189–e191.
    • (2016) Haematologica , vol.101 , Issue.5 , pp. e189-e191
    • Cante-Barrett, K.1    Uitdehaag, J.C.2    Meijerink, J.P.3
  • 172
    • 84958092771 scopus 로고    scopus 로고
    • Activating JAK1 mutation may predict the sensitivity of JAK-STAT inhibition in hepatocellular carcinoma
    • Yang, S., Luo, C., Gu, Q., Xu, Q., Wang, G., Sun, H., et al. Activating JAK1 mutation may predict the sensitivity of JAK-STAT inhibition in hepatocellular carcinoma. Oncotarget 7:5 (2016), 5461–5469.
    • (2016) Oncotarget , vol.7 , Issue.5 , pp. 5461-5469
    • Yang, S.1    Luo, C.2    Gu, Q.3    Xu, Q.4    Wang, G.5    Sun, H.6
  • 173
    • 77955660663 scopus 로고    scopus 로고
    • Diverse somatic mutation patterns and pathway alterations in human cancers
    • Kan, Z., Jaiswal, B.S., Stinson, J., Janakiraman, V., Bhatt, D., Stern, H.M., et al. Diverse somatic mutation patterns and pathway alterations in human cancers. Nature 466:7308 (2010), 869–873.
    • (2010) Nature , vol.466 , Issue.7308 , pp. 869-873
    • Kan, Z.1    Jaiswal, B.S.2    Stinson, J.3    Janakiraman, V.4    Bhatt, D.5    Stern, H.M.6
  • 174
    • 82855168107 scopus 로고    scopus 로고
    • Mutations of PHF6 are associated with mutations of NOTCH1, JAK1 and rearrangement of SET-NUP214 in T-cell acute lymphoblastic leukemia
    • Wang, Q., Qiu, H., Jiang, H., Wu, L., Dong, S., Pan, J., et al. Mutations of PHF6 are associated with mutations of NOTCH1, JAK1 and rearrangement of SET-NUP214 in T-cell acute lymphoblastic leukemia. Haematologica 96:12 (2011), 1808–1814.
    • (2011) Haematologica , vol.96 , Issue.12 , pp. 1808-1814
    • Wang, Q.1    Qiu, H.2    Jiang, H.3    Wu, L.4    Dong, S.5    Pan, J.6
  • 175
    • 84923381331 scopus 로고    scopus 로고
    • Evaluation of the in vitro and in vivo efficacy of the JAK inhibitor AZD1480 against JAK-mutated acute lymphoblastic leukemia
    • Suryani, S., Bracken, L.S., Harvey, R.C., Sia, K.C., Carol, H., Chen, I., et al. Evaluation of the in vitro and in vivo efficacy of the JAK inhibitor AZD1480 against JAK-mutated acute lymphoblastic leukemia. Mol. Cancer Ther. 14:2 (2014), 364–374.
    • (2014) Mol. Cancer Ther. , vol.14 , Issue.2 , pp. 364-374
    • Suryani, S.1    Bracken, L.S.2    Harvey, R.C.3    Sia, K.C.4    Carol, H.5    Chen, I.6
  • 176
    • 84862907593 scopus 로고    scopus 로고
    • The genetic basis of early T-cell precursor acute lymphoblastic leukaemia
    • Zhang, J., Ding, L., Holmfeldt, L., Wu, G., Heatley, S.L., Payne-Turner, D., et al. The genetic basis of early T-cell precursor acute lymphoblastic leukaemia. Nature 481:7380 (2012), 157–163.
    • (2012) Nature , vol.481 , Issue.7380 , pp. 157-163
    • Zhang, J.1    Ding, L.2    Holmfeldt, L.3    Wu, G.4    Heatley, S.L.5    Payne-Turner, D.6
  • 177
    • 79958061888 scopus 로고    scopus 로고
    • Oncogenic JAK1 and JAK2-activating mutations resistant to ATP-competitive inhibitors
    • Hornakova, T., Springuel, L., Devreux, J., Dusa, A., Constantinescu, S.N., Knoops, L., et al. Oncogenic JAK1 and JAK2-activating mutations resistant to ATP-competitive inhibitors. Haematologica 96:6 (2011), 845–853.
    • (2011) Haematologica , vol.96 , Issue.6 , pp. 845-853
    • Hornakova, T.1    Springuel, L.2    Devreux, J.3    Dusa, A.4    Constantinescu, S.N.5    Knoops, L.6
  • 178
    • 52449119447 scopus 로고    scopus 로고
    • Somatic mutations of JAK1 and JAK3 in acute leukemias and solid cancers
    • Jeong, E.G., Kim, M.S., Nam, H.K., Min, C.K., Lee, S., Chung, Y.J., et al. Somatic mutations of JAK1 and JAK3 in acute leukemias and solid cancers. Clin. Cancer Res. 14:12 (2008), 3716–3721.
    • (2008) Clin. Cancer Res. , vol.14 , Issue.12 , pp. 3716-3721
    • Jeong, E.G.1    Kim, M.S.2    Nam, H.K.3    Min, C.K.4    Lee, S.5    Chung, Y.J.6
  • 179
    • 79959826613 scopus 로고    scopus 로고
    • PTPN2 negatively regulates oncogenic JAK1 in T-cell acute lymphoblastic leukemia
    • Kleppe, M., Soulier, J., Asnafi, V., Mentens, N., Hornakova, T., Knoops, L., et al. PTPN2 negatively regulates oncogenic JAK1 in T-cell acute lymphoblastic leukemia. Blood 117:26 (2011), 7090–7098.
    • (2011) Blood , vol.117 , Issue.26 , pp. 7090-7098
    • Kleppe, M.1    Soulier, J.2    Asnafi, V.3    Mentens, N.4    Hornakova, T.5    Knoops, L.6
  • 180
    • 29644439240 scopus 로고    scopus 로고
    • JAK1 and Tyk2 activation by the homologous polycythemia vera JAK2 V617F mutation cross-talk with IGF1 receptor
    • Staerk, J., Kallin, A., Demoulin, J., Vainchenker, W., Constantinescu, S.N., JAK1 and Tyk2 activation by the homologous polycythemia vera JAK2 V617F mutation cross-talk with IGF1 receptor. J. Biol. Chem. 280:51 (2005), 41893–41899.
    • (2005) J. Biol. Chem. , vol.280 , Issue.51 , pp. 41893-41899
    • Staerk, J.1    Kallin, A.2    Demoulin, J.3    Vainchenker, W.4    Constantinescu, S.N.5
  • 181
    • 85007011575 scopus 로고    scopus 로고
    • Biallelic JAK1 mutations in immunodeficient patient with mycobacterial infection
    • Eletto, D., Burns, S.O., Angulo, I., Plagnol, V., Gilmour, K.C., Henriquez, F., et al. Biallelic JAK1 mutations in immunodeficient patient with mycobacterial infection. Nat. Commun., 7, 2016, 13992.
    • (2016) Nat. Commun. , vol.7 , pp. 13992
    • Eletto, D.1    Burns, S.O.2    Angulo, I.3    Plagnol, V.4    Gilmour, K.C.5    Henriquez, F.6
  • 182
    • 33745793005 scopus 로고    scopus 로고
    • The mutation in the ATP-binding region of JAK1, identified in human uterine leiomyosarcomas, results in defective interferon-γ inducibility of TAP1 and LMP2
    • Hayashi, T., Kobayashi, Y., Kohsaka, S., Sano, K., The mutation in the ATP-binding region of JAK1, identified in human uterine leiomyosarcomas, results in defective interferon-γ inducibility of TAP1 and LMP2. Oncogene 25:29 (2006), 4016–4026.
    • (2006) Oncogene , vol.25 , Issue.29 , pp. 4016-4026
    • Hayashi, T.1    Kobayashi, Y.2    Kohsaka, S.3    Sano, K.4
  • 183
    • 84994579960 scopus 로고    scopus 로고
    • Gene panel sequencing improves the diagnostic work-up of patients with idiopathic erythrocytosis and identifies new mutations
    • Camps, C.D., Petousi, N., Bento, C., Cario, H., Copley, R.R., McMullin, M.F., et al. Gene panel sequencing improves the diagnostic work-up of patients with idiopathic erythrocytosis and identifies new mutations. Haematologica 101:11 (2016), 1306–1318.
    • (2016) Haematologica , vol.101 , Issue.11 , pp. 1306-1318
    • Camps, C.D.1    Petousi, N.2    Bento, C.3    Cario, H.4    Copley, R.R.5    McMullin, M.F.6
  • 184
    • 85015164274 scopus 로고    scopus 로고
    • Coexistence of gain-of-function JAK2 germline mutations with JAK2V617F in polycythemia vera
    • Lanikova, L., Babosova, O., Swierczek, S., Wang, L., Wheeler, D.A., Divoky, V., et al. Coexistence of gain-of-function JAK2 germline mutations with JAK2V617F in polycythemia vera. Blood 128:18 (2016), 2266–2270.
    • (2016) Blood , vol.128 , Issue.18 , pp. 2266-2270
    • Lanikova, L.1    Babosova, O.2    Swierczek, S.3    Wang, L.4    Wheeler, D.A.5    Divoky, V.6
  • 185
    • 77951904473 scopus 로고    scopus 로고
    • A new potential oncogenic mutation in the FERM domain of JAK2 in BCR/ABL1-negative and V617F-negative chronic myeloproliferative neoplasms revealed by a comprehensive screening of 17 tyrosine kinase coding genes
    • Aranaz, P., Ormazábal, C., Hurtado, C., Erquiaga, I., Calasanz, M.J., García-Delgado, M., et al. A new potential oncogenic mutation in the FERM domain of JAK2 in BCR/ABL1-negative and V617F-negative chronic myeloproliferative neoplasms revealed by a comprehensive screening of 17 tyrosine kinase coding genes. Cancer Genet. Cytogenet. 199:1 (2010), 1–8.
    • (2010) Cancer Genet. Cytogenet. , vol.199 , Issue.1 , pp. 1-8
    • Aranaz, P.1    Ormazábal, C.2    Hurtado, C.3    Erquiaga, I.4    Calasanz, M.J.5    García-Delgado, M.6
  • 186
    • 58849118941 scopus 로고    scopus 로고
    • Mutation profile of JAK2 transcripts in patients with chronic myeloproliferative neoplasias
    • Ma, W., Kantarjian, H., Zhang, X., Yeh, C.H., Zhang, Z.J., Verstovsek, S., et al. Mutation profile of JAK2 transcripts in patients with chronic myeloproliferative neoplasias. J. Mol. Diagn. 11:1 (2009), 49–53.
    • (2009) J. Mol. Diagn. , vol.11 , Issue.1 , pp. 49-53
    • Ma, W.1    Kantarjian, H.2    Zhang, X.3    Yeh, C.H.4    Zhang, Z.J.5    Verstovsek, S.6
  • 187
    • 33846660947 scopus 로고    scopus 로고
    • JAK2 exon 12 mutations in polycythemia vera and idiopathic erythrocytosis
    • Scott, L.M., Tong, W., Levine, R.L., Scott, M.A., Beer, P.A., Stratton, M.R., et al. JAK2 exon 12 mutations in polycythemia vera and idiopathic erythrocytosis. N. Engl. J. Med. 356:5 (2007), 459–468.
    • (2007) N. Engl. J. Med. , vol.356 , Issue.5 , pp. 459-468
    • Scott, L.M.1    Tong, W.2    Levine, R.L.3    Scott, M.A.4    Beer, P.A.5    Stratton, M.R.6
  • 188
    • 84992448488 scopus 로고    scopus 로고
    • Application of an NGS-based 28-gene panel in myeloproliferative neoplasms reveals distinct mutation patterns in essential thrombocythaemia, primary myelofibrosis and polycythaemia vera
    • Delic, S., Rose, D., Kern, W., Nadarajah, N., Haferlach, C., Haferlach, T., et al. Application of an NGS-based 28-gene panel in myeloproliferative neoplasms reveals distinct mutation patterns in essential thrombocythaemia, primary myelofibrosis and polycythaemia vera. Br. J. Haematol. 175:3 (2016), 419–426.
    • (2016) Br. J. Haematol. , vol.175 , Issue.3 , pp. 419-426
    • Delic, S.1    Rose, D.2    Kern, W.3    Nadarajah, N.4    Haferlach, C.5    Haferlach, T.6
  • 189
    • 84897903692 scopus 로고    scopus 로고
    • A novel activating, germline JAK2 mutation, JAK2R564Q, causes familial essential thrombocytosis
    • Etheridge, S.L., Cosgrove, M.E., Sangkhae, V., Corbo, L.M., Roh, M.E., Seeliger, M.A., et al. A novel activating, germline JAK2 mutation, JAK2R564Q, causes familial essential thrombocytosis. Blood 123:7 (2014), 1059–1068.
    • (2014) Blood , vol.123 , Issue.7 , pp. 1059-1068
    • Etheridge, S.L.1    Cosgrove, M.E.2    Sangkhae, V.3    Corbo, L.M.4    Roh, M.E.5    Seeliger, M.A.6
  • 190
    • 84857863366 scopus 로고    scopus 로고
    • Germline JAK2 mutation in a family with hereditary thrombocytosis
    • Mead, A.J., Rugless, M.J., Jacobsen, S.E.W., Schuh, A., Germline JAK2 mutation in a family with hereditary thrombocytosis. N. Engl. J. Med. 366:10 (2012), 967–969.
    • (2012) N. Engl. J. Med. , vol.366 , Issue.10 , pp. 967-969
    • Mead, A.J.1    Rugless, M.J.2    Jacobsen, S.E.W.3    Schuh, A.4
  • 191
    • 84880541262 scopus 로고    scopus 로고
    • Impact of isolated germline JAK2V617I mutation on human hematopoiesis
    • Mead, A.J., Chowdhury, O., Pecquet, C., Dusa, A., Woll, P., Atkinson, D., et al. Impact of isolated germline JAK2V617I mutation on human hematopoiesis. Blood 121:20 (2013), 4156–4165.
    • (2013) Blood , vol.121 , Issue.20 , pp. 4156-4165
    • Mead, A.J.1    Chowdhury, O.2    Pecquet, C.3    Dusa, A.4    Woll, P.5    Atkinson, D.6
  • 192
    • 84866777412 scopus 로고    scopus 로고
    • Amino acid residue E543 in JAK2 C618R is a potential therapeutic target for myeloproliferative disorders caused by JAK2 C618R mutation
    • Wu, Q.Y., Li, F., Guo, H.Y., Cao, J., Chen, C., Chen, W., et al. Amino acid residue E543 in JAK2 C618R is a potential therapeutic target for myeloproliferative disorders caused by JAK2 C618R mutation. Arch. Biochem. Biophys. 528:1 (2012), 57–66.
    • (2012) Arch. Biochem. Biophys. , vol.528 , Issue.1 , pp. 57-66
    • Wu, Q.Y.1    Li, F.2    Guo, H.Y.3    Cao, J.4    Chen, C.5    Chen, W.6
  • 193
    • 33751234537 scopus 로고    scopus 로고
    • Report on two novel nucleotide exchanges in the JAK2 pseudokinase domain: D620E and E627E
    • Schnittger, S., Bacher, U., Kern, W., Schröder, M., Haferlach, T., Schoch, C., Report on two novel nucleotide exchanges in the JAK2 pseudokinase domain: D620E and E627E. Leukemia 20:12 (2006), 2195–2197.
    • (2006) Leukemia , vol.20 , Issue.12 , pp. 2195-2197
    • Schnittger, S.1    Bacher, U.2    Kern, W.3    Schröder, M.4    Haferlach, T.5    Schoch, C.6
  • 195
    • 54349086521 scopus 로고    scopus 로고
    • Mutations of JAK2 in acute lymphoblastic leukaemias associated with down's syndrome
    • Bercovich, D., Ganmore, I., Scott, L.M., Wainreb, G., Birger, Y., Elimelech, A., et al. Mutations of JAK2 in acute lymphoblastic leukaemias associated with down's syndrome. Lancet 372:9648 (2008), 1484–1492.
    • (2008) Lancet , vol.372 , Issue.9648 , pp. 1484-1492
    • Bercovich, D.1    Ganmore, I.2    Scott, L.M.3    Wainreb, G.4    Birger, Y.5    Elimelech, A.6
  • 196
    • 84899696697 scopus 로고    scopus 로고
    • Germ-line JAK2 mutations in the kinase domain are responsible for hereditary thrombocytosis and are resistant to JAK2 and HSP90 inhibitors
    • Marty, C., Saint-Martin, C., Pecquet, C., Grosjean, S., Saliba, J., Mouton, C., et al. Germ-line JAK2 mutations in the kinase domain are responsible for hereditary thrombocytosis and are resistant to JAK2 and HSP90 inhibitors. Blood 123:9 (2014), 1372–1383.
    • (2014) Blood , vol.123 , Issue.9 , pp. 1372-1383
    • Marty, C.1    Saint-Martin, C.2    Pecquet, C.3    Grosjean, S.4    Saliba, J.5    Mouton, C.6
  • 197
    • 85015256474 scopus 로고    scopus 로고
    • Cooperation of germ line JAK2 mutations E846D and R1063H in hereditary erythrocytosis with megakaryocytic atypia
    • Kapralova, K., Horvathova, M., Pecquet, C., Fialova Kucerova, J., Pospisilova, D., Leroy, E., et al. Cooperation of germ line JAK2 mutations E846D and R1063H in hereditary erythrocytosis with megakaryocytic atypia. Blood 128:10 (2016), 1418–1423.
    • (2016) Blood , vol.128 , Issue.10 , pp. 1418-1423
    • Kapralova, K.1    Horvathova, M.2    Pecquet, C.3    Fialova Kucerova, J.4    Pospisilova, D.5    Leroy, E.6
  • 198
    • 1542343959 scopus 로고    scopus 로고
    • Janus kinase 3 (JAK3) deficiency: Clinical, immunologic, and molecular analyses of 10 patients and outcomes of stem cell transplantation
    • Roberts, J.L., Lengi, A., Brown, S.M., Chen, M., Zhou, Y.J., O'Shea, J.J., et al. Janus kinase 3 (JAK3) deficiency: Clinical, immunologic, and molecular analyses of 10 patients and outcomes of stem cell transplantation. Blood 103:6 (2004), 2009–2018.
    • (2004) Blood , vol.103 , Issue.6 , pp. 2009-2018
    • Roberts, J.L.1    Lengi, A.2    Brown, S.M.3    Chen, M.4    Zhou, Y.J.5    O'Shea, J.J.6
  • 200
    • 43449107692 scopus 로고    scopus 로고
    • Functional analysis of JAK3 mutations in transient myeloproliferative disorder and acute megakaryoblastic leukaemia accompanying down syndrome
    • Sato, T., Toki, T., Kanezaki, R., Xu, G., Terui, K., Kanegane, H., et al. Functional analysis of JAK3 mutations in transient myeloproliferative disorder and acute megakaryoblastic leukaemia accompanying down syndrome. Br. J. Haematol. 141:5 (2008), 681–688.
    • (2008) Br. J. Haematol. , vol.141 , Issue.5 , pp. 681-688
    • Sato, T.1    Toki, T.2    Kanezaki, R.3    Xu, G.4    Terui, K.5    Kanegane, H.6
  • 201
    • 0033559793 scopus 로고    scopus 로고
    • Autosomal SCID caused by a point mutation in the N-terminus of Jak3: Mapping of the Jak3-receptor interaction domain
    • Cacalano, N.A., Migone, T.S., Bazan, F., Hanson, E.P., Chen, M., Candotti, F., et al. Autosomal SCID caused by a point mutation in the N-terminus of Jak3: Mapping of the Jak3-receptor interaction domain. EMBO J. 18:6 (1999), 1549–1558.
    • (1999) EMBO J. , vol.18 , Issue.6 , pp. 1549-1558
    • Cacalano, N.A.1    Migone, T.S.2    Bazan, F.3    Hanson, E.P.4    Chen, M.5    Candotti, F.6
  • 202
    • 0034805720 scopus 로고    scopus 로고
    • Critical sites for the interaction between IL-2Rγ and JAK3 and the following signaling
    • Tang, W., Huo, H., Zhu, J., Ji, H., Zou, W., Xu, L., et al. Critical sites for the interaction between IL-2Rγ and JAK3 and the following signaling. Biochem. Biophys. Res. Commun. 283:3 (2001), 598–605.
    • (2001) Biochem. Biophys. Res. Commun. , vol.283 , Issue.3 , pp. 598-605
    • Tang, W.1    Huo, H.2    Zhu, J.3    Ji, H.4    Zou, W.5    Xu, L.6
  • 203
    • 33745713168 scopus 로고    scopus 로고
    • Activating alleles of JAK3 in acute megakaryoblastic leukemia
    • Walters, D.K., Mercher, T., Gu, T., O'Hare, T., Tyner, J.W., Loriaux, M., et al. Activating alleles of JAK3 in acute megakaryoblastic leukemia. Cancer Cell 10:1 (2006), 65–75.
    • (2006) Cancer Cell , vol.10 , Issue.1 , pp. 65-75
    • Walters, D.K.1    Mercher, T.2    Gu, T.3    O'Hare, T.4    Tyner, J.W.5    Loriaux, M.6
  • 204
    • 80052062979 scopus 로고    scopus 로고
    • Description of a novel janus kinase 3 P132A mutation in acute megakaryoblastic leukemia and demonstration of previously reported janus kinase 3 mutations in normal subjects
    • Riera, L., Lasorsa, E., Bonello, L., Sismondi, F., Tondat, F., Di Bello, C., et al. Description of a novel janus kinase 3 P132A mutation in acute megakaryoblastic leukemia and demonstration of previously reported janus kinase 3 mutations in normal subjects. Leuk Lymphoma 52:9 (2011), 1742–1750.
    • (2011) Leuk Lymphoma , vol.52 , Issue.9 , pp. 1742-1750
    • Riera, L.1    Lasorsa, E.2    Bonello, L.3    Sismondi, F.4    Tondat, F.5    Di Bello, C.6
  • 206
    • 80053638747 scopus 로고    scopus 로고
    • FERM domain mutations induce gain of function in JAK3 in adult T-cell leukemia/lymphoma
    • Elliott, N.E., Cleveland, S.M., Grann, V., Janik, J., Waldmann, T.A., Davé, U.P., FERM domain mutations induce gain of function in JAK3 in adult T-cell leukemia/lymphoma. Blood 118:14 (2011), 3911–3921.
    • (2011) Blood , vol.118 , Issue.14 , pp. 3911-3921
    • Elliott, N.E.1    Cleveland, S.M.2    Grann, V.3    Janik, J.4    Waldmann, T.A.5    Davé, U.P.6
  • 207
    • 84942880558 scopus 로고    scopus 로고
    • Comprehensive serial molecular profiling of an “N of 1” exceptional non-responder with metastatic prostate cancer progressing to small cell carcinoma on treatment
    • Kadakia, K.C., Tomlins, S.A., Sanghvi, S.K., Cani, A.K., Omata, K., Hovelson, D.H., et al. Comprehensive serial molecular profiling of an “N of 1” exceptional non-responder with metastatic prostate cancer progressing to small cell carcinoma on treatment. J. Hematol. Oncol., 8(1), 2015, 109.
    • (2015) J. Hematol. Oncol. , vol.8 , Issue.1 , pp. 109
    • Kadakia, K.C.1    Tomlins, S.A.2    Sanghvi, S.K.3    Cani, A.K.4    Omata, K.5    Hovelson, D.H.6
  • 208
    • 84911909502 scopus 로고    scopus 로고
    • JAK3 mutants transform hematopoietic cells through JAK1 activation, causing T-cell acute lymphoblastic leukemia in a mouse model
    • Degryse, S., de Bock, C.E., Cox, L., Demeyer, S., Gielen, O., Mentens, N., et al. JAK3 mutants transform hematopoietic cells through JAK1 activation, causing T-cell acute lymphoblastic leukemia in a mouse model. Blood 124:20 (2014), 3092–3100.
    • (2014) Blood , vol.124 , Issue.20 , pp. 3092-3100
    • Degryse, S.1    de Bock, C.E.2    Cox, L.3    Demeyer, S.4    Gielen, O.5    Mentens, N.6
  • 209
    • 84938756599 scopus 로고    scopus 로고
    • Targeted sequencing identifies associations between IL7R-JAK mutations and epigenetic modulators in T-cell acute lymphoblastic leukemia
    • Vicente, C., Schwab, C., Broux, M., Geerdens, E., Degryse, S., Demeyer, S., et al. Targeted sequencing identifies associations between IL7R-JAK mutations and epigenetic modulators in T-cell acute lymphoblastic leukemia. Haematologica 100:10 (2015), 1301–1310.
    • (2015) Haematologica , vol.100 , Issue.10 , pp. 1301-1310
    • Vicente, C.1    Schwab, C.2    Broux, M.3    Geerdens, E.4    Degryse, S.5    Demeyer, S.6
  • 210
    • 0030729823 scopus 로고    scopus 로고
    • Structural and functional basis for JAK3-deficient severe combined immunodeficiency
    • Candotti, F., Oakes, S.A., Johnston, J.A., Giliani, S., Schumacher, R.F., Mella, P., et al. Structural and functional basis for JAK3-deficient severe combined immunodeficiency. Blood 90:10 (1997), 3996–4003.
    • (1997) Blood , vol.90 , Issue.10 , pp. 3996-4003
    • Candotti, F.1    Oakes, S.A.2    Johnston, J.A.3    Giliani, S.4    Schumacher, R.F.5    Mella, P.6
  • 211
    • 0034021778 scopus 로고    scopus 로고
    • Complete genomic organization of the human JAK3 gene and mutation analysis in severe combined immunodeficiency by single-strand conformation polymorphism
    • Schumacher, R.F., Mella, P., Badolato, R., Fiorini, M., Savoldi, G., Giliani, S., et al. Complete genomic organization of the human JAK3 gene and mutation analysis in severe combined immunodeficiency by single-strand conformation polymorphism. Hum. Genet. 106:1 (2000), 73–79.
    • (2000) Hum. Genet. , vol.106 , Issue.1 , pp. 73-79
    • Schumacher, R.F.1    Mella, P.2    Badolato, R.3    Fiorini, M.4    Savoldi, G.5    Giliani, S.6
  • 212
    • 73649122760 scopus 로고    scopus 로고
    • Impaired IL-7 signaling may explain a case of atypical JAK3-SCID
    • Li, J., Nara, H., Rahman, M., Juliana, F.M., Araki, A., Asao, H., Impaired IL-7 signaling may explain a case of atypical JAK3-SCID. Cytokine 49:2 (2010), 221–228.
    • (2010) Cytokine , vol.49 , Issue.2 , pp. 221-228
    • Li, J.1    Nara, H.2    Rahman, M.3    Juliana, F.M.4    Araki, A.5    Asao, H.6
  • 214
    • 63849275092 scopus 로고    scopus 로고
    • Constitutive JAK3 activation induces lymphoproliferative syndromes in murine bone marrow transplantation models
    • Cornejo, M.G., Kharas, M.G., Werneck, M.B., Le Bras, S., Moore, S.A., Ball, B., et al. Constitutive JAK3 activation induces lymphoproliferative syndromes in murine bone marrow transplantation models. Blood 113:12 (2009), 2746–2754.
    • (2009) Blood , vol.113 , Issue.12 , pp. 2746-2754
    • Cornejo, M.G.1    Kharas, M.G.2    Werneck, M.B.3    Le Bras, S.4    Moore, S.A.5    Ball, B.6
  • 215
    • 85053113672 scopus 로고    scopus 로고
    • Transforming mutations of Jak3 (A573V and M511I) show differential sensitivity to selective Jak3 inhibitors
    • Martinez, G.S., Ross, J.A., Kirken, R.A., Transforming mutations of Jak3 (A573V and M511I) show differential sensitivity to selective Jak3 inhibitors. Clin. Cancer Drugs 3:2 (2016), 131–137.
    • (2016) Clin. Cancer Drugs , vol.3 , Issue.2 , pp. 131-137
    • Martinez, G.S.1    Ross, J.A.2    Kirken, R.A.3
  • 216
    • 85019045647 scopus 로고    scopus 로고
    • Novel JAK3-activating mutations in extranodal NK/T-cell lymphoma, nasal type
    • Sim, S.H., Kim, S., Kim, T.M., Jeon, Y.K., Nam, S.J., Ahn, Y., et al. Novel JAK3-activating mutations in extranodal NK/T-cell lymphoma, nasal type. Am. J. Pathol. 187:5 (2017), 980–986.
    • (2017) Am. J. Pathol. , vol.187 , Issue.5 , pp. 980-986
    • Sim, S.H.1    Kim, S.2    Kim, T.M.3    Jeon, Y.K.4    Nam, S.J.5    Ahn, Y.6
  • 217
    • 33847202261 scopus 로고    scopus 로고
    • JAK3 mutations occur in acute megakaryoblastic leukemia both in down syndrome children and non-down syndrome adults
    • Kiyoi, H., Yamaji, S., Kojima, S., Naoe, T., JAK3 mutations occur in acute megakaryoblastic leukemia both in down syndrome children and non-down syndrome adults. Leukemia 21:3 (2007), 574–576.
    • (2007) Leukemia , vol.21 , Issue.3 , pp. 574-576
    • Kiyoi, H.1    Yamaji, S.2    Kojima, S.3    Naoe, T.4
  • 218
    • 0035490376 scopus 로고    scopus 로고
    • Eleven novel JAK3 mutations in patients with severe combined immunodeficiency—including the first patients with mutations in the kinase domain
    • Mella, P., Schumacher, R.F., Cranston, T., de Saint, Basile G, Savoldi, G., Notarangelo, L.D., Eleven novel JAK3 mutations in patients with severe combined immunodeficiency—including the first patients with mutations in the kinase domain. Hum. Mutat. 18:4 (2001), 355–356.
    • (2001) Hum. Mutat. , vol.18 , Issue.4 , pp. 355-356
    • Mella, P.1    Schumacher, R.F.2    Cranston, T.3    de Saint, B.G.4    Savoldi, G.5    Notarangelo, L.D.6
  • 219
    • 84865860654 scopus 로고    scopus 로고
    • Newly described activating JAK3 mutations in T-cell acute lymphoblastic leukemia
    • Bains, T., Heinrich, M., Loriaux, M., Beadling, C., Nelson, D., Warrick, A., et al. Newly described activating JAK3 mutations in T-cell acute lymphoblastic leukemia. Leukemia 26:9 (2012), 2144–2146.
    • (2012) Leukemia , vol.26 , Issue.9 , pp. 2144-2146
    • Bains, T.1    Heinrich, M.2    Loriaux, M.3    Beadling, C.4    Nelson, D.5    Warrick, A.6
  • 220
    • 84948452018 scopus 로고    scopus 로고
    • Distinct acute lymphoblastic leukemia (ALL)-associated janus kinase 3 (JAK3) mutants exhibit different cytokine-receptor requirements and JAK inhibitor specificities
    • Losdyck, E., Hornakova, T., Springuel, L., Degryse, S., Gielen, O., Cools, J., et al. Distinct acute lymphoblastic leukemia (ALL)-associated janus kinase 3 (JAK3) mutants exhibit different cytokine-receptor requirements and JAK inhibitor specificities. J. Biol. Chem. 290:48 (2015), 29022–29034.
    • (2015) J. Biol. Chem. , vol.290 , Issue.48 , pp. 29022-29034
    • Losdyck, E.1    Hornakova, T.2    Springuel, L.3    Degryse, S.4    Gielen, O.5    Cools, J.6
  • 221
    • 34249791783 scopus 로고    scopus 로고
    • A novel mutation of intron 22 in janus kinase 3–deficient severe combined immunodeficiency
    • Mjaanes, C.M., Hendershot, R.W., Quinones, R.R., Gelfand, E.W., A novel mutation of intron 22 in janus kinase 3–deficient severe combined immunodeficiency. J. Allergy Clin. Immunol. 119:6 (2007), 1542–1545.
    • (2007) J. Allergy Clin. Immunol. , vol.119 , Issue.6 , pp. 1542-1545
    • Mjaanes, C.M.1    Hendershot, R.W.2    Quinones, R.R.3    Gelfand, E.W.4
  • 222
    • 84881020319 scopus 로고    scopus 로고
    • Exome sequencing identifies secondary mutations of SETBP1 and JAK3 in juvenile myelomonocytic leukemia
    • Sakaguchi, H., Okuno, Y., Muramatsu, H., Yoshida, K., Shiraishi, Y., Takahashi, M., et al. Exome sequencing identifies secondary mutations of SETBP1 and JAK3 in juvenile myelomonocytic leukemia. Nat. Genet. 45:8 (2013), 937–941.
    • (2013) Nat. Genet. , vol.45 , Issue.8 , pp. 937-941
    • Sakaguchi, H.1    Okuno, Y.2    Muramatsu, H.3    Yoshida, K.4    Shiraishi, Y.5    Takahashi, M.6
  • 223
    • 84893803763 scopus 로고    scopus 로고
    • Recurrent JAK1 and JAK3 somatic mutations in T-cell prolymphocytic leukemia
    • Bellanger, D., Jacquemin, V., Chopin, M., Pierron, G., Bernard, O., Ghysdael, J., et al. Recurrent JAK1 and JAK3 somatic mutations in T-cell prolymphocytic leukemia. Leukemia 28:2 (2014), 417–419.
    • (2014) Leukemia , vol.28 , Issue.2 , pp. 417-419
    • Bellanger, D.1    Jacquemin, V.2    Chopin, M.3    Pierron, G.4    Bernard, O.5    Ghysdael, J.6
  • 224
    • 0003544659 scopus 로고    scopus 로고
    • Primary Immunodeficiency Diseases: A Molecular and Cellular Approach
    • OUP USA
    • Ochs, H.D., Smith, C.I.E., Puck, J.M., Primary Immunodeficiency Diseases: A Molecular and Cellular Approach. 2013, OUP, USA.
    • (2013)
    • Ochs, H.D.1    Smith, C.I.E.2    Puck, J.M.3
  • 225
    • 84969760884 scopus 로고    scopus 로고
    • Mutations of SETBP1 and JAK3 in juvenile myelomonocytic leukemia: A report from the italian AIEOP study group
    • Bresolin, S., De Filippi, P., Vendemini, F., D'Alia, M., Zecca, M., Meyer, L.H., et al. Mutations of SETBP1 and JAK3 in juvenile myelomonocytic leukemia: A report from the italian AIEOP study group. Oncotarget 7:20 (2016), 28914–28919.
    • (2016) Oncotarget , vol.7 , Issue.20 , pp. 28914-28919
    • Bresolin, S.1    De Filippi, P.2    Vendemini, F.3    D'Alia, M.4    Zecca, M.5    Meyer, L.H.6
  • 226
    • 84899734963 scopus 로고    scopus 로고
    • Comprehensive analysis of transcriptome variation uncovers known and novel driver events in T-cell acute lymphoblastic leukemia
    • Atak, Z.K., Gianfelici, V., Hulselmans, G., De Keersmaecker, K., Devasia, A.G., Geerdens, E., et al. Comprehensive analysis of transcriptome variation uncovers known and novel driver events in T-cell acute lymphoblastic leukemia. PLoS Genet, 9(12), 2013, e1003997.
    • (2013) PLoS Genet , vol.9 , Issue.12 , pp. e1003997
    • Atak, Z.K.1    Gianfelici, V.2    Hulselmans, G.3    De Keersmaecker, K.4    Devasia, A.G.5    Geerdens, E.6
  • 227
    • 84866053994 scopus 로고    scopus 로고
    • Exome sequencing identifies a novel multiple sclerosis susceptibility variant in the TYK2 gene
    • Dyment, D.A., Cader, M.Z., Chao, M.J., Lincoln, M.R., Morrison, K.M., Disanto, G., et al. Exome sequencing identifies a novel multiple sclerosis susceptibility variant in the TYK2 gene. Neurology 79:5 (2012), 406–411.
    • (2012) Neurology , vol.79 , Issue.5 , pp. 406-411
    • Dyment, D.A.1    Cader, M.Z.2    Chao, M.J.3    Lincoln, M.R.4    Morrison, K.M.5    Disanto, G.6
  • 228
    • 47149087181 scopus 로고    scopus 로고
    • Somatic mutations and germline sequence variants in the expressed tyrosine kinase genes of patients with de novo acute myeloid leukemia
    • Tomasson, M.H., Xiang, Z., Walgren, R., Zhao, Y., Kasai, Y., Miner, T., et al. Somatic mutations and germline sequence variants in the expressed tyrosine kinase genes of patients with de novo acute myeloid leukemia. Blood 111:9 (2008), 4797–4808.
    • (2008) Blood , vol.111 , Issue.9 , pp. 4797-4808
    • Tomasson, M.H.1    Xiang, Z.2    Walgren, R.3    Zhao, Y.4    Kasai, Y.5    Miner, T.6
  • 229
    • 84949087898 scopus 로고    scopus 로고
    • Mutations in the TLR3 signaling pathway and beyond in adult patients with herpes simplex encephalitis
    • Mørk, N., Kofod-Olsen, E., Sørensen, K., Bach, E., Ørntoft, T., Østergaard, L., et al. Mutations in the TLR3 signaling pathway and beyond in adult patients with herpes simplex encephalitis. Genes Immun. 16:8 (2015), 552–566.
    • (2015) Genes Immun. , vol.16 , Issue.8 , pp. 552-566
    • Mørk, N.1    Kofod-Olsen, E.2    Sørensen, K.3    Bach, E.4    Ørntoft, T.5    Østergaard, L.6
  • 231
    • 84928920020 scopus 로고    scopus 로고
    • TYK2 protein-coding variants protect against rheumatoid arthritis and autoimmunity, with no evidence of major pleiotropic effects on non-autoimmune complex traits
    • Diogo, D., Bastarache, L., Liao, K.P., Graham, R.R., Fulton, R.S., Greenberg, J.D., et al. TYK2 protein-coding variants protect against rheumatoid arthritis and autoimmunity, with no evidence of major pleiotropic effects on non-autoimmune complex traits. PLoS One, 10(4), 2015, e1022271.
    • (2015) PLoS One , vol.10 , Issue.4 , pp. e1022271
    • Diogo, D.1    Bastarache, L.2    Liao, K.P.3    Graham, R.R.4    Fulton, R.S.5    Greenberg, J.D.6
  • 232
    • 84874260872 scopus 로고    scopus 로고
    • Two rare disease-associated Tyk2 variants are catalytically impaired but signaling competent
    • Li, Z., Gakovic, M., Ragimbeau, J., Eloranta, M., Rönnblom, L., Michel, F., et al. Two rare disease-associated Tyk2 variants are catalytically impaired but signaling competent. J. Immunol. 190:5 (2013), 2335–2344.
    • (2013) J. Immunol. , vol.190 , Issue.5 , pp. 2335-2344
    • Li, Z.1    Gakovic, M.2    Ragimbeau, J.3    Eloranta, M.4    Rönnblom, L.5    Michel, F.6
  • 233
    • 85005990043 scopus 로고    scopus 로고
    • Clinical genomic profiling identifies TYK2 mutation and overexpression in patients with neurofibromatosis type 1-associated malignant peripheral nerve sheath tumors
    • Hirbe, A.C., Kaushal, M., Sharma, M.K., Dahiya, S., Pekmezci, M., Perry, A., et al. Clinical genomic profiling identifies TYK2 mutation and overexpression in patients with neurofibromatosis type 1-associated malignant peripheral nerve sheath tumors. Cancer 123:7 (2017), 1194–1201.
    • (2017) Cancer , vol.123 , Issue.7 , pp. 1194-1201
    • Hirbe, A.C.1    Kaushal, M.2    Sharma, M.K.3    Dahiya, S.4    Pekmezci, M.5    Perry, A.6
  • 235
    • 36849065315 scopus 로고    scopus 로고
    • Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer
    • Rikova, K., Guo, A., Zeng, Q., Possemato, A., Yu, J., Haack, H., et al. Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell 131:6 (2007), 1190–1203.
    • (2007) Cell , vol.131 , Issue.6 , pp. 1190-1203
    • Rikova, K.1    Guo, A.2    Zeng, Q.3    Possemato, A.4    Yu, J.5    Haack, H.6
  • 236
    • 84865709926 scopus 로고    scopus 로고
    • Tyrosine 201 is required for constitutive activation of JAK2V617F and efficient induction of myeloproliferative disease in mice
    • Yan, D., Hutchison, R.E., Mohi, G., Tyrosine 201 is required for constitutive activation of JAK2V617F and efficient induction of myeloproliferative disease in mice. Blood 120:9 (2012), 1888–1898.
    • (2012) Blood , vol.120 , Issue.9 , pp. 1888-1898
    • Yan, D.1    Hutchison, R.E.2    Mohi, G.3
  • 237
    • 33846241616 scopus 로고    scopus 로고
    • The N-terminal SH2 domain of the tyrosine phosphatase, SHP-2, is essential for Jak2-dependent signaling via the angiotensin II type AT1 receptor
    • Godeny, M.D., Sayyah, J., VonDerLinden, D., Johns, M., Ostrov, D.A., Caldwell-Busby, J., et al. The N-terminal SH2 domain of the tyrosine phosphatase, SHP-2, is essential for Jak2-dependent signaling via the angiotensin II type AT1 receptor. Cell. Signal. 19:3 (2007), 600–609.
    • (2007) Cell. Signal. , vol.19 , Issue.3 , pp. 600-609
    • Godeny, M.D.1    Sayyah, J.2    VonDerLinden, D.3    Johns, M.4    Ostrov, D.A.5    Caldwell-Busby, J.6
  • 239
    • 2442659839 scopus 로고    scopus 로고
    • Tyrosine 813 is a site of JAK2 autophosphorylation critical for activation of JAK2 by SH2-B beta
    • Kurzer, J.H., Argetsinger, L.S., Zhou, Y.J., Kouadio, J.L., O'Shea, J.J., Carter-Su, C., Tyrosine 813 is a site of JAK2 autophosphorylation critical for activation of JAK2 by SH2-B beta. Mol. Cell. Biol. 24:10 (2004), 4557–4570.
    • (2004) Mol. Cell. Biol. , vol.24 , Issue.10 , pp. 4557-4570
    • Kurzer, J.H.1    Argetsinger, L.S.2    Zhou, Y.J.3    Kouadio, J.L.4    O'Shea, J.J.5    Carter-Su, C.6
  • 240
    • 77954845356 scopus 로고    scopus 로고
    • Tyrosines 868, 966, and 972 in the kinase domain of JAK2 are autophosphorylated and required for maximal JAK2 kinase activity
    • Argetsinger, L.S., Stuckey, J.A., Robertson, S.A., Koleva, R.I., Cline, J.M., Marto, J.A., et al. Tyrosines 868, 966, and 972 in the kinase domain of JAK2 are autophosphorylated and required for maximal JAK2 kinase activity. Mol. Endocrinol. 24:5 (2010), 1062–1076.
    • (2010) Mol. Endocrinol. , vol.24 , Issue.5 , pp. 1062-1076
    • Argetsinger, L.S.1    Stuckey, J.A.2    Robertson, S.A.3    Koleva, R.I.4    Cline, J.M.5    Marto, J.A.6
  • 241
    • 52149086993 scopus 로고    scopus 로고
    • Negative regulation of Jak2 by its auto-phosphorylation at tyrosine 913 via the epo signaling pathway
    • Funakoshi-Tago, M., Tago, K., Kasahara, T., Parganas, E., Ihle, J.N., Negative regulation of Jak2 by its auto-phosphorylation at tyrosine 913 via the epo signaling pathway. Cell. Signal. 20:11 (2008), 1995–2001.
    • (2008) Cell. Signal. , vol.20 , Issue.11 , pp. 1995-2001
    • Funakoshi-Tago, M.1    Tago, K.2    Kasahara, T.3    Parganas, E.4    Ihle, J.N.5
  • 242
    • 52949090018 scopus 로고    scopus 로고
    • SOCS regulation of the JAK/STAT signalling pathway
    • Croker, B.A., Kiu, H., Nicholson, S.E., SOCS regulation of the JAK/STAT signalling pathway. Semin. Cell Dev. Biol. 19:4 (2008), 414–422.
    • (2008) Semin. Cell Dev. Biol. , vol.19 , Issue.4 , pp. 414-422
    • Croker, B.A.1    Kiu, H.2    Nicholson, S.E.3
  • 243
    • 76349083132 scopus 로고    scopus 로고
    • Large, rare chromosomal deletions associated with severe early-onset obesity
    • Bochukova, E.G., Huang, N., Keogh, J., Henning, E., Purmann, C., Blaszczyk, K., et al. Large, rare chromosomal deletions associated with severe early-onset obesity. Nature 463:7281 (2010), 666–670.
    • (2010) Nature , vol.463 , Issue.7281 , pp. 666-670
    • Bochukova, E.G.1    Huang, N.2    Keogh, J.3    Henning, E.4    Purmann, C.5    Blaszczyk, K.6
  • 244
    • 76249116215 scopus 로고    scopus 로고
    • A new highly penetrant form of obesity due to deletions on chromosome 16p11. 2
    • Walters, R., Jacquemont, S., Valsesia, A., De Smith, A., Martinet, D., Andersson, J., et al. A new highly penetrant form of obesity due to deletions on chromosome 16p11. 2. Nature 463:7281 (2010), 671–675.
    • (2010) Nature , vol.463 , Issue.7281 , pp. 671-675
    • Walters, R.1    Jacquemont, S.2    Valsesia, A.3    De Smith, A.4    Martinet, D.5    Andersson, J.6
  • 245
    • 84871570099 scopus 로고    scopus 로고
    • Mutation screen in the GWAS derived obesity gene SH2B1 including functional analyses of detected variants
    • Volckmar, A., Bolze, F., Jarick, I., Knoll, N., Scherag, A., Reinehr, T., et al. Mutation screen in the GWAS derived obesity gene SH2B1 including functional analyses of detected variants. BMC Med. Genomics, 5(1), 2012, 65.
    • (2012) BMC Med. Genomics , vol.5 , Issue.1 , pp. 65
    • Volckmar, A.1    Bolze, F.2    Jarick, I.3    Knoll, N.4    Scherag, A.5    Reinehr, T.6
  • 246
    • 0027215519 scopus 로고
    • Truncated erythropoietin receptor causes dominantly inherited benign human erythrocytosis
    • de la Chapelle, A., Traskelin, A.L., Juvonen, E., Truncated erythropoietin receptor causes dominantly inherited benign human erythrocytosis. Proc. Natl. Acad. Sci. U. S. A. 90:10 (1993), 4495–4499.
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , Issue.10 , pp. 4495-4499
    • de la Chapelle, A.1    Traskelin, A.L.2    Juvonen, E.3
  • 247
    • 84958647271 scopus 로고    scopus 로고
    • Truncating erythropoietin receptor rearrangements in acute lymphoblastic leukemia
    • Iacobucci, I., Li, Y., Roberts, K.G., Dobson, S.M., Kim, J.C., Payne-Turner, D., et al. Truncating erythropoietin receptor rearrangements in acute lymphoblastic leukemia. Cancer Cell 29:2 (2016), 186–200.
    • (2016) Cancer Cell , vol.29 , Issue.2 , pp. 186-200
    • Iacobucci, I.1    Li, Y.2    Roberts, K.G.3    Dobson, S.M.4    Kim, J.C.5    Payne-Turner, D.6
  • 248
    • 77952887619 scopus 로고    scopus 로고
    • Deletion of the protein tyrosine phosphatase gene PTPN2 in T-cell acute lymphoblastic leukemia
    • Kleppe, M., Lahortiga, I., El Chaar, T., De Keersmaecker, K., Mentens, N., Graux, C., et al. Deletion of the protein tyrosine phosphatase gene PTPN2 in T-cell acute lymphoblastic leukemia. Nat. Genet. 42:6 (2010), 530–535.
    • (2010) Nat. Genet. , vol.42 , Issue.6 , pp. 530-535
    • Kleppe, M.1    Lahortiga, I.2    El Chaar, T.3    De Keersmaecker, K.4    Mentens, N.5    Graux, C.6
  • 249
    • 84861070995 scopus 로고    scopus 로고
    • Mutation of the receptor tyrosine phosphatase PTPRC (CD45) in T-cell acute lymphoblastic leukemia
    • Porcu, M., Kleppe, M., Gianfelici, V., Geerdens, E., De Keersmaecker, K., Tartaglia, M., et al. Mutation of the receptor tyrosine phosphatase PTPRC (CD45) in T-cell acute lymphoblastic leukemia. Blood 119:19 (2012), 4476–4479.
    • (2012) Blood , vol.119 , Issue.19 , pp. 4476-4479
    • Porcu, M.1    Kleppe, M.2    Gianfelici, V.3    Geerdens, E.4    De Keersmaecker, K.5    Tartaglia, M.6
  • 250
    • 18344385476 scopus 로고    scopus 로고
    • Mutations in PTPN11, encoding the protein tyrosine phosphatase SHP-2, cause noonan syndrome
    • Tartaglia, M., Mehler, E.L., Goldberg, R., Zampino, G., Brunner, H.G., Kremer, H., et al. Mutations in PTPN11, encoding the protein tyrosine phosphatase SHP-2, cause noonan syndrome. Nat. Genet., 29(4), 2001.
    • (2001) Nat. Genet. , vol.29 , Issue.4
    • Tartaglia, M.1    Mehler, E.L.2    Goldberg, R.3    Zampino, G.4    Brunner, H.G.5    Kremer, H.6
  • 251
    • 10844290923 scopus 로고    scopus 로고
    • Activating mutations of the noonan syndrome-associated SHP2/PTPN11 gene in human solid tumors and adult acute myelogenous leukemia
    • Bentires-Alj, M., Paez, J.G., David, F.S., Keilhack, H., Halmos, B., Naoki, K., et al. Activating mutations of the noonan syndrome-associated SHP2/PTPN11 gene in human solid tumors and adult acute myelogenous leukemia. Cancer Res. 64:24 (2004), 8816–8820.
    • (2004) Cancer Res. , vol.64 , Issue.24 , pp. 8816-8820
    • Bentires-Alj, M.1    Paez, J.G.2    David, F.S.3    Keilhack, H.4    Halmos, B.5    Naoki, K.6
  • 252
    • 2542502506 scopus 로고    scopus 로고
    • Familial essential thrombocythemia associated with a dominant-positive activating mutation of the c-MPL gene, which encodes for the receptor for thrombopoietin
    • Ding, J., Komatsu, H., Wakita, A., Kato-Uranishi, M., Ito, M., Satoh, A., et al. Familial essential thrombocythemia associated with a dominant-positive activating mutation of the c-MPL gene, which encodes for the receptor for thrombopoietin. Blood 103:11 (2004), 4198–4200.
    • (2004) Blood , vol.103 , Issue.11 , pp. 4198-4200
    • Ding, J.1    Komatsu, H.2    Wakita, A.3    Kato-Uranishi, M.4    Ito, M.5    Satoh, A.6
  • 253
    • 33750534561 scopus 로고    scopus 로고
    • MPL515 mutations in myeloproliferative and other myeloid disorders: A study of 1182 patients
    • Pardanani, A.D., Levine, R.L., Lasho, T., Pikman, Y., Mesa, R.A., Wadleigh, M., et al. MPL515 mutations in myeloproliferative and other myeloid disorders: A study of 1182 patients. Blood 108:10 (2006), 3472–3476.
    • (2006) Blood , vol.108 , Issue.10 , pp. 3472-3476
    • Pardanani, A.D.1    Levine, R.L.2    Lasho, T.3    Pikman, Y.4    Mesa, R.A.5    Wadleigh, M.6
  • 254
    • 80053385665 scopus 로고    scopus 로고
    • Oncogenic IL7R gain-of-function mutations in childhood T-cell acute lymphoblastic leukemia
    • Zenatti, P.P., Ribeiro, D., Li, W., Zuurbier, L., Silva, M.C., Paganin, M., et al. Oncogenic IL7R gain-of-function mutations in childhood T-cell acute lymphoblastic leukemia. Nat. Genet. 43:10 (2011), 932–939.
    • (2011) Nat. Genet. , vol.43 , Issue.10 , pp. 932-939
    • Zenatti, P.P.1    Ribeiro, D.2    Li, W.3    Zuurbier, L.4    Silva, M.C.5    Paganin, M.6
  • 255
    • 84938747577 scopus 로고    scopus 로고
    • JAK kinase inhibitors for the treatment of acute lymphoblastic leukemia
    • Degryse, S., Cools, J., JAK kinase inhibitors for the treatment of acute lymphoblastic leukemia. J. Hematol. Oncol., 8(1), 2015, 91.
    • (2015) J. Hematol. Oncol. , vol.8 , Issue.1 , pp. 91
    • Degryse, S.1    Cools, J.2
  • 256
    • 84902589906 scopus 로고    scopus 로고
    • From janus kinase 2 to calreticulin: The clinically relevant genomic landscape of myeloproliferative neoplasms
    • Cazzola, M., Kralovics, R., From janus kinase 2 to calreticulin: The clinically relevant genomic landscape of myeloproliferative neoplasms. Blood 123:24 (2014), 3714–3719.
    • (2014) Blood , vol.123 , Issue.24 , pp. 3714-3719
    • Cazzola, M.1    Kralovics, R.2
  • 257
    • 85030155677 scopus 로고    scopus 로고
    • Novel molecular mechanism of cellular transformation by a mutant molecular chaperone in myeloproliferative neoplasms
    • Araki, M., Komatsu, N., Novel molecular mechanism of cellular transformation by a mutant molecular chaperone in myeloproliferative neoplasms. Cancer Sci. 108:10 (2017), 1907–1912.
    • (2017) Cancer Sci. , vol.108 , Issue.10 , pp. 1907-1912
    • Araki, M.1    Komatsu, N.2


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