메뉴 건너뛰기




Volumn 20, Issue 11, 2006, Pages 2734-2746

Ligand-independent dimerization of the human prolactin receptor isoforms: Functional implications

Author keywords

[No Author keywords available]

Indexed keywords

LIGAND; PROLACTIN RECEPTOR;

EID: 33751526473     PISSN: 08888809     EISSN: 08888809     Source Type: Journal    
DOI: 10.1210/me.2006-0114     Document Type: Article
Times cited : (108)

References (57)
  • 3
    • 0025102756 scopus 로고
    • Haematopoietic receptors and helical cytokines
    • Bazan JF 1990 Haematopoietic receptors and helical cytokines. Immunol Today 11:350-354
    • (1990) Immunol Today , vol.11 , pp. 350-354
    • Bazan, J.F.1
  • 4
    • 0031930298 scopus 로고    scopus 로고
    • Stoichiometric structure/function analysis of the prolactin receptor signaling domains by receptor chimeras
    • Chang W-P, Ye Y, Clevenger CV 1998 Stoichiometric structure/function analysis of the prolactin receptor signaling domains by receptor chimeras. Mol Cell Biol 18:896-905
    • (1998) Mol Cell Biol , vol.18 , pp. 896-905
    • Chang, W.-P.1    Ye, Y.2    Clevenger, C.V.3
  • 6
    • 0027965825 scopus 로고
    • JAK2 activation and cell proliferation induced by antibody-mediated prolactin receptor dimerization
    • Rui H, Lebrun J-J, Kirken RA, Kelly PA, Farrar WL 1994 JAK2 activation and cell proliferation induced by antibody-mediated prolactin receptor dimerization. Endocrinology 135:1299-1306
    • (1994) Endocrinology , vol.135 , pp. 1299-1306
    • Rui, H.1    Lebrun, J.-J.2    Kirken, R.A.3    Kelly, P.A.4    Farrar, W.L.5
  • 7
    • 0036794307 scopus 로고    scopus 로고
    • Characterization of a novel and functional human prolactin receptor isoform (ΔS1PRLr) containing only one fibronectin-like domain
    • Kline JB, Rycyzyn MA, Clevenger CV 2002 Characterization of a novel and functional human prolactin receptor isoform (ΔS1PRLr) containing only one fibronectin-like domain. Mol Endocrinol 16:2310-2322
    • (2002) Mol Endocrinol , vol.16 , pp. 2310-2322
    • Kline, J.B.1    Rycyzyn, M.A.2    Clevenger, C.V.3
  • 8
    • 0028243306 scopus 로고
    • fyn is associated with prolactin receptor and is activated by prolactin stimulation of T-lymphocytes
    • fyn is associated with prolactin receptor and is activated by prolactin stimulation of T-lymphocytes. Mol Endocrinol 8:674-681
    • (1994) Mol Endocrinol , vol.8 , pp. 674-681
    • Clevenger, C.V.1    Medaglia, M.V.2
  • 10
    • 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
    • Goupille O, Daniel N, Bignon C, Jolivet J, Djiane J 1997 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 127:155-169
    • (1997) Mol Endocrinol , vol.127 , pp. 155-169
    • Goupille, O.1    Daniel, N.2    Bignon, C.3    Jolivet, J.4    Djiane, J.5
  • 11
    • 0028059104 scopus 로고
    • Prolactin induces rapid phosphorylation and activation of prolactin receptor associated Raf-1 kinase in a T-cell line
    • Clevenger CV, Torigoe T, Reed JC 1994 Prolactin induces rapid phosphorylation and activation of prolactin receptor associated Raf-1 kinase in a T-cell line. J Biol Chem 269:5559-5565
    • (1994) J Biol Chem , vol.269 , pp. 5559-5565
    • Clevenger, C.V.1    Torigoe, T.2    Reed, J.C.3
  • 12
    • 0029112369 scopus 로고
    • Prolactin activates Ras via signaling proteins SHC, growth factor receptor bound 2, and son of sevenless
    • Erwin RA, Kirken RA, Malbarba MG, Farrar WL, Rui H 1995 Prolactin activates Ras via signaling proteins SHC, growth factor receptor bound 2, and son of sevenless. Endocrinology 136:3512-3518
    • (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
  • 13
    • 0029770041 scopus 로고    scopus 로고
    • Crystal structure of an antagonist mutant of the human growth hormone, G120R, in complex with its receptor at 2.9 A resolution
    • Sundstrom M, Lundqvist T, Rodin J, Giebel LB, MIlligan D, Norstedt G 1996 Crystal structure of an antagonist mutant of the human growth hormone, G120R, in complex with its receptor at 2.9 A resolution. J Biol Chem 271:32197-32203
    • (1996) J Biol Chem , vol.271 , pp. 32197-32203
    • Sundstrom, M.1    Lundqvist, T.2    Rodin, J.3    Giebel, L.B.4    Milligan, D.5    Norstedt, G.6
  • 14
    • 0029072085 scopus 로고
    • Vav is necessary for prolactin-stimulated proliferation and is translocated into the nucleus of a T-cell line
    • Clevenger CV, Ngo W, Luger SM, Gewirtz AM 1995 Vav is necessary for prolactin-stimulated proliferation and is translocated into the nucleus of a T-cell line. J Biol Chem 270:13246-13253
    • (1995) J Biol Chem , vol.270 , pp. 13246-13253
    • Clevenger, C.V.1    Ngo, W.2    Luger, S.M.3    Gewirtz, A.M.4
  • 15
    • 0030893637 scopus 로고    scopus 로고
    • Role of Bag-1 in the survival and proliferation of the cytokine-dependent lymphocyte lines, Ba/F3 and Nb2
    • Clevenger CV, Thickman K, Ngo W, Chang W-P, Takayama S, Reed JC 1997 Role of Bag-1 in the survival and proliferation of the cytokine-dependent lymphocyte lines, Ba/F3 and Nb2. Mol Endocrinol 11:608-618
    • (1997) Mol Endocrinol , vol.11 , pp. 608-618
    • Clevenger, C.V.1    Thickman, K.2    Ngo, W.3    Chang, W.-P.4    Takayama, S.5    Reed, J.C.6
  • 16
    • 0026749173 scopus 로고
    • Requirement for prolactin during cell cycle regulated gene expression in cloned T-lymphocytes
    • Clevenger CV, Sillman AL, Hanley-Hyde J, Prystowsky MB 1992 Requirement for prolactin during cell cycle regulated gene expression in cloned T-lymphocytes. Endocrinol 130:3216-3222
    • (1992) Endocrinol , vol.130 , pp. 3216-3222
    • Clevenger, C.V.1    Sillman, A.L.2    Hanley-Hyde, J.3    Prystowsky, M.B.4
  • 17
    • 0025190187 scopus 로고
    • Prolactin stimulates transcription of growth-related genes in Nb2 T lymphoma cells
    • Yu-Lee L-Y 1990 Prolactin stimulates transcription of growth-related genes in Nb2 T lymphoma cells. Mol Cell Endocrinol 68:21-28
    • (1990) Mol Cell Endocrinol , vol.68 , pp. 21-28
    • Yu-Lee, L.-Y.1
  • 18
    • 0029989302 scopus 로고    scopus 로고
    • Growth hormone and a GH antogonist promote GH receptor dimerization and internalization
    • Harding P, Wang X, Okada S, Chen WY, Wan W, Kopchick JJ 1996 Growth hormone and a GH antogonist promote GH receptor dimerization and internalization. Bioessays 271:6708-6712
    • (1996) Bioessays , vol.271 , pp. 6708-6712
    • Harding, P.1    Wang, X.2    Okada, S.3    Chen, W.Y.4    Wan, W.5    Kopchick, J.J.6
  • 20
    • 0025162844 scopus 로고
    • Structural design and molecular evolution of a cytokine receptor superfamily
    • Bazan JF 1990 Structural design and molecular evolution of a cytokine receptor superfamily. Proc Natl Acad Sci USA 87:6934-6938
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 6934-6938
    • Bazan, J.F.1
  • 21
    • 0033544961 scopus 로고    scopus 로고
    • Functional characterization of the intermediate isoform of the human prolactin receptor
    • Kline JB, Roehrs H, Clevenger CV 1999 Functional characterization of the intermediate isoform of the human prolactin receptor. J Biol Chem 274:35461-35468
    • (1999) J Biol Chem , vol.274 , pp. 35461-35468
    • Kline, J.B.1    Roehrs, H.2    Clevenger, C.V.3
  • 22
    • 0033543571 scopus 로고    scopus 로고
    • Biological properties of human prolactin analogs depend not only on global hormone affinity, but also on the relative affinities of both receptor binding sites
    • Kinet S, Bernichtein S, Kelly PA, Martial JA, Goffin V 1999 Biological properties of human prolactin analogs depend not only on global hormone affinity, but also on the relative affinities of both receptor binding sites. J Biol Chem 274:16033-26043
    • (1999) J Biol Chem , vol.274 , pp. 16033-26043
    • Kinet, S.1    Bernichtein, S.2    Kelly, P.A.3    Martial, J.A.4    Goffin, V.5
  • 23
    • 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
    • Hu Z, Meng J, Dufau ML 2001 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 276:41086-41094
    • (2001) J Biol Chem , vol.276 , pp. 41086-41094
    • Hu, Z.1    Meng, J.2    Dufau, M.L.3
  • 24
    • 0037294370 scopus 로고    scopus 로고
    • Alternative splicing to exon 11 of human prolactin receptor gene results in multiple isoforms including a secreted prolactin-binding protein
    • Trott JF, Hovey RC, Koduri S, Vonderhaar BK 2003 Alternative splicing to exon 11 of human prolactin receptor gene results in multiple isoforms including a secreted prolactin-binding protein. J Mol Endocrinol 30:31-47
    • (2003) J Mol Endocrinol , vol.30 , pp. 31-47
    • Trott, J.F.1    Hovey, R.C.2    Koduri, S.3    Vonderhaar, B.K.4
  • 25
    • 17644413692 scopus 로고    scopus 로고
    • Unmodified prolactin (PRL) and S179D Prl-initiated bioluminescence resonance energy transfer between homo - And hetero - pairs of long and short human PRL receptors in living human cells
    • Tan D, Johnson DA, Wu W, Zeng L, Chen YH, Chen WY, Vonderhaar BK, Walker AM 2005 Unmodified prolactin (PRL) and S179D Prl-initiated bioluminescence resonance energy transfer between homo - and hetero - pairs of long and short human PRL receptors in living human cells. Mol Endocrinol 19:1291-1303
    • (2005) Mol Endocrinol , vol.19 , pp. 1291-1303
    • Tan, D.1    Johnson, D.A.2    Wu, W.3    Zeng, L.4    Chen, Y.H.5    Chen, W.Y.6    Vonderhaar, B.K.7    Walker, A.M.8
  • 26
    • 0035816689 scopus 로고    scopus 로고
    • Identification and characterization of the prolactin-binding protein (PRLBP) in human serum and milk
    • Kline JB, Clevenger CV 2001 Identification and characterization of the prolactin-binding protein (PRLBP) in human serum and milk. J Biol Chem 276:24760-24766
    • (2001) J Biol Chem , vol.276 , pp. 24760-24766
    • Kline, J.B.1    Clevenger, C.V.2
  • 27
    • 26644471035 scopus 로고    scopus 로고
    • Proteasomes mediate prolactin-induced receptor down-regulation and fragment generation in breast cancer cells
    • Lu JC, Piazza TM, Schuler LA 2005 Proteasomes mediate prolactin-induced receptor down-regulation and fragment generation in breast cancer cells. J Biol Chem 280:33909-33916
    • (2005) J Biol Chem , vol.280 , pp. 33909-33916
    • Lu, J.C.1    Piazza, T.M.2    Schuler, L.A.3
  • 29
    • 0027412707 scopus 로고
    • Evidence for generation of the growth hormone-binding protein through proteolysis of the growth hormone membrane receptor
    • Sotiropoulos A, Goujon L, Simonin G, Kelly PA, Postel-Vinay MC, Finidori J 1993 Evidence for generation of the growth hormone-binding protein through proteolysis of the growth hormone membrane receptor. Endocrinology 132:1863-1865
    • (1993) Endocrinology , vol.132 , pp. 1863-1865
    • Sotiropoulos, A.1    Goujon, L.2    Simonin, G.3    Kelly, P.A.4    Postel-Vinay, M.C.5    Finidori, J.6
  • 31
    • 0034520154 scopus 로고    scopus 로고
    • Tumor necrosis factor-α converting enzyme (TACE) is a growth hormone binding protein (GHBP) sheddase: The metalloprotease TACE/ADAM-17 is critical for (PMA-induced) GH receptor proteolysis and GHBP generation
    • Zhang Y, Jiang J, Black RA, Baumann G, Frank SJ 2000 Tumor necrosis factor-α converting enzyme (TACE) is a growth hormone binding protein (GHBP) sheddase: the metalloprotease TACE/ADAM-17 is critical for (PMA-induced) GH receptor proteolysis and GHBP generation. Endocrinology 141:4342-4348
    • (2000) Endocrinology , vol.141 , pp. 4342-4348
    • Zhang, Y.1    Jiang, J.2    Black, R.A.3    Baumann, G.4    Frank, S.J.5
  • 33
    • 0028032203 scopus 로고
    • The X-ray structure of a growth hormone-prolactin receptor complex
    • Somers W, Ultsch M, de Vos AM, Kossiakoff AA 1994 The X-ray structure of a growth hormone-prolactin receptor complex. Nature 372:478-481
    • (1994) Nature , vol.372 , pp. 478-481
    • Somers, W.1    Ultsch, M.2    De Vos, A.M.3    Kossiakoff, A.A.4
  • 34
    • 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
    • Gertler A, Grosclaude J, Strasburger CJ, Nir S, Djiane J 1996 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 271:24482-24491
    • (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
  • 35
    • 0026332810 scopus 로고
    • Dimerization of the extracellular domain of the human growth hormone receptor by a single hormone molecule
    • Cunningham BC, Ultsch M, DeVoss AM, Mulkerrin MG, Clauser KR, Wells JA 1991 Dimerization of the extracellular domain of the human growth hormone receptor by a single hormone molecule. Science 254:821-825
    • (1991) Science , vol.254 , pp. 821-825
    • Cunningham, B.C.1    Ultsch, M.2    DeVoss, A.M.3    Mulkerrin, M.G.4    Clauser, K.R.5    Wells, J.A.6
  • 36
    • 0035040522 scopus 로고    scopus 로고
    • Binding and functional studies with the growth hormone receptor antagonist B2036-PEG (Pegvisomant), reveal effects of pegylation and evidence that it binds to a receptor dimer
    • Ross RJM, Leung KC, Maamra M, Bennett W, Doyle N, Waters MJ, Ho KKY 2001 Binding and functional studies with the growth hormone receptor antagonist B2036-PEG (Pegvisomant), reveal effects of pegylation and evidence that it binds to a receptor dimer. J Clin Endocrinol Metab 86:1716-1723
    • (2001) J Clin Endocrinol Metab , vol.86 , pp. 1716-1723
    • Ross, R.J.M.1    Leung, K.C.2    Maamra, M.3    Bennett, W.4    Doyle, N.5    Waters, M.J.6    Ho, K.K.Y.7
  • 37
    • 0037162458 scopus 로고    scopus 로고
    • Ligand-independent growth hormone receptor dimerization occurs in the endoplasmic reticulum and is required for ubiquitin system-dependent endocytosis
    • Gent J, van Kerkhof P, Roza M, Bu G, Strous GJ 2002 Ligand-independent growth hormone receptor dimerization occurs in the endoplasmic reticulum and is required for ubiquitin system-dependent endocytosis. Proc Natl Acad Sci USA 100:6
    • (2002) Proc Natl Acad Sci USA , vol.100 , pp. 6
    • Gent, J.1    Van Kerkhof, P.2    Roza, M.3    Bu, G.4    Strous, G.J.5
  • 39
    • 0033548259 scopus 로고    scopus 로고
    • Crystallographic evidence for preformed dimers of erythropoietin receptor before ligand activation
    • Livnah O, Stura EA, Middleton SA, Johnson DL, Joliffe LK, Wilson IA 1999 Crystallographic evidence for preformed dimers of erythropoietin receptor before ligand activation. Science 283:987-990
    • (1999) Science , vol.283 , pp. 987-990
    • Livnah, O.1    Stura, E.A.2    Middleton, S.A.3    Johnson, D.L.4    Joliffe, L.K.5    Wilson, I.A.6
  • 41
    • 0035102191 scopus 로고    scopus 로고
    • The erythropoietin receptor cytosolic juxtamembrane domain contains an essential, precisely oriented, hydrophobic motif
    • Constantinescu SN, Huang L-S, Nam H-S, Lodish HF 2001 The erythropoietin receptor cytosolic juxtamembrane domain contains an essential, precisely oriented, hydrophobic motif. Mol Cell 7:377-385
    • (2001) Mol Cell , vol.7 , pp. 377-385
    • Constantinescu, S.N.1    Huang, L.-S.2    Nam, H.-S.3    Lodish, H.F.4
  • 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
    • Kline JB, Moore DJ, Clevenger CV 2001 Activation and association of the Tec tyrosine kinase with the human prolactin receptor: mapping of a Tec/Vav1-receptor binding site. Mol Endocrinol 15:832-841
    • (2001) Mol Endocrinol , vol.15 , pp. 832-841
    • Kline, J.B.1    Moore, D.J.2    Clevenger, C.V.3
  • 44
    • 0028963516 scopus 로고
    • Expression of prolactin and prolactin receptor in human breast carcinoma. Evidence for an autocrine/paracrine loop
    • Clevenger CV, Chang WP, Ngo W, Pasha TL, Montone KT, Tomaszewski JE 1995 Expression of prolactin and prolactin receptor in human breast carcinoma. Evidence for an autocrine/paracrine loop. Am J Pathol 146:695-705
    • (1995) Am J Pathol , vol.146 , pp. 695-705
    • Clevenger, C.V.1    Chang, W.P.2    Ngo, W.3    Pasha, T.L.4    Montone, K.T.5    Tomaszewski, J.E.6
  • 45
    • 0030754999 scopus 로고    scopus 로고
    • The short form of the prolactin (PRL) receptor silences PRL induction of the beta-casein gene promoter
    • Berlanga JJ, Garcia-Ruiz JP, Perrot-Applanat M, Kelly PA, Edery M 1997 The short form of the prolactin (PRL) receptor silences PRL induction of the beta-casein gene promoter. Mol Endocrinol 11:1448-1457
    • (1997) Mol Endocrinol , vol.11 , pp. 1448-1457
    • Berlanga, J.J.1    Garcia-Ruiz, J.P.2    Perrot-Applanat, M.3    Kelly, P.A.4    Edery, M.5
  • 46
    • 2342516767 scopus 로고    scopus 로고
    • A mutant receptor with enhanced dominant-negative activity for the blockade of human prolactin signaling
    • Flynn A, Whittington V, Goffin V, Uney J, Norman M 2004 A mutant receptor with enhanced dominant-negative activity for the blockade of human prolactin signaling. J Mol Endocrinol 32:385-396
    • (2004) J Mol Endocrinol , vol.32 , pp. 385-396
    • Flynn, A.1    Whittington, V.2    Goffin, V.3    Uney, J.4    Norman, M.5
  • 47
    • 0942276402 scopus 로고    scopus 로고
    • The interface between self-assembling erythropoietin receptor transmembrane segments corresponds to a membrane-spanning leucine zipper
    • Ruan W, Becker V, Klingmuller U, Langosch D 2004 The interface between self-assembling erythropoietin receptor transmembrane segments corresponds to a membrane-spanning leucine zipper. J Biol Chem 279:3273-3279
    • (2004) J Biol Chem , vol.279 , pp. 3273-3279
    • Ruan, W.1    Becker, V.2    Klingmuller, U.3    Langosch, D.4
  • 48
    • 0037085373 scopus 로고    scopus 로고
    • The single transmembrane domains of ErbB receptors self-associate in cell membranes
    • Mendrola JM, Berger MB, King MC, Lemmon MA 2002 The single transmembrane domains of ErbB receptors self-associate in cell membranes. J Biol Chem 277:4704-4712
    • (2002) J Biol Chem , vol.277 , pp. 4704-4712
    • Mendrola, J.M.1    Berger, M.B.2    King, M.C.3    Lemmon, M.A.4
  • 49
    • 0036320471 scopus 로고    scopus 로고
    • Ligand-independent dimer formation of epidermal growth factor receptor (EGFR) is a step separable from ligand-induced EGFR signaling
    • Yu X, Sharma KD, Takahashi T, Iwamoto R, Mekada E 2002 Ligand-independent dimer formation of epidermal growth factor receptor (EGFR) is a step separable from ligand-induced EGFR signaling. Mol Biol Cell 13:2547-2557
    • (2002) Mol Biol Cell , vol.13 , pp. 2547-2557
    • Yu, X.1    Sharma, K.D.2    Takahashi, T.3    Iwamoto, R.4    Mekada, E.5
  • 50
    • 0026598960 scopus 로고
    • Human growth hormone and extracellular domain of its receptor: Crystal structure of the complex
    • de Vos AM, Ultsch M, Kossiakoff AA 1992 Human growth hormone and extracellular domain of its receptor: Crystal structure of the complex. Science 255:306-312
    • (1992) Science , vol.255 , pp. 306-312
    • De Vos, A.M.1    Ultsch, M.2    Kossiakoff, A.A.3
  • 51
    • 0032540358 scopus 로고    scopus 로고
    • Structural and functional analysis of the 1:1 growth hormone: Receptor complex reveals the molecular basis for receptor affinity
    • Clackson T, Ultsch M, Well JA, de Vos AM 1998 Structural and functional analysis of the 1:1 growth hormone: receptor complex reveals the molecular basis for receptor affinity. J Mol Biol 277:1111-1128
    • (1998) J Mol Biol , vol.277 , pp. 1111-1128
    • Clackson, T.1    Ultsch, M.2    Well, J.A.3    De Vos, A.M.4
  • 52
    • 33746606004 scopus 로고    scopus 로고
    • Ligand-independent homo- And hetero- dimerization of the human prolactin receptor variants: Inhibitory action of the short forms by heterodimerization
    • 23 March 10.1210/me. 2005-0291
    • Qazi AM, Tsai-Morris CH, Dufau ML 23 March 2006 Ligand-independent homo- and hetero- dimerization of the human prolactin receptor variants: inhibitory action of the short forms by heterodimerization. Mol Endocrinol 10.1210/me. 2005-0291
    • (2006) Mol Endocrinol
    • Qazi, A.M.1    Tsai-Morris, C.H.2    Dufau, M.L.3
  • 53
    • 0042315351 scopus 로고    scopus 로고
    • Ovine placental lactogen-induced heterodimerization of ovine growth hormone and prolactin receptors in living cells is demonstrated by fluorescence resonance energy transfer microscopy and leads to prolonged phosphorylation of signal transducer and activator of transcription (STAT) 1 and STAT3
    • Biener E, Martin C, Daniel N, Frank SJ, Centonze VE, Herman B, Djiane J, Gertler A 2003 Ovine placental lactogen-induced heterodimerization of ovine growth hormone and prolactin receptors in living cells is demonstrated by fluorescence resonance energy transfer microscopy and leads to prolonged phosphorylation of signal transducer and activator of transcription (STAT) 1 and STAT3. Endocrinology 144:3532-3540
    • (2003) Endocrinology , vol.144 , pp. 3532-3540
    • Biener, E.1    Martin, C.2    Daniel, N.3    Frank, S.J.4    Centonze, V.E.5    Herman, B.6    Djiane, J.7    Gertler, A.8
  • 54
    • 0030013232 scopus 로고    scopus 로고
    • Modulation of growth factor receptor function by isoform heterodimerization
    • Chang WP, Clevenger CV 1996 Modulation of growth factor receptor function by isoform heterodimerization. Proc Natl Acad Sci USA 93:5947-5952
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 5947-5952
    • Chang, W.P.1    Clevenger, C.V.2
  • 55
    • 33751542181 scopus 로고    scopus 로고
    • A human prolactin antagonist, hPRL-G129R, inhibits breast cancer cell proliferation
    • Chen WY, Ramamoorthy P, Chen N-Y, Sticca R, Wagner TE 1999 A human prolactin antagonist, hPRL-G129R, inhibits breast cancer cell proliferation Int J Oncol 17:1179-1185
    • (1999) Int J Oncol , vol.17 , pp. 1179-1185
    • Chen, W.Y.1    Ramamoorthy, P.2    Chen, N.-Y.3    Sticca, R.4    Wagner, T.E.5
  • 57
    • 0037076393 scopus 로고    scopus 로고
    • The intranuclear prolactin/ cyclophilin B complex as a transcriptional inducer
    • Rycyzyn MA, Clevenger CV 2002 The intranuclear prolactin/ cyclophilin B complex as a transcriptional inducer. Proc Natl Acad Sci USA 99:6790-6795
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 6790-6795
    • Rycyzyn, M.A.1    Clevenger, C.V.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.