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Volumn 18, Issue , 2003, Pages 75-86

Role of prolactin/prolactin receptor signaling in human breast cancer

Author keywords

[No Author keywords available]

Indexed keywords

CYCLOPHILIN; ISOMERASE; JANUS KINASE 2; PROLACTIN; PROLACTIN RECEPTOR; PROTEIN KINASE P60; PROTEIN TYROSINE KINASE; REPRESSOR PROTEIN; SERINE; STAT3 PROTEIN; STAT5 PROTEIN; TRANSCRIPTION FACTOR; TYROSINE;

EID: 4444255613     PISSN: 08886008     EISSN: None     Source Type: Journal    
DOI: 10.3233/BD-2003-18108     Document Type: Review
Times cited : (55)

References (118)
  • 1
    • 0025162844 scopus 로고
    • Structural design and molecular evolution of a cytokine receptor superfamily
    • J.F. Bazan, Structural design and molecular evolution of a cytokine receptor superfamily, Proc Natl Acad Sci USA 87 (1990), 6934-6938.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 6934-6938
    • Bazan, J.F.1
  • 2
    • 0002825985 scopus 로고
    • Development of the human mammary gland
    • M.C. Neville and C.W. Daniels, New York, Plenum Press
    • J. Russo and I.H. Russo, Development of the human mammary gland, in: The mammary gland, M.C. Neville and C.W. Daniels, New York, Plenum Press, 1987, pp. 67-93.
    • (1987) The Mammary Gland , pp. 67-93
    • Russo, J.1    Russo, I.H.2
  • 4
    • 0017615463 scopus 로고
    • Prolactin and Murine Mammary Tumorigenesis, A Review
    • C.W. Welsch and H. Nagasawa, Prolactin and Murine Mammary Tumorigenesis, A Review, Cancer Res 37 (1977), 951-963.
    • (1977) Cancer Res. , vol.37 , pp. 951-963
    • Welsch, C.W.1    Nagasawa, H.2
  • 5
    • 0022004418 scopus 로고
    • Host factors affecting the growth of carcinogen-induced rat mammary carcinomas, A review and tribute to Charles Brenton Huggins
    • C.W. Welsch, Host factors affecting the growth of carcinogen-induced rat mammary carcinomas, A review and tribute to Charles Brenton Huggins, Cancer Res 45 (1985), 3415-3443.
    • (1985) Cancer Res. , vol.45 , pp. 3415-3443
    • Welsch, C.W.1
  • 6
    • 0022573031 scopus 로고
    • Promotion by prolactin of the growth of human breast neoplasms cultured in vitro in the soft agar clonogenic assay
    • A. Manni, C. Wright, G. Davis, J. Glenn, R. Joehl and P. Feil, Promotion by prolactin of the growth of human breast neoplasms cultured in vitro in the soft agar clonogenic assay, Cancer Res 46 (1986), 1669-1672.
    • (1986) Cancer Res. , vol.46 , pp. 1669-1672
    • Manni, A.1    Wright, C.2    Davis, G.3    Glenn, J.4    Joehl, R.5    Feil, P.6
  • 7
    • 0020700098 scopus 로고
    • Physiological concentrations of prolactin can promote the growth of human breast tumor cells in culture
    • W.B. Malarkey, M. Kennedy, L.E. Allred and G. Milo, Physiological concentrations of prolactin can promote the growth of human breast tumor cells in culture, J Clin Endocrinol Metab 56 (1983), 673-677.
    • (1983) J. Clin. Endocrinol. Metab. , vol.56 , pp. 673-677
    • Malarkey, W.B.1    Kennedy, M.2    Allred, L.E.3    Milo, G.4
  • 8
    • 0021150074 scopus 로고
    • Twenty-four hour prolactin profiles and prolactin response to dopamine in long distance running women
    • F.E. Chang, S.R. Richards, M.H. Kim and W.B. Malarkey, Twenty-four hour prolactin profiles and prolactin response to dopamine in long distance running women, J Clin Endocrinol Metab 59 (1984), 631-635.
    • (1984) J. Clin. Endocrinol. Metab. , vol.59 , pp. 631-635
    • Chang, F.E.1    Richards, S.R.2    Kim, M.H.3    Malarkey, W.B.4
  • 10
    • 0015325380 scopus 로고
    • Clinical trial of 2-Br-a-ergocryptine (CB154) in advanced breast cancer
    • J.C. Heuson, A. Coune and M. Staquet, Clinical trial of 2-Br-a-ergocryptine (CB154) in advanced breast cancer, Eur J Cancer 8 (1972), 155-156.
    • (1972) Eur. J. Cancer. , vol.8 , pp. 155-156
    • Heuson, J.C.1    Coune, A.2    Staquet, M.3
  • 11
    • 0024262887 scopus 로고
    • Cappelaere Tamoxifen plus bromocriptine versus tamoxifen plus placebo in advanced breast cancer, Results of a double blind multicenter clinical trial
    • J. Bonneterre, L. Mauriac, B. Weber, H. Roche, P. Fargeot, M. Tubiana-Hulin, M. Sevin, P. Chollet and P. Cappelaere, Tamoxifen plus bromocriptine versus tamoxifen plus placebo in advanced breast cancer, Results of a double blind multicenter clinical trial, Eur J Cancer 24 (1988), 1851-1853.
    • (1988) Eur. J. Cancer , vol.24 , pp. 1851-1853
    • Bonneterre, J.1    Mauriac, L.2    Weber, B.3    Roche, P.4    Fargeot, M.5    Tubiana-Hulin, M.6    Sevin, P.7    Chollet, P.8
  • 12
    • 0028963516 scopus 로고
    • Expression of prolactin and prolactin receptor in human breast carcinoma, Evidence for an autocrine/paracrine loop
    • C.V. Clevenger, W.-P. Chang, W. Ngo, T.L.M. Pasha, K.T. Montone and J.E. Tomaszewski, Expression of prolactin and prolactin receptor in human breast carcinoma, Evidence for an autocrine/paracrine loop, Am J Pathol 146 (1995), 695-705.
    • (1995) Am. J. Pathol. , vol.146 , pp. 695-705
    • Clevenger, C.V.1    Chang, W.-P.2    Ngo, W.3    Pasha, T.L.M.4    Montone, K.T.5    Tomaszewski, J.E.6
  • 14
    • 0030621563 scopus 로고    scopus 로고
    • Prolactin as an autocrine/ paracrine growth factor in breast tissue
    • C.V. Clevenger and T.L. Plank, Prolactin as an autocrine/ paracrine growth factor in breast tissue, J Mammary Gland Biol Neoplasia 2 (1997), 59-68.
    • (1997) J. Mammary Gland Biol. Neoplasia , vol.2 , pp. 59-68
    • Clevenger, C.V.1    Plank, T.L.2
  • 17
    • 0029005357 scopus 로고
    • Prolactin synthesis and secretion by human breast cancer cells
    • E. Ginsburg and B.K. Vonderhaar, Prolactin synthesis and secretion by human breast cancer cells, Cancer Res 55 (1995), 2591-2595.
    • (1995) Cancer Res. , vol.55 , pp. 2591-2595
    • Ginsburg, E.1    Vonderhaar, B.K.2
  • 18
    • 0031851198 scopus 로고    scopus 로고
    • Prolactin, The forgotten hormone of human breast cancer
    • B.K. Vonderhaar, Prolactin, The forgotten hormone of human breast cancer, Pharmacol Ther 79 (1998), 169-178.
    • (1998) Pharmacol. Ther. , vol.79 , pp. 169-178
    • Vonderhaar, B.K.1
  • 19
    • 0242585005 scopus 로고    scopus 로고
    • Prolactin regulates mammary epithelial cell proliferation via autocrine/paracrine mechanism
    • M.J. Naylor, J.A. Lockefeer, N.D. Horseman and C.J. Ormandy, Prolactin regulates mammary epithelial cell proliferation via autocrine/paracrine mechanism, Endocrine 20 (2003), 111-114.
    • (2003) Endocrine , vol.20 , pp. 111-114
    • Naylor, M.J.1    Lockefeer, J.A.2    Horseman, N.D.3    Ormandy, C.J.4
  • 20
    • 0026750040 scopus 로고
    • Expression of prolactin and its receptor in human lymphoid cells
    • I. Pellegrini, J-J. Lebrun, S. Ali and P.A. Kelly, Expression of prolactin and its receptor in human lymphoid cells, Mol Endocrinol 6 (1992), 1023-1031.
    • (1992) Mol. Endocrinol. , vol.6 , pp. 1023-1031
    • Pellegrini, I.1    Lebrun, J.-J.2    Ali, S.3    Kelly, P.A.4
  • 21
    • 0024381360 scopus 로고
    • Regulation of prolactin secretion in the human B-lymphoblastoid cell line IM-9-P3 by dexamethasone but not other regulators of pituitary prolactin secretion
    • B. Gellersen, G.E. DiMattia, H.G. Friesen and H.G. Bohnet, Regulation of prolactin secretion in the human B-lymphoblastoid cell line IM-9-P3 by dexamethasone but not other regulators of pituitary prolactin secretion, Endocrinology 125 (1989), 2853-2861.
    • (1989) Endocrinology , vol.125 , pp. 2853-2861
    • Gellersen, B.1    DiMattia, G.E.2    Friesen, H.G.3    Bohnet, H.G.4
  • 22
  • 26
    • 0028301226 scopus 로고
    • Growth signaling and JAK2 association mediated by membrane-proximal cytoplasmic regions of prolactin receptors
    • L. DaSilva, O.M.Z. Howard, H. Rui, R.A. Kirken and W.L. Farrar, Growth signaling and JAK2 association mediated by membrane-proximal cytoplasmic regions of prolactin receptors, J Biol Chem 269 (1994), 18267-18270.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18267-18270
    • DaSilva, L.1    Howard, O.M.Z.2    Rui, H.3    Kirken, R.A.4    Farrar, W.L.5
  • 27
    • 0033544961 scopus 로고    scopus 로고
    • Functional characterization of the intermediate isoform of the human prolactin receptor
    • J.B. Kline, H. Roehrs and C.V. Clevenger, Functional characterization of the intermediate isoform of the human prolactin receptor, J Biol Chem 274 (1999), 35461-35468.
    • (1999) J. Biol. Chem. , vol.274 , pp. 35461-35468
    • Kline, J.B.1    Roehrs, H.2    Clevenger, C.V.3
  • 28
    • 0036794307 scopus 로고    scopus 로고
    • Characterization of a novel and functional human prolactin receptor isoform (ΔSIPRCr) containing only one fibronectin-like domain
    • J.B. Kline, M.A. Rycyzyn and C.V. Clevenger, Characterization of a novel and functional human prolactin receptor isoform (Δ SIPRCr) containing only one fibronectin-like domain, Mol Endocrinol 16 (2002), 2310-2322.
    • (2002) Mol. Endocrinol. , vol.16 , pp. 2310-2322
    • Kline, J.B.1    Rycyzyn, M.A.2    Clevenger, C.V.3
  • 29
    • 0035816689 scopus 로고    scopus 로고
    • Identification and characterization of the prolactin-binding protein (PRLBP) in human serum and milk
    • J.B. Kline and C.V. Clevenger, Identification and characterization of the prolactin-binding protein (PRLBP) in human serum and milk, J Biol Chem 276 (2001), 24760-24766.
    • (2001) J. Biol. Chem. , vol.276 , pp. 24760-24766
    • Kline, J.B.1    Clevenger, C.V.2
  • 30
    • 0037294370 scopus 로고    scopus 로고
    • Alternative splicing to exon 11 of human prolactin receptor results in multiple isoforms including a secreted prolactin-binding protein
    • J. Trott, R. Hovey, S. Koduri and B.K. Vonderhaar, Alternative splicing to exon 11 of human prolactin receptor results in multiple isoforms including a secreted prolactin-binding protein, J Mol Endocrinol 30 (2003), 31-47.
    • (2003) J. Mol. Endocrinol. , vol.30 , pp. 31-47
    • Trott, J.1    Hovey, R.2    Koduri, S.3    Vonderhaar, B.K.4
  • 32
    • 0035798602 scopus 로고    scopus 로고
    • Isolation and characterization of two novel forms of the human prolactin receptor generated by alternative splicing of a newly identified exon 11
    • in press
    • Z-Z. Hu, J. Meng and M.L. Dufau, Isolation and characterization of two novel forms of the human prolactin receptor generated by alternative splicing of a newly identified exon 11, J Biol Chem (2001), in press.
    • (2001) J. Biol. Chem.
    • Hu, Z.-Z.1    Meng, J.2    Dufau, M.L.3
  • 33
    • 0029785849 scopus 로고    scopus 로고
    • Real-time measurements of the interactions between lactogenic hormones and prolactin-receptor extracellular domains from several species support the model hormone-induced transient receptor dimerization
    • A. Gertler, J. Grosclaude, C.J. Strasburger, S. Nir and J. Djiane, Real-time measurements of the interactions between lactogenic hormones and prolactin-receptor extracellular domains from several species support the model hormone-induced transient receptor dimerization, J Biol Chem 271 (1996), 24482-24491.
    • (1996) J. Biol. Chem. , vol.271 , pp. 24482-24491
    • Gertler, A.1    Grosclaude, J.2    Strasburger, C.J.3    Nir, S.4    Djiane, J.5
  • 34
    • 0028032203 scopus 로고
    • The X-ray structure of a growth hormone-prolactin receptor complex
    • W. Somers, M. Ultsch, A.M. de Vos and A.A. Kossiakoff, The X-ray structure of a growth hormone-prolactin receptor complex, Nature 272 (1994), 478-481.
    • (1994) Nature , vol.272 , pp. 478-481
    • Somers, W.1    Ultsch, M.2    de Vos, A.M.3    Kossiakoff, A.A.4
  • 37
    • 0026332810 scopus 로고
    • Dimerization of the extracellular domain of the human growth hormone receptor by a single hormone molecule
    • B.C. Cunningham, M. Ultsch, A.M. DeVoss, M.G. Mulkerrin, K.R. Clauser and J.A. Wells, Dimerization of the extracellular domain of the human growth hormone receptor by a single hormone molecule, Science 254 (1991), 821-825.
    • (1991) Science , vol.254 , pp. 821-825
    • Cunningham, B.C.1    Ultsch, M.2    DeVoss, A.M.3    Mulkerrin, M.G.4    Clauser, M.G.5    Wells, J.A.6
  • 38
    • 0030013232 scopus 로고    scopus 로고
    • Modulation of growth factor receptor function by isoform heterodimerization
    • W-P. Chang and C.V. Clevenger, Modulation of growth factor receptor function by isoform heterodimerization, Proc Natl Acad Sci USA 93 (1996), 5947-5952.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 5947-5952
    • Chang, W.-P.1    Clevenger, C.V.2
  • 39
    • 0031000938 scopus 로고    scopus 로고
    • Prolactin signal transduction to milk protein genes, carboxy-terminal part of the prolactin receptor and its tyrosine phosphorylation are not obligatory for JAK2 and STAT5 activation
    • O. Goupille, N. Daniel, C. Bignon, J. Jolivet and J. Djiane, Prolactin signal transduction to milk protein genes, carboxy-terminal part of the prolactin receptor and its tyrosine phosphorylation are not obligatory for JAK2 and STAT5 activation, Mol Endocrinol 127 (1997), 155-169.
    • (1997) Mol. Endocrinol. , vol.127 , pp. 155-169
    • Goupille, O.1    Daniel, N.2    Bignon, C.3    Jolivet, J.4    Djiane, J.5
  • 40
    • 0028059104 scopus 로고
    • Prolactin induces rapid phosphorylation and activation of prolactin receptor associated Raf-1 kinase in a T-cell line
    • C.V. Clevenger, T. Torigoe and J.C. Reed, Prolactin induces rapid phosphorylation and activation of prolactin receptor associated Raf-1 kinase in a T-cell line, J Biol Chem 269 (1994), 5559-5565.
    • (1994) J. Biol. Chem. , vol.269 , pp. 5559-5565
    • Clevenger, C.V.1    Torigoe, T.2    Reed, J.C.3
  • 41
    • 0029112369 scopus 로고
    • Prolactin activates Ras via signaling proteins SHC, growth factor receptor bound 2, and son of sevenless
    • R.A. Erwin, R.A. Kirken, M.G. Malbarba, W.L. Farrar and H. Rui, Prolactin activates Ras via signaling proteins SHC, growth factor receptor bound 2, and son of sevenless, Endocrinology 136 (1995), 3512-3518.
    • (1995) Endocrinology , vol.136 , pp. 3512-3518
    • Erwin, R.A.1    Kirken, R.A.2    Malbarba, M.G.3    Farrar, W.L.4    Rui, H.5
  • 42
    • 0029817335 scopus 로고    scopus 로고
    • Activation of raf-1, MEK, and MAP kinase in prolactin responsive mammary cells
    • R. Das and B.K. Vonderhaar, Activation of raf-1, MEK, and MAP kinase in prolactin responsive mammary cells, Breast Cancer Res Treat 40 (1996), 141-149.
    • (1996) Breast Cancer Res. Treat. , vol.40 , pp. 141-149
    • Das, R.1    Vonderhaar, B.K.2
  • 43
    • 0035012866 scopus 로고    scopus 로고
    • Activation and association of the Tec tyrosine kinase with the human prolactin receptor, Mapping of a Tec/Vav1 - Receptor binding site
    • J.B. Kline, D.J. Moore and C.V. Clevenger, Activation and association of the Tec tyrosine kinase with the human prolactin receptor, Mapping of a Tec/Vav1 - receptor binding site, Mol Endocrinol 15 (2001), 832-841.
    • (2001) Mol. Endocrinol. , vol.15 , pp. 832-841
    • Kline, J.B.1    Moore, D.J.2    Clevenger, C.V.3
  • 44
    • 0035172222 scopus 로고    scopus 로고
    • Src family kinases are required for prolactin induction of cell proliferation
    • J.A. Fresno Vara, M.A. Caceres, A. Silva and J. Martin-Perez, Src family kinases are required for prolactin induction of cell proliferation, Mol Biol Cell 12 (2001), 2171-2183.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2171-2183
    • Fresno Vara, J.A.1    Caceres, M.A.2    Silva, A.3    Martin-Perez, J.4
  • 45
    • 0031590720 scopus 로고    scopus 로고
    • Involvement of c-src in beta-casein expression by mammary epithelial cells
    • P. Sorensen and L.G. Sheffield, Involvement of c-src in beta-casein expression by mammary epithelial cells, Biochem Biophys Res Commun 241 (1997), 710-713.
    • (1997) Biochem. Biophys. Res. Commun. , vol.241 , pp. 710-713
    • Sorensen, P.1    Sheffield, L.G.2
  • 46
    • 0028243306 scopus 로고
    • The protein tyrosine kinase p59fyn is associated with prolactin receptor and is activated by prolactin stimulation of T-lymphocytes
    • C.V. Clevenger and M.V. Medaglia, The protein tyrosine kinase p59fyn is associated with prolactin receptor and is activated by prolactin stimulation of T-lymphocytes, Mol Endocrinol 8 (1994), 674-681.
    • (1994) Mol. Endocrinol. , vol.8 , pp. 674-681
    • Clevenger, C.V.1    Medaglia, M.V.2
  • 47
    • 0026749173 scopus 로고
    • Requirement for prolactin during cell cycle regulated gene expression in cloned T-lymphocytes
    • C.V. Clevenger, A.L. Sillman, J. Hanley-Hyde and M.B. Prystowsky, Requirement for prolactin during cell cycle regulated gene expression in cloned T-lymphocytes, Endocrinology 130 (1992), 3216-3222.
    • (1992) Endocrinology , vol.130 , pp. 3216-3222
    • Clevenger, C.V.1    Sillman, A.L.2    Hanley-Hyde, J.3    Prystowsky, M.B.4
  • 48
    • 0025190187 scopus 로고
    • Prolactin stimulates transcription of growth-related genes in Nb2 T lymphoma cells
    • L-Y. Yu-Lee, Prolactin stimulates transcription of growth-related genes in Nb2 T lymphoma cells, Mol Cell Endocrinol 68 (1990), 21-28.
    • (1990) Mol. Cell Endocrinol. , vol.68 , pp. 21-28
    • Yu-Lee, L.-Y.1
  • 49
    • 0024545159 scopus 로고
    • Differential regulation of rat b-casein-chloramphenical acetyltransferase fusion gene expression in transgenic mice
    • K.F. Lee, S.H. Atiee and J.M. Rosen, Differential regulation of rat b-casein-chloramphenical acetyltransferase fusion gene expression in transgenic mice, Mol Cell Biol 9 (1989), 560-565.
    • (1989) Mol. Cell Biol. , vol.9 , pp. 560-565
    • Lee, K.F.1    Atiee, S.H.2    Rosen, J.M.3
  • 50
    • 0032491579 scopus 로고    scopus 로고
    • Cyclin D expression is controlled post-transcriptionally via a phosphatidylinositol 3-kinase/Akt-dependent pathway
    • R.C. Muise-Helmericks, H.L. Grimes, A. Bellacosa, S.E. Malstrom, P.N. Tsichlis and N. Rosen, Cyclin D expression is controlled post-transcriptionally via a phosphatidylinositol 3-kinase/Akt-dependent pathway, J Biol Chem 273 (1998), 29864-29872.
    • (1998) J. Biol. Chem. , vol.273 , pp. 29864-29872
    • Muise-Helmericks, R.C.1    Grimes, H.L.2    Bellacosa, A.3    Malstrom, S.E.4    Tsichlis, P.N.5    Rosen, N.6
  • 51
    • 0035151007 scopus 로고    scopus 로고
    • Cooperative effects of STAT5 and C/EBP b on b-casein gene transcription are mediated by the glucocorticoid receptor
    • S.L. Wysomierski and J.M. Rosen, Cooperative effects of STAT5 and C/EBP b on b-casein gene transcription are mediated by the glucocorticoid receptor, Mol Endo 15 (2001), 228-240.
    • (2001) Mol. Endo. , vol.15 , pp. 228-240
    • Wysomierski, S.L.1    Rosen, J.M.2
  • 52
    • 0031930298 scopus 로고    scopus 로고
    • Stoichiometric structure/function analysis of the prolactin receptor signaling domains by receptor chimeras
    • W-P. Chang, Y. Ye and C.V. Clevenger, Stoichiometric structure/function analysis of the prolactin receptor signaling domains by receptor chimeras, Mol Cell Biol 18 (1998), 896-905.
    • (1998) Mol. Cell Biol. , vol.18 , pp. 896-905
    • Chang, W.-P.1    Ye, Y.2    Clevenger, C.V.3
  • 53
    • 0027327484 scopus 로고
    • JAK2 associates with the erythropoietin receptor and is tyrosine phosphorylated and activated following stimulation with erythropoietin
    • B.A. Witthuhn, F.W. Quelle, O. Silvennoinen, T. Yi, B. Tang, O. Miura and J.N. Ihle, JAK2 associates with the erythropoietin receptor and is tyrosine phosphorylated and activated following stimulation with erythropoietin, Cell 74 (1993), 227-236.
    • (1993) Cell , vol.74 , pp. 227-236
    • Witthuhn, B.A.1    Quelle, F.W.2    Silvennoinen, O.3    Yi, T.4    Tang, B.5    Miura, O.6    Ihle, J.N.7
  • 56
    • 0029011115 scopus 로고
    • The amino-terminal portion of the JAK2 protein kinase is necessary for binding and phosphorylation of the granulocyte-macrophage colony-stimulated factor receptor bc chain
    • Y. Zhao, F. Wagner, S.J. Frank and A.S. Kraft, The amino-terminal portion of the JAK2 protein kinase is necessary for binding and phosphorylation of the granulocyte-macrophage colony-stimulated factor receptor bc chain, J Biol Chem 270 (1995), 13814-13818.
    • (1995) J. Biol. Chem. , vol.270 , pp. 13814-13818
    • Zhao, Y.1    Wagner, F.2    Frank, S.J.3    Kraft, A.S.4
  • 57
    • 0027941433 scopus 로고
    • Activation of receptor-associated tyrosine kinase JAK2 by prolactin
    • H. Rui, R.A. Kirken and W.L. Farrar, Activation of receptor-associated tyrosine kinase JAK2 by prolactin, J Biol Chem 269 (1994), 5364-5368.
    • (1994) J. Biol. Chem. , vol.269 , pp. 5364-5368
    • Rui, H.1    Kirken, R.A.2    Farrar, W.L.3
  • 59
    • 0028342870 scopus 로고
    • Identification of JAK protein tyrosine kinases as signaling molecules for prolactin. Functional analysis of prolactin receptor and prolactin-erythropoietin receptor chimera expressed in lymphod cells
    • I. Dusanter-Fourt, O. Muller, A. Ziemicki, P. Mayeux, B. Drucker, J. Dijane, A. Wilks, A.G. Harpur, S. Fischer and S. Gisselbrecht, Identification of JAK protein tyrosine kinases as signaling molecules for prolactin. Functional analysis of prolactin receptor and prolactin-erythropoietin receptor chimera expressed in lymphod cells, EMBO J 13 (1994), 2583-2591.
    • (1994) EMBO J. , vol.13 , pp. 2583-2591
    • Dusanter-Fourt, I.1    Muller, O.2    Ziemicki, A.3    Mayeux, P.4    Drucker, B.5    Dijane, J.6    Wilks, A.7    Harpur, A.G.8    Fischer, S.9    Gisselbrecht, S.10
  • 60
    • 0037134424 scopus 로고    scopus 로고
    • Role of tyrosine kinase Jak2 in prolactin-induced differentiation and growth of mammary epithelial cells
    • J. Xie, M.J. LeBaron, M.T. Nevalainen and H. Rui, Role of tyrosine kinase Jak2 in prolactin-induced differentiation and growth of mammary epithelial cells, J Biol Chem 277 (2002), 14020-14030.
    • (2002) J. Biol. Chem. , vol.277 , pp. 14020-14030
    • Xie, J.1    LeBaron, M.J.2    Nevalainen, M.T.3    Rui, H.4
  • 61
    • 0036214521 scopus 로고    scopus 로고
    • PRL activates the cyclin d1 promoter via the jak2/stat pathway
    • J.L. Brockman, M.D. Schroeder and L.A. Schuler, PRL activates the cyclin d1 promoter via the jak2/stat pathway, Mol Endocrinol 16 (2002), 774-784.
    • (2002) Mol. Endocrinol. , vol.16 , pp. 774-784
    • Brockman, J.L.1    Schroeder, M.D.2    Schuler, L.A.3
  • 62
    • 0028921573 scopus 로고
    • Jaks and Stats in signaling by the cytokine receptor superfamily
    • J.N. Ihle and I.M. Kerr, Jaks and Stats in signaling by the cytokine receptor superfamily, Trends Genet 11 (1995), 69-74.
    • (1995) Trends Genet. , vol.11 , pp. 69-74
    • Ihle, J.N.1    Kerr, I.M.2
  • 63
    • 0038371050 scopus 로고    scopus 로고
    • Autoinhibition of Jak2 tyrosine kinase is dependent on specific regions in tis pseudokinase domain
    • P. Saharinen, M. Vihinen and O. Silvennoinen, Autoinhibition of Jak2 tyrosine kinase is dependent on specific regions in tis pseudokinase domain, Molecular Biology of the Cell 14 (2003), 1448-1459.
    • (2003) Molecular Biology of the Cell , vol.14 , pp. 1448-1459
    • Saharinen, P.1    Vihinen, M.2    Silvennoinen, O.3
  • 65
    • 0028174290 scopus 로고
    • Prolactin-induced proliferation Nb2 cells involves tyrosine phosphorylation of the prolactin receptor and its associated tyrosine kinase JAK2
    • J.J. Lebrun, S. Ali, L. Sofer, A. Ullrich and P.A. Kelly, Prolactin-induced proliferation Nb2 cells involves tyrosine phosphorylation of the prolactin receptor and its associated tyrosine kinase JAK2, J Biol Chem 269 (1994), 14021-14026.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14021-14026
    • Lebrun, J.J.1    Ali, S.2    Sofer, L.3    Ullrich, A.4    Kelly, P.A.5
  • 66
    • 0028956974 scopus 로고
    • Proline-rich sequence-mediated Jak2 association to the prolactin receptor is required but not sufficient for signal transduction
    • J-J. Lebrun, S. Ali, A. Ullrich and P.A. Kelly, Proline-rich sequence-mediated Jak2 association to the prolactin receptor is required but not sufficient for signal transduction, J Biol Chem 270 (1995), 10664-10670.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10664-10670
    • Lebrun, J.-J.1    Ali, S.2    Ullrich, A.3    Kelly, P.A.4
  • 67
    • 0030830179 scopus 로고    scopus 로고
    • Tyrosine docking sites of the rat prolactin receptor required for association and activation Stat5
    • A. Pezet, F. Ferrag, P.A. Kelly and M. Edery, Tyrosine docking sites of the rat prolactin receptor required for association and activation Stat5, J Biol Chem 272 (1997), 25043-25050.
    • (1997) J. Biol. Chem. , vol.272 , pp. 25043-25050
    • Pezet, A.1    Ferrag, F.2    Kelly, P.A.3    Edery, M.4
  • 69
    • 0032571383 scopus 로고    scopus 로고
    • Prolactin receptor regulates Stat5 tyrosine phosphorylation and nuclear translocation by two separate pathways
    • S. Ali, Prolactin receptor regulates Stat5 tyrosine phosphorylation and nuclear translocation by two separate pathways, J Biol Chem 273 (1998), 7709-7716.
    • (1998) J. Biol. Chem. , vol.273 , pp. 7709-7716
    • Ali, S.1
  • 70
    • 0031033714 scopus 로고    scopus 로고
    • Molecular characterization of specific interactions between SHP-2 phosphatase and Jak tyrosine kinases
    • T. Yin, R. Shen, G-S. Feng and Y-C. Yang, Molecular characterization of specific interactions between SHP-2 phosphatase and Jak tyrosine kinases, J Biol Chem 272 (1997), 1032-1037.
    • (1997) J. Biol. Chem. , vol.272 , pp. 1032-1037
    • Yin, T.1    Shen, R.2    Feng, G.-S.3    Yang, Y.-C.4
  • 72
    • 0035209861 scopus 로고    scopus 로고
    • Cytokine-inducible SH2-containing protein suppresses PRL signaling by binding the PRL receptor
    • F. Dif, E. Saunier, B. Demeneix, P.A. Kelly and M. Edery, Cytokine-inducible SH2-containing protein suppresses PRL signaling by binding the PRL receptor, Endocrinology 142 (2001), 5286-5293.
    • (2001) Endocrinology , vol.142 , pp. 5286-5293
    • Dif, F.1    Saunier, E.2    Demeneix, B.3    Kelly, P.A.4    Edery, M.5
  • 73
    • 0032721623 scopus 로고    scopus 로고
    • SOCS-1, -2, -3 selective targets and functions downstream of the prolactin receptor
    • S. Tomic, N. Chugtai and S. Ali, SOCS-1, -2, -3 selective targets and functions downstream of the prolactin receptor, Mol Cell Endocrinol 158 (1999), 45-54.
    • (1999) Mol. Cell Endocrinol. , vol.158 , pp. 45-54
    • Tomic, S.1    Chugtai, N.2    Ali, S.3
  • 74
    • 0033609928 scopus 로고    scopus 로고
    • Inhibition and restoration of prolactin signal transduction by suppressors of cytokine signaling
    • A. Pezet, H. Favre, P.A. Kelly and M. Edery, Inhibition and restoration of prolactin signal transduction by suppressors of cytokine signaling, J Biol Chem 274 (1999), 24497-24502.
    • (1999) J. Biol. Chem. , vol.274 , pp. 24497-24502
    • Pezet, A.1    Favre, H.2    Kelly, P.A.3    Edery, M.4
  • 78
    • 0028492201 scopus 로고
    • Protein tyrosine kinases, with emphasis on the Src family
    • S.A. Courtneidge, Protein tyrosine kinases, with emphasis on the Src family, Cancer Biology 5 (1994), 239-246.
    • (1994) Cancer Biology , vol.5 , pp. 239-246
    • Courtneidge, S.A.1
  • 79
    • 0033546315 scopus 로고    scopus 로고
    • ErbB receptor-induced activation of stat transcription factors is mediated by Src tyrosine kinases
    • M.A. Olayioye, I. Beuvink, K. Horsch, J.M. Daly and N.E. Hynes, ErbB receptor-induced activation of stat transcription factors is mediated by Src tyrosine kinases, J Biol Chem 274 (1999), 17209-17218.
    • (1999) J. Biol. Chem. , vol.274 , pp. 17209-17218
    • Olayioye, M.A.1    Beuvink, I.2    Horsch, K.3    Daly, J.M.4    Hynes, N.E.5
  • 81
    • 0033529715 scopus 로고    scopus 로고
    • Differential effects of prolactin and src/abl kinases on the nuclear translocation of STAT5B and STAT5A
    • A.B. Kazansky, E.B. Kabotyanski, S.L. Wyszomierski, M.A. Mancini and J.M. Rosen, Differential effects of prolactin and src/abl kinases on the nuclear translocation of STAT5B and STAT5A, J Biol Chem 274 (1999), 22484-22492.
    • (1999) J. Biol. Chem. , vol.274 , pp. 22484-22492
    • Kazansky, A.B.1    Kabotyanski, E.B.2    Wyszomierski, S.L.3    Mancini, M.A.4    Rosen, J.M.5
  • 82
    • 0033544961 scopus 로고    scopus 로고
    • Functional characterization of the intermediate isoform of the human prolactin receptor
    • J.B. Kline, H. Roehrs and C.V. Clevenger, Functional characterization of the intermediate isoform of the human prolactin receptor, J Biol Chem 274 (1999), 35461-35468.
    • (1999) J. Biol. Chem. , vol.274 , pp. 35461-35468
    • Kline, J.B.1    Roehrs, H.2    Clevenger, C.V.3
  • 83
    • 0030798980 scopus 로고    scopus 로고
    • Lck phosphorylates the activaiton loop tyrosine of the Itk kinase domain and activates Itk kinase activity
    • S.D. Heyeck, H.M. Wilcox, S.C. Bunnel and L.J. Berg, Lck phosphorylates the activaiton loop tyrosine of the Itk kinase domain and activates Itk kinase activity, J Biol Chem 272 (1997), 25401-25408.
    • (1997) J. Biol. Chem. , vol.272 , pp. 25401-25408
    • Heyeck, S.D.1    Wilcox, H.M.2    Bunnel, S.C.3    Berg, L.J.4
  • 84
    • 0033610868 scopus 로고    scopus 로고
    • Fyn and ZAP-70 are required for Vav phosphorylation in T cells stimulated by antigen-presenting cells
    • F. Michel, L. Grimaud, L. Tuosto and O. Acuto, Fyn and ZAP-70 are required for Vav phosphorylation in T cells stimulated by antigen-presenting cells, J Biol Chem 273 (1998), 31932-31938.
    • (1998) J. Biol. Chem. , vol.273 , pp. 31932-31938
    • Michel, F.1    Grimaud, L.2    Tuosto, L.3    Acuto, O.4
  • 85
    • 0031437959 scopus 로고    scopus 로고
    • Prolactin induced tyrosine phosphorylation of p59fyn may mediate phosphatidyinositol 3-kinase activation in Nb2 cells
    • K.A. Al-Sakkaf, P.R.M. Dobson and B.L. Brown, Prolactin induced tyrosine phosphorylation of p59fyn may mediate phosphatidyinositol 3-kinase activation in Nb2 cells, J Mol Endocrinol 19 (1997), 347-350.
    • (1997) J. Mol. Endocrinol. , vol.19 , pp. 347-350
    • Al-Sakkaf, K.A.1    Dobson, P.R.M.2    Brown, B.L.3
  • 86
    • 0033593322 scopus 로고    scopus 로고
    • Fyn associates with Cbl and phosphorylates tyrosine 731 in Cbl, a binding site for phosphatidylinositol 3-kinase
    • S. Hunter, E.A. Burton, S.C. Wu and S.M. Anderson, Fyn associates with Cbl and phosphorylates tyrosine 731 in Cbl, a binding site for phosphatidylinositol 3-kinase, J Biol Chem 274 (1999), 2097-2106.
    • (1999) J. Biol. Chem. , vol.274 , pp. 2097-2106
    • Hunter, S.1    Burton, E.A.2    Wu, S.C.3    Anderson, S.M.4
  • 87
    • 0036676540 scopus 로고    scopus 로고
    • Beyond calcium, new signaling pathways for Tec family kinases
    • A. Takesono, L.D. Finkelstein and P.L. Schwartzberg, Beyond calcium, new signaling pathways for Tec family kinases, J Cell Sci 115 (2002), 3039-3048.
    • (2002) J. Cell Sci. , vol.115 , pp. 3039-3048
    • Takesono, A.1    Finkelstein, L.D.2    Schwartzberg, P.L.3
  • 88
    • 0029086023 scopus 로고
    • Interleukin 3 and erythropoietin induce association of Vav with Tec kinase through Tec homology domain
    • M. Machide, H. Mano and K. Todokoro, Interleukin 3 and erythropoietin induce association of Vav with Tec kinase through Tec homology domain, Oncogene 11 (1995), 619-625.
    • (1995) Oncogene , vol.11 , pp. 619-625
    • Machide, M.1    Mano, H.2    Todokoro, K.3
  • 89
    • 0030926348 scopus 로고    scopus 로고
    • Tec tyrosine kinase links the cytokine receptors to PI-3 kinase probably through Jak
    • M. Takahashi, M. Hibi, M. Fujitani, T. Fukada, T. Yamaguchi and T. Hirano, Tec tyrosine kinase links the cytokine receptors to PI-3 kinase probably through Jak, Oncogene 14 (1997), 2273-2282.
    • (1997) Oncogene , vol.14 , pp. 2273-2282
    • Takahashi, M.1    Hibi, M.2    Fujitani, M.3    Fukada, T.4    Yamaguchi, T.5    Hirano, T.6
  • 90
    • 0029832590 scopus 로고    scopus 로고
    • Tec protein kinase is involved in the signaling mechanism of granulocyte colony-stimulating factor receptor
    • A. Miyazato, Y. Yamashita, K. Hatake, Y. Miura, K. Ozawa and H. Mano, Tec protein kinase is involved in the signaling mechanism of granulocyte colony-stimulating factor receptor, Cell Growth and Differentiation 7 (1996), 1135-1139.
    • (1996) Cell Growth and Differentiation , vol.7 , pp. 1135-1139
    • Miyazato, A.1    Yamashita, Y.2    Hatake, K.3    Miura, Y.4    Ozawa, K.5    Mano, H.6
  • 91
    • 0032189144 scopus 로고    scopus 로고
    • Tec/Bmx non-receptor tyrosine kinases are involved in regulation of Rho and serum response factor by Ga12/13
    • J. Mao, W. Xie, H. Yuan, M. Simon, H. Mano and D. Wu, Tec/Bmx non-receptor tyrosine kinases are involved in regulation of Rho and serum response factor by Ga12/13, EMBO J 17 (1998), 5638-5646.
    • (1998) EMBO J. , vol.17 , pp. 5638-5646
    • Mao, J.1    Xie, W.2    Yuan, H.3    Simon, M.4    Mano, H.5    Wu, D.6
  • 93
    • 0029072085 scopus 로고
    • Vav is necessary for prolactin-stimutated proliferation and is translocated into the nucleus of a T-cell line
    • C.V. Clevenger, W. Ngo, S.M. Luger and A.M. Gewirtz, Vav is necessary for prolactin-stimutated proliferation and is translocated into the nucleus of a T-cell line, J Biol Chem 270 (1995), 13246-13253.
    • (1995) J. Biol. Chem. , vol.270 , pp. 13246-13253
    • Clevenger, C.V.1    Ngo, W.2    Luger, S.M.3    Gewirtz, A.M.4
  • 94
    • 0028109973 scopus 로고
    • Tec protein kinase directly associates with Lyn protein tyrosine kinase through its N-terminal unique domain
    • H. Mano, K. Sato, Y. Yazuki and H. Hirai, Tec protein kinase directly associates with Lyn protein tyrosine kinase through its N-terminal unique domain, Oncogene 9 (1994), 3205-3211.
    • (1994) Oncogene , vol.9 , pp. 3205-3211
    • Mano, H.1    Sato, K.2    Yazuki, Y.3    Hirai, H.4
  • 97
    • 0028234529 scopus 로고
    • JAK-STAT pathways and transcriptional activation in response to IFNs and other extracellular signaling proteins
    • J.E. Darnell, I.M. Kerr and G.R. Stark, JAK-STAT pathways and transcriptional activation in response to IFNs and other extracellular signaling proteins, Science 264 (1994), 1415-1421.
    • (1994) Science , vol.264 , pp. 1415-1421
    • Darnell, J.E.1    Kerr, I.M.2    Stark, G.R.3
  • 98
    • 0035230599 scopus 로고    scopus 로고
    • Stat transcription factors in mammary gland development and tumorigenesis
    • C.J. Watson, Stat transcription factors in mammary gland development and tumorigenesis, J Mammary Gland Biol Neoplasia 6 (2001), 115-127.
    • (2001) J. Mammary Gland Biol. Neoplasia , vol.6 , pp. 115-127
    • Watson, C.J.1
  • 99
    • 0032460226 scopus 로고    scopus 로고
    • Prolactin (PRL) and its receptor, Actions, signal transduction pathways and phenotypes observed in PRL receptor knockout mice
    • C. Bole-Feysot, V. Goffin, M. Edery, N. Binart and P.A. Kelly, Prolactin (PRL) and its receptor, Actions, signal transduction pathways and phenotypes observed in PRL receptor knockout mice, Endocrine Rev 19 (1998), 225-268.
    • (1998) Endocrine Rev. , vol.19 , pp. 225-268
    • Bole-Feysot, C.1    Goffin, V.2    Edery, M.3    Binart, N.4    Kelly, P.A.5
  • 102
    • 0028923658 scopus 로고
    • Elevated levels of members of the STAT family of transcription factors in breast carcinoma nuclear extracts
    • C.J. Watson and W.R. Miller, Elevated levels of members of the STAT family of transcription factors in breast carcinoma nuclear extracts, Br J Cancer 71 (1995), 840-844.
    • (1995) Br. J. Cancer , vol.71 , pp. 840-844
    • Watson, C.J.1    Miller, W.R.2
  • 103
    • 0037124102 scopus 로고    scopus 로고
    • Autocrine-mediated activation of STAT3 correlates with cell proliferation in breast carcinoma lines
    • L. Li and P.E. Shaw, Autocrine-mediated activation of STAT3 correlates with cell proliferation in breast carcinoma lines, J Biol Chem 277 (2002), 17397-17405.
    • (2002) J. Biol. Chem. , vol.277 , pp. 17397-17405
    • Li, L.1    Shaw, P.E.2
  • 104
    • 85047698100 scopus 로고    scopus 로고
    • Inhibition of constitutively active Stat3 suppresses growth of human ovarian and breast cancer cells
    • W.M. Burke, X. Jin, H.J. Lin, M. Huang, R. Liu, R.K. Reynolds and J. Lin, Inhibition of constitutively active Stat3 suppresses growth of human ovarian and breast cancer cells, Oncogene 20 (2001), 7925-7934.
    • (2001) Oncogene , vol.20 , pp. 7925-7934
    • Burke, W.M.1    Jin, X.2    Lin, H.J.3    Huang, M.4    Liu, R.5    Reynolds, R.K.6    Lin, J.7
  • 105
    • 0346024125 scopus 로고    scopus 로고
    • Stat5a is activated and nuclear localizaed in a high proportion of human breast cancers
    • in press
    • I. Cotarla, S. Ren, Y. Zhang, E. Gehan, B. Singh and P.A. Furth, Stat5a is activated and nuclear localizaed in a high proportion of human breast cancers, Int J Cancer (2003), in press.
    • Int. J. Cancer , vol.2003
    • Cotarla, I.1    Ren, S.2    Zhang, Y.3    Gehan, E.4    Singh, B.5    Furth, P.A.6
  • 107
    • 0035141924 scopus 로고    scopus 로고
    • Signal transducers and activators of transcription 5B potentiates v-Src mediated transformation of NIH-3T3 cells
    • A.V. Kazansky and J.M. Rosen, Signal transducers and activators of transcription 5B potentiates v-Src mediated transformation of NIH-3T3 cells, Cell Growth and Differentiation 12 (2001), 1-7.
    • (2001) Cell Growth and Differentiation , vol.12 , pp. 1-7
    • Kazansky, A.V.1    Rosen, J.M.2
  • 108
    • 0037142617 scopus 로고    scopus 로고
    • Loss of Stat5a delays mammary cancer progression in a mouse model
    • S. Ren, H.R. Cai, M. Li and P.A. Furth, Loss of Stat5a delays mammary cancer progression in a mouse model, Oncogene 21 (2002), 4355-4339.
    • (2002) Oncogene , vol.21 , pp. 4339-4355
    • Ren, S.1    Cai, H.R.2    Li, M.3    Furth, P.A.4
  • 109
    • 0032577678 scopus 로고    scopus 로고
    • Crystal structure of a tyrosine phosphorylated STAT-1 dimer bound to DNA
    • X. Chen, U. Vinkemeier, Y. Zhao, D. Jerzalmi, J.E. Darnell and J. Kuriyan, Crystal structure of a tyrosine phosphorylated STAT-1 dimer bound to DNA, Cell 93 (1998), 827-839.
    • (1998) Cell , vol.93 , pp. 827-839
    • Chen, X.1    Vinkemeier, U.2    Zhao, Y.3    Jerzalmi, D.4    Darnell, J.E.5    Kuriyan, J.6
  • 110
    • 0029693897 scopus 로고    scopus 로고
    • The JAK-STAT pathway, Summary of initial studies and recent advances
    • J.E. Darnell, The JAK-STAT pathway, Summary of initial studies and recent advances, Rec Prog Horm Res 51 (1996), 391-404.
    • (1996) Rec. Prog. Horm. Res. , vol.51 , pp. 391-404
    • Darnell, J.E.1
  • 111
    • 0029655971 scopus 로고    scopus 로고
    • Function of Stat2 protein in transcriptional activation alpha interferon
    • S.A. Qureshi, S. Leung, I.M. Kerr, G.R. Stark and J.E. Darnell, Function of Stat2 protein in transcriptional activation alpha interferon, Mol Cell Biol 16 (1996), 288-293.
    • (1996) Mol. Cell Biol. , vol.16 , pp. 288-293
    • Qureshi, S.A.1    Leung, S.2    Kerr, I.M.3    Stark, G.R.4    Darnell, J.E.5
  • 112
    • 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
  • 113
    • 0029117304 scopus 로고
    • Maximal activation of transcription by Stat1 and Stat3 requires both tyrosine and serine phosphorylation
    • Z. Wen, Z. Zhong and J.E. Darnell, Maximal activation of transcription by Stat1 and Stat3 requires both tyrosine and serine phosphorylation, Cell 82 (1995), 241-250.
    • (1995) Cell , vol.82 , pp. 241-250
    • Wen, Z.1    Zhong, Z.2    Darnell, J.E.3
  • 114
    • 0032515146 scopus 로고    scopus 로고
    • Differential control of the phosphorylation state of proline-juxtaposed serine residues Ser725 of Stat5a and Ser730 of Stat5b in prolactin-sensitive cells
    • H. Yamashita, J. Xu, R.A. Erwin, W.L. Farrar, R.A. Kirken and H. Rui, Differential control of the phosphorylation state of proline-juxtaposed serine residues Ser725 of Stat5a and Ser730 of Stat5b in prolactin-sensitive cells, J Biol Chem 273 (1998), 30218-30224.
    • (1998) J. Biol. Chem. , vol.273 , pp. 30218-30224
    • Yamashita, H.1    Xu, J.2    Erwin, R.A.3    Farrar, W.L.4    Kirken, R.A.5    Rui, H.6
  • 115
    • 0038724938 scopus 로고    scopus 로고
    • Nuclear localization and function of polypeptide ligands and their receptors, A new paradigm for hormone specificity within the mammary gland?
    • C.V. Clevenger, Nuclear localization and function of polypeptide ligands and their receptors, A new paradigm for hormone specificity within the mammary gland? Breast Cancer Research 5 (2003), 181-187.
    • (2003) Breast Cancer Research , vol.5 , pp. 181-187
    • Clevenger, C.V.1
  • 116
    • 0034463072 scopus 로고    scopus 로고
    • Role of cyclophilin B in PRL signal transduction and nuclear retrotranslocation
    • M.A. Rycyzyn, S.C. Reilly, K. O'Malley and C.V. Clevenger, Role of cyclophilin B in PRL signal transduction and nuclear retrotranslocation, Mol Endocrinol 14 (2000), 1175-1186.
    • (2000) Mol. Endocrinol. , vol.14 , pp. 1175-1186
    • Rycyzyn, M.A.1    Reilly, S.C.2    O'Malley, K.3    Clevenger, C.V.4
  • 117
    • 0025609177 scopus 로고
    • Interleukin-2 driven nuclear translocation of prolactin in cloned T-lymphocytes
    • C.V. Clevenger, A.L. Sillman and M.B. Prystowsky, Interleukin-2 driven nuclear translocation of prolactin in cloned T-lymphocytes, Endocrinology 127 (1990), 3151-3159.
    • (1990) Endocrinology , vol.127 , pp. 3151-3159
    • Clevenger, C.V.1    Sillman, A.L.2    Prystowsky, M.B.3
  • 118
    • 0037076393 scopus 로고    scopus 로고
    • The intranuclear prolactin/cyclophilin B complex as a transcriptional inducer
    • M.A. Rycyzyn and C.V. Clevenger, The intranuclear prolactin/cyclophilin B complex as a transcriptional inducer, Proc Natl Acad Sci USA 99 (2002), 6790-6795.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 6790-6795
    • Rycyzyn, M.A.1    Clevenger, C.V.2


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