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Volumn 71, Issue 6, 2006, Pages 713-721

JAK/STAT signal transduction: Regulators and implication in hematological malignancies

Author keywords

JAK STAT pathway; Oncogenesis; Regulation of STAT activity; Signal transduction

Indexed keywords

CD45 ANTIGEN; CYTOKINE; CYTOKINE RECEPTOR; ESTERASE; GROWTH FACTOR; HORMONE; HYBRID PROTEIN; JANUS KINASE; JANUS KINASE 2; PROTEIN; PROTEIN INHIBITOR OF ACTIVATED STAT; PROTEIN TYROSINE PHOSPHATASE; PROTEIN TYROSINE PHOSPHATASE 1B; PROTEIN TYROSINE PHOSPHATASE SHP; STAT PROTEIN; SUPPRESSOR OF CYTOKINE SIGNALING; TRANSCRIPTION FACTOR; TYROSINE PHOSPHATASE; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG;

EID: 32144453842     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bcp.2005.12.017     Document Type: Note
Times cited : (220)

References (103)
  • 1
    • 0031919849 scopus 로고    scopus 로고
    • Jaks and STATs: Biological implications
    • W.J. Leonard, and J.J. O'Shea Jaks and STATs: biological implications Annu Rev Immunol 16 1998 293 322
    • (1998) Annu Rev Immunol , vol.16 , pp. 293-322
    • Leonard, W.J.1    O'Shea, J.J.2
  • 2
    • 0034012330 scopus 로고    scopus 로고
    • Regulation of the Jak2 tyrosine kinase by its pseudokinase domain
    • P. Saharinen, K. Takaluoma, and O. Silvennoinen Regulation of the Jak2 tyrosine kinase by its pseudokinase domain Mol Cell Biol 20 2000 3387 3395
    • (2000) Mol Cell Biol , vol.20 , pp. 3387-3395
    • Saharinen, P.1    Takaluoma, K.2    Silvennoinen, O.3
  • 3
    • 0032425542 scopus 로고    scopus 로고
    • Janus kinases and focal adhesion kinases play in the 4.1 band: A superfamily of band 4.1 domains important for cell structure and signal transduction
    • J.A. Girault, G. Labesse, J.P. Mornon, and I. Callebaut Janus kinases and focal adhesion kinases play in the 4.1 band: a superfamily of band 4.1 domains important for cell structure and signal transduction Mol Med 4 1998 751 769
    • (1998) Mol Med , vol.4 , pp. 751-769
    • Girault, J.A.1    Labesse, G.2    Mornon, J.P.3    Callebaut, I.4
  • 4
    • 0034638632 scopus 로고    scopus 로고
    • Computational and functional analysis of the putative SH2 domain in Janus Kinases
    • D. Kampa, and J. Burnside Computational and functional analysis of the putative SH2 domain in Janus Kinases Biochem Biophys Res Commun 278 2000 175 182
    • (2000) Biochem Biophys Res Commun , vol.278 , pp. 175-182
    • Kampa, D.1    Burnside, J.2
  • 5
    • 15444339209 scopus 로고    scopus 로고
    • A TEL-JAK2 fusion protein with constitutive kinase activity in human leukaemia
    • V. Lacronique, A. Boureux, V.D. Valle, H. Poirel, C.T. Quang, and M. Mauchauffe A TEL-JAK2 fusion protein with constitutive kinase activity in human leukaemia Science 278 1997 1309 1312
    • (1997) Science , vol.278 , pp. 1309-1312
    • Lacronique, V.1    Boureux, A.2    Valle, V.D.3    Poirel, H.4    Quang, C.T.5    Mauchauffe, M.6
  • 6
    • 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
    • P. Peeters, S.D. Raynaud, J. Cools, I. Wlodarska, J. Grosgeorge, and P. Philip 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 1997 2535 2540
    • (1997) Blood , vol.90 , pp. 2535-2540
    • Peeters, P.1    Raynaud, S.D.2    Cools, J.3    Wlodarska, I.4    Grosgeorge, J.5    Philip, P.6
  • 7
    • 25844469587 scopus 로고    scopus 로고
    • A BCR-JAK2 fusion gene as the result of a t(9;22)(p24;q11.2) translocation in a patient with a clinically typical chronic myeloid leukemia
    • F. Griesinger, H. Hennig, F. Hillmer, M. Podleschny, R. Steffens, and A. Pies A BCR-JAK2 fusion gene as the result of a t(9;22)(p24;q11.2) translocation in a patient with a clinically typical chronic myeloid leukemia Genes Chromosomes Cancer 44 2005 329 333
    • (2005) Genes Chromosomes Cancer , vol.44 , pp. 329-333
    • Griesinger, F.1    Hennig, H.2    Hillmer, F.3    Podleschny, M.4    Steffens, R.5    Pies, A.6
  • 9
    • 0027422977 scopus 로고
    • A coiled-coil oligomerization domain of Bcr is essential for the transforming function of Bcr-Abl oncoproteins
    • J.R. McWhirter, D.L. Galasso, and J.Y. Wang A coiled-coil oligomerization domain of Bcr is essential for the transforming function of Bcr-Abl oncoproteins Mol Cell Biol 13 1993 7587 7595
    • (1993) Mol Cell Biol , vol.13 , pp. 7587-7595
    • McWhirter, J.R.1    Galasso, D.L.2    Wang, J.Y.3
  • 10
    • 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
    • A. Reiter, C. Walz, A. Watmore, C. Schoch, I. Blau, and B. Schlegelberger The t(8;9)(p22;p24) is a recurrent abnormality in chronic and acute leukemia that fuses PCM1 to JAK2 Cancer Res 65 2005 2662 2667
    • (2005) Cancer Res , vol.65 , pp. 2662-2667
    • Reiter, A.1    Walz, C.2    Watmore, A.3    Schoch, C.4    Blau, I.5    Schlegelberger, B.6
  • 11
    • 27944481825 scopus 로고    scopus 로고
    • The t(8;9)(p22;p24) translocation in atypical chronic myeloid leukaemia yields a new PCM1-JAK2 fusion gene
    • M. Bousquet, C. Quelen, V. De Mas, E. Duchayne, B. Roquefeuil, and G. Delsol The t(8;9)(p22;p24) translocation in atypical chronic myeloid leukaemia yields a new PCM1-JAK2 fusion gene Oncogene 24 2005 7248 7252
    • (2005) Oncogene , vol.24 , pp. 7248-7252
    • Bousquet, M.1    Quelen, C.2    De Mas, V.3    Duchayne, E.4    Roquefeuil, B.5    Delsol, G.6
  • 12
    • 20144363192 scopus 로고    scopus 로고
    • Acquired mutation of the tyrosine kinase JAK2 in human myeloproliferative disorders
    • E.J. Baxter, L.M. Scott, P.J. Campbell, C. East, N. Fourouclas, and S. Swanton Acquired mutation of the tyrosine kinase JAK2 in human myeloproliferative disorders Lancet 365 2005 1054 1061
    • (2005) Lancet , vol.365 , pp. 1054-1061
    • Baxter, E.J.1    Scott, L.M.2    Campbell, P.J.3    East, C.4    Fourouclas, N.5    Swanton, S.6
  • 13
    • 17844383458 scopus 로고    scopus 로고
    • A unique clonal JAK2 mutation leading to constitutive signalling causes polycythaemia vera
    • C. James, V. Ugo, J.P. Le Couedic, J. Staerk, F. Delhommeau, and C. Lacout A unique clonal JAK2 mutation leading to constitutive signalling causes polycythaemia vera Nature 434 2005 1144 1148
    • (2005) Nature , vol.434 , pp. 1144-1148
    • James, C.1    Ugo, V.2    Le Couedic, J.P.3    Staerk, J.4    Delhommeau, F.5    Lacout, C.6
  • 14
    • 21344440357 scopus 로고    scopus 로고
    • The JAK2 V617F activating tyrosine kinase mutation is an infrequent event in both "atypical" myeloproliferative disorders and the myelodysplastic syndrome
    • D.P. Steensma, G.W. Dewald, T.L. Lasho, H.L. Powell, R.F. McClure, and R.L. Levine The JAK2 V617F activating tyrosine kinase mutation is an infrequent event in both "atypical" myeloproliferative disorders and the myelodysplastic syndrome Blood 106 2005 1207 1209
    • (2005) Blood , vol.106 , pp. 1207-1209
    • Steensma, D.P.1    Dewald, G.W.2    Lasho, T.L.3    Powell, H.L.4    McClure, R.F.5    Levine, R.L.6
  • 16
    • 20244369569 scopus 로고    scopus 로고
    • Activating mutation in the tyrosine kinase JAK2 in polycythemia vera, essential thrombocythemia, and myeloid metaplasia with myelofibrosis
    • R.L. Levine, M. Wadleigh, J. Cools, B.L. Ebert, G. Wernig, and B.J. Huntly Activating mutation in the tyrosine kinase JAK2 in polycythemia vera, essential thrombocythemia, and myeloid metaplasia with myelofibrosis Cancer Cell 7 2005 387 397
    • (2005) Cancer Cell , vol.7 , pp. 387-397
    • Levine, R.L.1    Wadleigh, M.2    Cools, J.3    Ebert, B.L.4    Wernig, G.5    Huntly, B.J.6
  • 17
    • 20744460045 scopus 로고    scopus 로고
    • Identification of an acquired JAK2 mutation in polycythemia vera
    • R. Zhao, S. Xing, Z. Li, X. Fu, Q. Li, and S.B. Krantz Identification of an acquired JAK2 mutation in polycythemia vera J Biol Chem 280 2005 22788 22792
    • (2005) J Biol Chem , vol.280 , pp. 22788-22792
    • Zhao, R.1    Xing, S.2    Li, Z.3    Fu, X.4    Li, Q.5    Krantz, S.B.6
  • 18
    • 0037428669 scopus 로고    scopus 로고
    • Hodgkin's lymphoma cell lines are characterized by frequent aberrations on chromosomes 2p and 9p including REL and JAK2
    • S. Joos, M. Granzow, H. Holtgreve-Grez, R. Siebert, L. Harder, and J.I. Martin-Subero Hodgkin's lymphoma cell lines are characterized by frequent aberrations on chromosomes 2p and 9p including REL and JAK2 Int J Cancer 103 2003 489 495
    • (2003) Int J Cancer , vol.103 , pp. 489-495
    • Joos, S.1    Granzow, M.2    Holtgreve-Grez, H.3    Siebert, R.4    Harder, L.5    Martin-Subero, J.I.6
  • 19
    • 0030840464 scopus 로고    scopus 로고
    • STATs and gene regulation
    • J.E. Darnell Jr. STATs and gene regulation Science 277 1997 1630 1635
    • (1997) Science , vol.277 , pp. 1630-1635
    • Darnell Jr., J.E.1
  • 22
    • 0034658024 scopus 로고    scopus 로고
    • Serine phosphorylation of STATs
    • T. Decker, and P. Kovarik Serine phosphorylation of STATs Oncogene 19 2000 2628 2637
    • (2000) Oncogene , vol.19 , pp. 2628-2637
    • Decker, T.1    Kovarik, P.2
  • 23
    • 0037184052 scopus 로고    scopus 로고
    • An LXXLL motif in the transactivation domain of STAT6 mediates recruitment of NCoA-1/SRC-1
    • C.M. Litterst, and E. Pfitzner An LXXLL motif in the transactivation domain of STAT6 mediates recruitment of NCoA-1/SRC-1 J Biol Chem 277 2002 36052 36060
    • (2002) J Biol Chem , vol.277 , pp. 36052-36060
    • Litterst, C.M.1    Pfitzner, E.2
  • 24
    • 17644374227 scopus 로고    scopus 로고
    • The transcriptional co-activator protein p100 recruits histone acetyltransferase activity to STAT6 and mediates interaction between the CREB-binding protein and STAT6
    • T. Valineva, J. Yang, R. Palovuori, and O. Silvennoinen The transcriptional co-activator protein p100 recruits histone acetyltransferase activity to STAT6 and mediates interaction between the CREB-binding protein and STAT6 J Biol Chem 280 2005 14989 14996
    • (2005) J Biol Chem , vol.280 , pp. 14989-14996
    • Valineva, T.1    Yang, J.2    Palovuori, R.3    Silvennoinen, O.4
  • 25
    • 0036251154 scopus 로고    scopus 로고
    • Stat proteins and oncogenesis
    • J. Bromberg Stat proteins and oncogenesis J Clin Invest 109 2002 1139 1142
    • (2002) J Clin Invest , vol.109 , pp. 1139-1142
    • Bromberg, J.1
  • 26
    • 0032984589 scopus 로고    scopus 로고
    • Constitutive activation of Stat3 signaling confers resistance to apoptosis in human U266 myeloma cells
    • R. Catlett-Falcone, T.H. Landowski, M.M. Oshiro, J. Turkson, A. Levitzki, and R. Savino Constitutive activation of Stat3 signaling confers resistance to apoptosis in human U266 myeloma cells Immunity 10 1999 105 115
    • (1999) Immunity , vol.10 , pp. 105-115
    • Catlett-Falcone, R.1    Landowski, T.H.2    Oshiro, M.M.3    Turkson, J.4    Levitzki, A.5    Savino, R.6
  • 27
    • 2442663092 scopus 로고    scopus 로고
    • Activated signal transducer and activator of transcription (STAT) 3 localization in focal adhesions and function in ovarian cancer cell motility
    • D.L. Silver, H. Naora, J. Liu, W. Cheng, and D.J. Montell Activated signal transducer and activator of transcription (STAT) 3 localization in focal adhesions and function in ovarian cancer cell motility Cancer Res 64 2004 3550 3558
    • (2004) Cancer Res , vol.64 , pp. 3550-3558
    • Silver, D.L.1    Naora, H.2    Liu, J.3    Cheng, W.4    Montell, D.J.5
  • 28
    • 1242292306 scopus 로고    scopus 로고
    • STAT-1: A novel regulator of apoptosis
    • A. Stephanou, and D.S. Latchman STAT-1: a novel regulator of apoptosis Int J Exp Pathol 84 2003 239 244
    • (2003) Int J Exp Pathol , vol.84 , pp. 239-244
    • Stephanou, A.1    Latchman, D.S.2
  • 29
    • 0029059985 scopus 로고
    • Human protein tyrosine phosphatase 1C (PTPN6) gene structure: Alternate promoter usage and exon skipping generate multiple transcripts
    • D. Banville, R. Stocco, and S.H. Shen Human protein tyrosine phosphatase 1C (PTPN6) gene structure: alternate promoter usage and exon skipping generate multiple transcripts Genomics 27 1995 165 173
    • (1995) Genomics , vol.27 , pp. 165-173
    • Banville, D.1    Stocco, R.2    Shen, S.H.3
  • 30
    • 0345357773 scopus 로고    scopus 로고
    • Gene silencing in cancer in association with promoter hypermethylation
    • J.G. Herman, and S.B. Baylin Gene silencing in cancer in association with promoter hypermethylation N Engl J Med 349 2003 2042 2054
    • (2003) N Engl J Med , vol.349 , pp. 2042-2054
    • Herman, J.G.1    Baylin, S.B.2
  • 31
    • 0032960181 scopus 로고    scopus 로고
    • Cancer epigenetics comes of age
    • P.A. Jones, and P.W. Laird Cancer epigenetics comes of age Nat Genet 21 1999 163 167
    • (1999) Nat Genet , vol.21 , pp. 163-167
    • Jones, P.A.1    Laird, P.W.2
  • 32
    • 0037112439 scopus 로고    scopus 로고
    • Gene silencing of the tyrosine phosphatase SHP1 gene by aberrant methylation in leukemias/lymphomas
    • T. Oka, M. Ouchida, M. Koyama, Y. Ogama, S. Takada, and Y. Nakatani Gene silencing of the tyrosine phosphatase SHP1 gene by aberrant methylation in leukemias/lymphomas Cancer Res 62 2002 6390 6394
    • (2002) Cancer Res , vol.62 , pp. 6390-6394
    • Oka, T.1    Ouchida, M.2    Koyama, M.3    Ogama, Y.4    Takada, S.5    Nakatani, Y.6
  • 33
    • 18744395503 scopus 로고    scopus 로고
    • STAT3- and DNA methyltransferase 1-mediated epigenetic silencing of SHP-1 tyrosine phosphatase tumor suppressor gene in malignant T lymphocytes
    • Q. Zhang, H.Y. Wang, M. Marzec, P.N. Raghunath, T. Nagasawa, and M.A. Wasik STAT3- and DNA methyltransferase 1-mediated epigenetic silencing of SHP-1 tyrosine phosphatase tumor suppressor gene in malignant T lymphocytes Proc Natl Acad Sci USA 102 2005 6948 6953
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 6948-6953
    • Zhang, Q.1    Wang, H.Y.2    Marzec, M.3    Raghunath, P.N.4    Nagasawa, T.5    Wasik, M.A.6
  • 34
    • 2942584857 scopus 로고    scopus 로고
    • SOCS1 and SHP1 hypermethylation in multiple myeloma: Implications for epigenetic activation of the Jak/STAT pathway
    • C.S. Chim, T.K. Fung, W.C. Cheung, R. Liang, and Y.L. Kwong SOCS1 and SHP1 hypermethylation in multiple myeloma: implications for epigenetic activation of the Jak/STAT pathway Blood 103 2004 4630 4635
    • (2004) Blood , vol.103 , pp. 4630-4635
    • Chim, C.S.1    Fung, T.K.2    Cheung, W.C.3    Liang, R.4    Kwong, Y.L.5
  • 35
    • 17144366936 scopus 로고    scopus 로고
    • Aberrant methylation of the negative regulators RASSFIA SHP-1 and SOCS-1 in myelodysplastic syndromes and acute myeloid leukaemia
    • M.F. Johan, D.T. Bowen, M.E. Frew, A.C. Goodeve, and J.T. Reilly Aberrant methylation of the negative regulators RASSFIA SHP-1 and SOCS-1 in myelodysplastic syndromes and acute myeloid leukaemia Br J Haematol 129 2005 60 65
    • (2005) Br J Haematol , vol.129 , pp. 60-65
    • Johan, M.F.1    Bowen, D.T.2    Frew, M.E.3    Goodeve, A.C.4    Reilly, J.T.5
  • 36
    • 12144290834 scopus 로고    scopus 로고
    • The role of the inhibitors of interleukin-6 signal transduction SHP2 and SOCS3 for desensitization of interleukin-6 signalling
    • P. Fischer, U. Lehmann, R.M. Sobota, J. Schmitz, C. Niemand, and S. Linnemann The role of the inhibitors of interleukin-6 signal transduction SHP2 and SOCS3 for desensitization of interleukin-6 signalling Biochem J 378 2004 449 460
    • (2004) Biochem J , vol.378 , pp. 449-460
    • Fischer, P.1    Lehmann, U.2    Sobota, R.M.3    Schmitz, J.4    Niemand, C.5    Linnemann, S.6
  • 38
    • 4043056497 scopus 로고    scopus 로고
    • Mouse model of Noonan syndrome reveals cell type- and gene dosage-dependent effects of Ptpn11 mutation
    • T. Araki, M.G. Mohi, F.A. Ismat, R.T. Bronson, I.R. Williams, and J.L. Kutok Mouse model of Noonan syndrome reveals cell type- and gene dosage-dependent effects of Ptpn11 mutation Nat Med 10 2004 849 857
    • (2004) Nat Med , vol.10 , pp. 849-857
    • Araki, T.1    Mohi, M.G.2    Ismat, F.A.3    Bronson, R.T.4    Williams, I.R.5    Kutok, J.L.6
  • 39
    • 0038278866 scopus 로고    scopus 로고
    • Somatic mutations in PTPN11 in juvenile myelomonocytic leukemia, myelodysplastic syndromes and acute myeloid leukemia
    • M. Tartaglia, C.M. Niemeyer, A. Fragale, X. Song, J. Buechner, and A. Jung Somatic mutations in PTPN11 in juvenile myelomonocytic leukemia, myelodysplastic syndromes and acute myeloid leukemia Nat Genet 34 2003 148 150
    • (2003) Nat Genet , vol.34 , pp. 148-150
    • Tartaglia, M.1    Niemeyer, C.M.2    Fragale, A.3    Song, X.4    Buechner, J.5    Jung, A.6
  • 40
    • 0028346560 scopus 로고
    • CD45: An emerging role as a protein tyrosine phosphatase required for lymphocyte activation and development
    • I.S. Trowbridge, and M.L. Thomas CD45: an emerging role as a protein tyrosine phosphatase required for lymphocyte activation and development Annu Rev Immunol 12 1994 85 116
    • (1994) Annu Rev Immunol , vol.12 , pp. 85-116
    • Trowbridge, I.S.1    Thomas, M.L.2
  • 41
    • 0038815306 scopus 로고    scopus 로고
    • CD45: A critical regulator of signaling thresholds in immune cells
    • M.L. Hermiston, Z. Xu, and A. Weiss CD45: a critical regulator of signaling thresholds in immune cells Annu Rev Immunol 21 2003 107 137
    • (2003) Annu Rev Immunol , vol.21 , pp. 107-137
    • Hermiston, M.L.1    Xu, Z.2    Weiss, A.3
  • 42
    • 0026584285 scopus 로고
    • The nontransmembrane tyrosine phosphatase PTP-1B localizes to the endoplasmic reticulum via its 35 amino acid C-terminal sequence
    • J.V. Frangioni, P.H. Beahm, V. Shifrin, C.A. Jost, and B.G. Neel The nontransmembrane tyrosine phosphatase PTP-1B localizes to the endoplasmic reticulum via its 35 amino acid C-terminal sequence Cell 68 1992 545 560
    • (1992) Cell , vol.68 , pp. 545-560
    • Frangioni, J.V.1    Beahm, P.H.2    Shifrin, V.3    Jost, C.A.4    Neel, B.G.5
  • 44
    • 0037022564 scopus 로고    scopus 로고
    • Members of the PIAS family act as SUMO ligases for c-Jun and p53 and repress p53 activity
    • D. Schmidt, and S. Muller Members of the PIAS family act as SUMO ligases for c-Jun and p53 and repress p53 activity Proc Natl Acad Sci USA 99 2002 2872 2877
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 2872-2877
    • Schmidt, D.1    Muller, S.2
  • 45
    • 23444461182 scopus 로고    scopus 로고
    • Regulation of gene-activation pathways by PIAS proteins in the immune system
    • K. Shuai, and B. Liu Regulation of gene-activation pathways by PIAS proteins in the immune system Nat Rev Immunol 5 2005 593 605
    • (2005) Nat Rev Immunol , vol.5 , pp. 593-605
    • Shuai, K.1    Liu, B.2
  • 47
    • 0030725378 scopus 로고    scopus 로고
    • Specific inhibition of Stat3 signal transduction by PIAS3
    • C.D. Chung, J. Liao, B. Liu, X. Rao, P. Jay, and P. Perte Specific inhibition of Stat3 signal transduction by PIAS3 Science 278 1997 1803 1805
    • (1997) Science , vol.278 , pp. 1803-1805
    • Chung, C.D.1    Liao, J.2    Liu, B.3    Rao, X.4    Jay, P.5    Perte, P.6
  • 48
    • 0035853098 scopus 로고    scopus 로고
    • A transcriptional corepressor of Stat1 with an essential LXXLL signature motif
    • B. Liu, M. Gross, J. ten Hoeve, and K. Shuai A transcriptional corepressor of Stat1 with an essential LXXLL signature motif Proc Natl Acad Sci USA 98 2001 3203 3207
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 3203-3207
    • Liu, B.1    Gross, M.2    Ten Hoeve, J.3    Shuai, K.4
  • 49
    • 0037677203 scopus 로고    scopus 로고
    • PIASx is a transcriptional co-repressor of signal transducer and activator of transcription 4
    • T. Aurora, B. Liu, H. He, J. Kim, T.L. Murphy, and K.M. Murphy PIASx is a transcriptional co-repressor of signal transducer and activator of transcription 4 J Biol Chem 278 2003 21327 21330
    • (2003) J Biol Chem , vol.278 , pp. 21327-21330
    • Aurora, T.1    Liu, B.2    He, H.3    Kim, J.4    Murphy, T.L.5    Murphy, K.M.6
  • 50
    • 4644367257 scopus 로고    scopus 로고
    • PIAS1 selectively inhibits interferon-inducible genes and is important in innate immunity
    • B. Liu, S. Mink, K.A. Wong, N. Stein, C. German, and P.W. Dempsey PIAS1 selectively inhibits interferon-inducible genes and is important in innate immunity Nat Immunol 5 2004 891 898
    • (2004) Nat Immunol , vol.5 , pp. 891-898
    • Liu, B.1    Mink, S.2    Wong, K.A.3    Stein, N.4    German, C.5    Dempsey, P.W.6
  • 52
    • 0036134884 scopus 로고    scopus 로고
    • Multilevel dysregulation of STAT3 activation in anaplastic lymphoma kinase-positive T/null-cell lymphoma
    • Q. Zhang, P.N. Raghunath, L. Xue, M. Majewski, D.F. Carpentieri, and N. Odum Multilevel dysregulation of STAT3 activation in anaplastic lymphoma kinase-positive T/null-cell lymphoma J Immunol 168 2002 466 474
    • (2002) J Immunol , vol.168 , pp. 466-474
    • Zhang, Q.1    Raghunath, P.N.2    Xue, L.3    Majewski, M.4    Carpentieri, D.F.5    Odum, N.6
  • 53
    • 0142215552 scopus 로고    scopus 로고
    • DNA microarray analysis of stage progression mechanism in myelodysplastic syndrome
    • M. Ueda, J. Ota, Y. Yamashita, Y.L. Choi, R. Ohki, and T. Wada DNA microarray analysis of stage progression mechanism in myelodysplastic syndrome Br J Haematol 123 2003 288 296
    • (2003) Br J Haematol , vol.123 , pp. 288-296
    • Ueda, M.1    Ota, J.2    Yamashita, Y.3    Choi, Y.L.4    Ohki, R.5    Wada, T.6
  • 54
    • 0029014206 scopus 로고
    • A novel cytokine-inducible gene CIS encodes an SH2-containing protein that binds to tyrosine-phosphorylated interleukin 3 and erythropoietin receptors
    • A. Yoshimura, T. Ohkubo, T. Kiguchi, N.A. Jenkins, D.J. Gilbert, and N.G. Copeland A novel cytokine-inducible gene CIS encodes an SH2-containing protein that binds to tyrosine-phosphorylated interleukin 3 and erythropoietin receptors Embo J 14 1995 2816 2826
    • (1995) Embo J , vol.14 , pp. 2816-2826
    • Yoshimura, A.1    Ohkubo, T.2    Kiguchi, T.3    Jenkins, N.A.4    Gilbert, D.J.5    Copeland, N.G.6
  • 55
    • 0032561322 scopus 로고    scopus 로고
    • Proteasomes regulate erythropoietin receptor and signal transducer and activator of transcription 5 (STAT5) activation Possible involvement of the ubiquitinated Cis protein
    • F. Verdier, S. Chretien, O. Muller, P. Varlet, A. Yoshimura, and S. Gisselbrecht Proteasomes regulate erythropoietin receptor and signal transducer and activator of transcription 5 (STAT5) activation Possible involvement of the ubiquitinated Cis protein J Biol Chem 273 1998 28185 28190
    • (1998) J Biol Chem , vol.273 , pp. 28185-28190
    • Verdier, F.1    Chretien, S.2    Muller, O.3    Varlet, P.4    Yoshimura, A.5    Gisselbrecht, S.6
  • 59
    • 0034724677 scopus 로고    scopus 로고
    • SOCS3 exerts its inhibitory function on interleukin-6 signal transduction through the SHP2 recruitment site of gp130
    • J. Schmitz, M. Weissenbach, S. Haan, P.C. Heinrich, and F. Schaper SOCS3 exerts its inhibitory function on interleukin-6 signal transduction through the SHP2 recruitment site of gp130 J Biol Chem 275 2000 12848 12856
    • (2000) J Biol Chem , vol.275 , pp. 12848-12856
    • Schmitz, J.1    Weissenbach, M.2    Haan, S.3    Heinrich, P.C.4    Schaper, F.5
  • 60
    • 0037174816 scopus 로고    scopus 로고
    • Biological evidence that SOCS-2 can act either as an enhancer or suppressor of growth hormone signaling
    • C.J. Greenhalgh, D. Metcalf, A.L. Thaus, J.E. Corbin, R. Uren, and P.O. Morgan Biological evidence that SOCS-2 can act either as an enhancer or suppressor of growth hormone signaling J Biol Chem 277 2002 40181 40184
    • (2002) J Biol Chem , vol.277 , pp. 40181-40184
    • Greenhalgh, C.J.1    Metcalf, D.2    Thaus, A.L.3    Corbin, J.E.4    Uren, R.5    Morgan, P.O.6
  • 62
    • 0033558088 scopus 로고    scopus 로고
    • Socs1 binds to multiple signalling proteins and suppresses steel factor-dependent proliferation
    • P. De Sepulveda, K. Okkenhaug, J.L. Rose, R.G. Hawley, P. Dubreuil, and R. Rottapel Socs1 binds to multiple signalling proteins and suppresses steel factor-dependent proliferation Embo J 18 1999 904 915
    • (1999) Embo J , vol.18 , pp. 904-915
    • De Sepulveda, P.1    Okkenhaug, K.2    Rose, J.L.3    Hawley, R.G.4    Dubreuil, P.5    Rottapel, R.6
  • 63
    • 0036233985 scopus 로고    scopus 로고
    • Regulation of Jak2 through the ubiquitin-proteasome pathway involves phosphorylation of Jak2 on Y1007 and interaction with SOCS-1
    • D. Ungureanu, P. Saharinen, I. Junttila, D.J. Hilton, and O. Silvennoinen Regulation of Jak2 through the ubiquitin-proteasome pathway involves phosphorylation of Jak2 on Y1007 and interaction with SOCS-1 Mol Cell Biol 22 2002 3316 3326
    • (2002) Mol Cell Biol , vol.22 , pp. 3316-3326
    • Ungureanu, D.1    Saharinen, P.2    Junttila, I.3    Hilton, D.J.4    Silvennoinen, O.5
  • 64
    • 0035918239 scopus 로고    scopus 로고
    • The SOCS box of SOCS-1 accelerates ubiquitin-dependent proteolysis of TEL-JAK2
    • S. Kamizono, T. Hanada, H. Yasukawa, S. Minoguchi, R. Kato, and M. Minoguchi The SOCS box of SOCS-1 accelerates ubiquitin-dependent proteolysis of TEL-JAK2 J Biol Chem 276 2001 12530 12538
    • (2001) J Biol Chem , vol.276 , pp. 12530-12538
    • Kamizono, S.1    Hanada, T.2    Yasukawa, H.3    Minoguchi, S.4    Kato, R.5    Minoguchi, M.6
  • 65
    • 0035036625 scopus 로고    scopus 로고
    • Socs-1 inhibits TEL-JAK2-mediated transformation of hematopoietic cells through inhibition of JAK2 kinase activity and induction of proteasome-mediated degradation
    • J. Frantsve, J. Schwaller, D.W. Sternberg, J. Kutok, and D.G. Gilliland Socs-1 inhibits TEL-JAK2-mediated transformation of hematopoietic cells through inhibition of JAK2 kinase activity and induction of proteasome-mediated degradation Mol Cell Biol 21 2001 3547 3557
    • (2001) Mol Cell Biol , vol.21 , pp. 3547-3557
    • Frantsve, J.1    Schwaller, J.2    Sternberg, D.W.3    Kutok, J.4    Gilliland, D.G.5
  • 66
    • 0036830636 scopus 로고    scopus 로고
    • SOCS-1 and SOCS-3 block insulin signaling by ubiquitin-mediated degradation of IRS1 and IRS2
    • L. Rui, M. Yuan, D. Frantz, S. Shoelson, and M.F. White SOCS-1 and SOCS-3 block insulin signaling by ubiquitin-mediated degradation of IRS1 and IRS2 J Biol Chem 277 2002 42394 42398
    • (2002) J Biol Chem , vol.277 , pp. 42394-42398
    • Rui, L.1    Yuan, M.2    Frantz, D.3    Shoelson, S.4    White, M.F.5
  • 67
    • 0141865509 scopus 로고    scopus 로고
    • Negative regulation of FAK signaling by SOCS proteins
    • E. Liu, J.F. Cote, and K. Vuori Negative regulation of FAK signaling by SOCS proteins Embo J 22 2003 5036 5046
    • (2003) Embo J , vol.22 , pp. 5036-5046
    • Liu, E.1    Cote, J.F.2    Vuori, K.3
  • 68
    • 17944383969 scopus 로고    scopus 로고
    • A sequence of the CIS gene promoter interacts preferentially with two associated STAT5A dimers: A distinct biochemical difference between STAT5A and STAT5B
    • F. Verdier, R. Rabionet, F. Gouilleux, C. Beisenherz-Huss, P. Varlet, and O. Muller A sequence of the CIS gene promoter interacts preferentially with two associated STAT5A dimers: a distinct biochemical difference between STAT5A and STAT5B Mol Cell Biol 18 1998 5852 5860
    • (1998) Mol Cell Biol , vol.18 , pp. 5852-5860
    • Verdier, F.1    Rabionet, R.2    Gouilleux, F.3    Beisenherz-Huss, C.4    Varlet, P.5    Muller, O.6
  • 69
    • 0034120709 scopus 로고    scopus 로고
    • IFN regulatory factor-1-mediated transcriptional activation of mouse STAT-induced STAT inhibitor-1 gene promoter by IFN-gamma
    • H. Saito, Y. Morita, M. Fujimoto, M. Narazaki, T. Naka, and T. Kishimoto IFN regulatory factor-1-mediated transcriptional activation of mouse STAT-induced STAT inhibitor-1 gene promoter by IFN-gamma J Immunol 164 2000 5833 5843
    • (2000) J Immunol , vol.164 , pp. 5833-5843
    • Saito, H.1    Morita, Y.2    Fujimoto, M.3    Narazaki, M.4    Naka, T.5    Kishimoto, T.6
  • 70
    • 0345447641 scopus 로고    scopus 로고
    • IL-4 and IL-13 Induce SOCS-1 Gene Expression in A549 Cells by Three Functional STAT6-Binding Motifs Located Upstream of the Transcription Initiation Site
    • D. Hebenstreit, P. Luft, A. Schmiedlechner, G. Regl, A.M. Frischauf, and F. Aberger IL-4 and IL-13 Induce SOCS-1 Gene Expression in A549 Cells by Three Functional STAT6-Binding Motifs Located Upstream of the Transcription Initiation Site J Immunol 171 2003 5901 5907
    • (2003) J Immunol , vol.171 , pp. 5901-5907
    • Hebenstreit, D.1    Luft, P.2    Schmiedlechner, A.3    Regl, G.4    Frischauf, A.M.5    Aberger, F.6
  • 71
    • 4143105721 scopus 로고    scopus 로고
    • STAT6 and Ets-1 form a stable complex that modulates SOCS-1 expression by IL-4 in keratinocytes
    • J. Travagli, M. Letourneur, J. Bertoglio, and J. Pierre STAT6 and Ets-1 form a stable complex that modulates SOCS-1 expression by IL-4 in keratinocytes J Biol Chem 279 2004 35182 35192
    • (2004) J Biol Chem , vol.279 , pp. 35182-35192
    • Travagli, J.1    Letourneur, M.2    Bertoglio, J.3    Pierre, J.4
  • 72
    • 13044263097 scopus 로고    scopus 로고
    • The conserved SOCS box motif in suppressors of cytokine signaling binds to elongins B and C and may couple bound proteins to proteasomal degradation
    • J.G. Zhang, A. Farley, S.E. Nicholson, T.A. Willson, L.M. Zugaro, and R.J. Simpson The conserved SOCS box motif in suppressors of cytokine signaling binds to elongins B and C and may couple bound proteins to proteasomal degradation Proc Natl Acad Sci USA 96 1996 2071 2076
    • (1996) Proc Natl Acad Sci USA , vol.96 , pp. 2071-2076
    • Zhang, J.G.1    Farley, A.2    Nicholson, S.E.3    Willson, T.A.4    Zugaro, L.M.5    Simpson, R.J.6
  • 75
    • 0035040971 scopus 로고    scopus 로고
    • Knocking the SOCS off a tumor suppressor
    • T. Kishimoto, and H. Kikutani Knocking the SOCS off a tumor suppressor Nat Genet 28 2001 4 5
    • (2001) Nat Genet , vol.28 , pp. 4-5
    • Kishimoto, T.1    Kikutani, H.2
  • 77
    • 0037127270 scopus 로고    scopus 로고
    • Regulation of Socs gene expression by the proto-oncoprotein GFI-1B: Two routes for STAT5 target gene induction by erythropoietin
    • A.G. Jegalian, and H. Wu Regulation of Socs gene expression by the proto-oncoprotein GFI-1B: two routes for STAT5 target gene induction by erythropoietin J Biol Chem 277 2002 2345 2352
    • (2002) J Biol Chem , vol.277 , pp. 2345-2352
    • Jegalian, A.G.1    Wu, H.2
  • 78
    • 26244462644 scopus 로고    scopus 로고
    • Hepatitis C virus core protein exerts an inhibitory effect on suppressor of cytokine signaling (SOCS)-1 gene expression
    • H. Miyoshi, H. Fujie, Y. Shintani, T. Tsutsumi, S. Shinzawa, and M. Makuuchi Hepatitis C virus core protein exerts an inhibitory effect on suppressor of cytokine signaling (SOCS)-1 gene expression J Hepatol 43 2005 757 763
    • (2005) J Hepatol , vol.43 , pp. 757-763
    • Miyoshi, H.1    Fujie, H.2    Shintani, Y.3    Tsutsumi, T.4    Shinzawa, S.5    Makuuchi, M.6
  • 79
    • 3242881890 scopus 로고    scopus 로고
    • Methylation status of suppressor of cytokine signaling-1 gene in hepatocellular carcinoma
    • H. Miyoshi, H. Fujie, K. Moriya, Y. Shintani, T. Tsutsumi, and M. Makuuchi Methylation status of suppressor of cytokine signaling-1 gene in hepatocellular carcinoma J Gastroenterol 39 2004 563 569
    • (2004) J Gastroenterol , vol.39 , pp. 563-569
    • Miyoshi, H.1    Fujie, H.2    Moriya, K.3    Shintani, Y.4    Tsutsumi, T.5    Makuuchi, M.6
  • 80
    • 0035042611 scopus 로고    scopus 로고
    • SOCS-1, a negative regulator of the JAK/STAT pathway, is silenced by methylation in human hepatocellular carcinoma and shows growth-suppression activity
    • H. Yoshikawa, K. Matsubara, G.S. Qian, P. Jackson, J.D. Groopman, and J.E. Manning SOCS-1, a negative regulator of the JAK/STAT pathway, is silenced by methylation in human hepatocellular carcinoma and shows growth-suppression activity Nat Genet 28 2001 29 35
    • (2001) Nat Genet , vol.28 , pp. 29-35
    • Yoshikawa, H.1    Matsubara, K.2    Qian, G.S.3    Jackson, P.4    Groopman, J.D.5    Manning, J.E.6
  • 81
    • 0242610382 scopus 로고    scopus 로고
    • Methylation-mediated silencing of SOCS-1 gene in hepatocellular carcinoma derived from cirrhosis
    • O. Okochi, K. Hibi, M. Sakai, S. Inoue, S. Takeda, and T. Kaneko Methylation-mediated silencing of SOCS-1 gene in hepatocellular carcinoma derived from cirrhosis Clin Cancer Res 9 2003 5295 5298
    • (2003) Clin Cancer Res , vol.9 , pp. 5295-5298
    • Okochi, O.1    Hibi, K.2    Sakai, M.3    Inoue, S.4    Takeda, S.5    Kaneko, T.6
  • 82
    • 0035503704 scopus 로고    scopus 로고
    • CpG methylation as a basis for breast tumor-specific loss of NES1/kallikrein 10 expression
    • B. Li, J. Goyal, S. Dhar, G. Dimri, E. Evron, and S. Sukumar CpG methylation as a basis for breast tumor-specific loss of NES1/kallikrein 10 expression Cancer Res 61 2001 8014 8021
    • (2001) Cancer Res , vol.61 , pp. 8014-8021
    • Li, B.1    Goyal, J.2    Dhar, S.3    Dimri, G.4    Evron, E.5    Sukumar, S.6
  • 83
    • 0042575343 scopus 로고    scopus 로고
    • Aberrant methylation of suppressor of cytokine signalling-1 (SOCS-1) gene in pancreatic ductal neoplasms
    • N. Fukushima, N. Sato, F. Sahin, G.H. Su, R.H. Hruban, and M. Goggins Aberrant methylation of suppressor of cytokine signalling-1 (SOCS-1) gene in pancreatic ductal neoplasms Br J Cancer 89 2003 338 343
    • (2003) Br J Cancer , vol.89 , pp. 338-343
    • Fukushima, N.1    Sato, N.2    Sahin, F.3    Su, G.H.4    Hruban, R.H.5    Goggins, M.6
  • 84
    • 0037227602 scopus 로고    scopus 로고
    • Hypermethylation associated with inactivation of the SOCS-1 gene, a JAK/STAT inhibitor, in human hepatoblastomas
    • H. Nagai, T. Naka, Y. Terada, T. Komazaki, A. Yabe, and E. Jin Hypermethylation associated with inactivation of the SOCS-1 gene, a JAK/STAT inhibitor, in human hepatoblastomas J Hum Genet 48 2003 65 69
    • (2003) J Hum Genet , vol.48 , pp. 65-69
    • Nagai, H.1    Naka, T.2    Terada, Y.3    Komazaki, T.4    Yabe, A.5    Jin, E.6
  • 85
    • 1542345461 scopus 로고    scopus 로고
    • Aberrant methylation of SOCS-1 was observed in younger colorectal cancer patients
    • S. Fujitake, K. Hibi, O. Okochi, Y. Kodera, K. Ito, and S. Akiyama Aberrant methylation of SOCS-1 was observed in younger colorectal cancer patients J Gastroenterol 39 2004 120 124
    • (2004) J Gastroenterol , vol.39 , pp. 120-124
    • Fujitake, S.1    Hibi, K.2    Okochi, O.3    Kodera, Y.4    Ito, K.5    Akiyama, S.6
  • 86
    • 3242749984 scopus 로고    scopus 로고
    • Promoter CpG methylation of tumor suppressor genes in colorectal cancer and its relationship to clinical features
    • S.Y. Lin, K.T. Yeh, W.T. Chen, H.C. Chen, S.T. Chen, and H.Y. Chiou Promoter CpG methylation of tumor suppressor genes in colorectal cancer and its relationship to clinical features Oncol Rep 11 2004 341 348
    • (2004) Oncol Rep , vol.11 , pp. 341-348
    • Lin, S.Y.1    Yeh, K.T.2    Chen, W.T.3    Chen, H.C.4    Chen, S.T.5    Chiou, H.Y.6
  • 87
    • 8644249909 scopus 로고    scopus 로고
    • Epigenetic inactivation of SOCS-1 by CpG island hypermethylation in human gastric carcinoma
    • Y. Oshimo, K. Kuraoka, H. Nakayama, Y. Kitadai, K. Yoshida, and K. Chayama Epigenetic inactivation of SOCS-1 by CpG island hypermethylation in human gastric carcinoma Int J Cancer 112 2004 1003 1009
    • (2004) Int J Cancer , vol.112 , pp. 1003-1009
    • Oshimo, Y.1    Kuraoka, K.2    Nakayama, H.3    Kitadai, Y.4    Yoshida, K.5    Chayama, K.6
  • 89
    • 6944250441 scopus 로고    scopus 로고
    • Constitutional activation of IL-6-mediated JAK/STAT pathway through hypermethylation of SOCS-1 in human gastric cancer cell line
    • K.F. To, M.W. Chan, W.K. Leung, E.K. Ng, J. Yu, and A.H. Bai Constitutional activation of IL-6-mediated JAK/STAT pathway through hypermethylation of SOCS-1 in human gastric cancer cell line Br J Cancer 91 2004 1335 1341
    • (2004) Br J Cancer , vol.91 , pp. 1335-1341
    • To, K.F.1    Chan, M.W.2    Leung, W.K.3    Ng, E.K.4    Yu, J.5    Bai, A.H.6
  • 91
    • 0038784365 scopus 로고    scopus 로고
    • SOCS-1, a negative regulator of cytokine signaling, is frequently silenced by methylation in multiple myeloma
    • O. Galm, H. Yoshikawa, M. Esteller, R. Osieka, and J.G. Herman SOCS-1, a negative regulator of cytokine signaling, is frequently silenced by methylation in multiple myeloma Blood 101 2003 2784 2788
    • (2003) Blood , vol.101 , pp. 2784-2788
    • Galm, O.1    Yoshikawa, H.2    Esteller, M.3    Osieka, R.4    Herman, J.G.5
  • 93
    • 0346694510 scopus 로고    scopus 로고
    • Aberrant methylation in promoter-associated CpG islands of multiple genes in therapy-related leukemia
    • E. Uehara, S. Takeuchi, T. Tasaka, Y. Matsuhashi, Y. Yang, and M. Fujita Aberrant methylation in promoter-associated CpG islands of multiple genes in therapy-related leukemia Int J Oncol 23 2003 693 696
    • (2003) Int J Oncol , vol.23 , pp. 693-696
    • Uehara, E.1    Takeuchi, S.2    Tasaka, T.3    Matsuhashi, Y.4    Yang, Y.5    Fujita, M.6
  • 94
    • 7244237957 scopus 로고    scopus 로고
    • Aberrant methylation of multiple tumor suppressor genes in acute myeloid leukemia
    • C.G. Ekmekci, M.I. Gutierrez, A.K. Siraj, U. Ozbek, and K. Bhatia Aberrant methylation of multiple tumor suppressor genes in acute myeloid leukemia Am J Hematol 77 2004 233 240
    • (2004) Am J Hematol , vol.77 , pp. 233-240
    • Ekmekci, C.G.1    Gutierrez, M.I.2    Siraj, A.K.3    Ozbek, U.4    Bhatia, K.5
  • 95
    • 0031017533 scopus 로고    scopus 로고
    • Mutation in the Jak kinase JH2 domain hyperactivates Drosophila and mammalian Jak-Stat pathways
    • H. Luo, P. Rose, D. Barber, W.P. Hanratty, S. Lee, and T.M. Roberts Mutation in the Jak kinase JH2 domain hyperactivates Drosophila and mammalian Jak-Stat pathways Mol Cell Biol 17 1997 1562 1571
    • (1997) Mol Cell Biol , vol.17 , pp. 1562-1571
    • Luo, H.1    Rose, P.2    Barber, D.3    Hanratty, W.P.4    Lee, S.5    Roberts, T.M.6
  • 96
    • 4544358147 scopus 로고    scopus 로고
    • Suppressor of cytokine signalling-1 gene silencing in acute myeloid leukaemia and human haematopoietic cell lines
    • D. Watanabe, S. Ezoe, M. Fujimoto, A. Kimura, Y. Saito, and H. Nagai Suppressor of cytokine signalling-1 gene silencing in acute myeloid leukaemia and human haematopoietic cell lines Br J Haematol 126 2004 726 735
    • (2004) Br J Haematol , vol.126 , pp. 726-735
    • Watanabe, D.1    Ezoe, S.2    Fujimoto, M.3    Kimura, A.4    Saito, Y.5    Nagai, H.6
  • 97
    • 24944476696 scopus 로고    scopus 로고
    • Hypermethylation of the suppressor of cytokine signalling-1 (SOCS-1) in myelodysplastic syndrome
    • K. Brakensiek, F. Langer, B. Schlegelberger, H. Kreipe, and U. Lehmann Hypermethylation of the suppressor of cytokine signalling-1 (SOCS-1) in myelodysplastic syndrome Br J Haematol 130 2005 209 217
    • (2005) Br J Haematol , vol.130 , pp. 209-217
    • Brakensiek, K.1    Langer, F.2    Schlegelberger, B.3    Kreipe, H.4    Lehmann, U.5
  • 98
    • 27144433826 scopus 로고    scopus 로고
    • Methylation silencing of SOCS-3 promotes cell growth and migration by enhancing JAK/STAT and FAK signalings in human hepatocellular carcinoma
    • Y. Niwa, H. Kanda, Y. Shikauchi, A. Saiura, K. Matsubara, and T. Kitagawa Methylation silencing of SOCS-3 promotes cell growth and migration by enhancing JAK/STAT and FAK signalings in human hepatocellular carcinoma Oncogene 24 2005 6406 6417
    • (2005) Oncogene , vol.24 , pp. 6406-6417
    • Niwa, Y.1    Kanda, H.2    Shikauchi, Y.3    Saiura, A.4    Matsubara, K.5    Kitagawa, T.6
  • 99
    • 27144540201 scopus 로고    scopus 로고
    • SOCS-3 is frequently methylated in head and neck squamous cell carcinoma and its precursor lesions and causes growth inhibition
    • A. Weber, U.R. Hengge, W. Bardenheuer, I. Tischoff, F. Sommerer, and A. Markwarth SOCS-3 is frequently methylated in head and neck squamous cell carcinoma and its precursor lesions and causes growth inhibition Oncogene 24 2005 6699 6708
    • (2005) Oncogene , vol.24 , pp. 6699-6708
    • Weber, A.1    Hengge, U.R.2    Bardenheuer, W.3    Tischoff, I.4    Sommerer, F.5    Markwarth, A.6
  • 101
    • 15244350510 scopus 로고    scopus 로고
    • Biallelic mutation of SOCS-1 impairs JAK2 degradation and sustains phospho-JAK2 action in the MedB-1 mediastinal lymphoma line
    • I. Melzner, A.J. Bucur, S. Bruderlein, K. Dorsch, C. Hasel, and T.F. Barth Biallelic mutation of SOCS-1 impairs JAK2 degradation and sustains phospho-JAK2 action in the MedB-1 mediastinal lymphoma line Blood 105 2005 2535 2542
    • (2005) Blood , vol.105 , pp. 2535-2542
    • Melzner, I.1    Bucur, A.J.2    Bruderlein, S.3    Dorsch, K.4    Hasel, C.5    Barth, T.F.6
  • 102
    • 32144453118 scopus 로고    scopus 로고
    • Biallelic deletion within 16p13.13 including SOCS-1 in Karpas1106P mediastinal B-cell lymphoma line is associated with delayed degradation of JAK2 protein
    • I. Melzner, M.A. Weniger, A.J. Bucur, S. Bruderlein, K. Dorsch, and C. Hasel Biallelic deletion within 16p13.13 including SOCS-1 in Karpas1106P mediastinal B-cell lymphoma line is associated with delayed degradation of JAK2 protein Int J Cancer 2005
    • (2005) Int J Cancer
    • Melzner, I.1    Weniger, M.A.2    Bucur, A.J.3    Bruderlein, S.4    Dorsch, K.5    Hasel, C.6
  • 103


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