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Volumn 24, Issue 2-3, 1998, Pages 120-130

TGF-β receptors and signalling mechanisms

Author keywords

MAD related proteins; Signal transduction; Smad; TGF

Indexed keywords

ACTIVIN; BONE MORPHOGENETIC PROTEIN; CELL SURFACE RECEPTOR; LIGAND; MEMBRANE PROTEIN; PROTEIN SERINE THREONINE KINASE; RECEPTOR; RECEPTOR SUBTYPE; TRANSCRIPTION FACTOR; TRANSFORMING GROWTH FACTOR BETA; TRANSFORMING GROWTH FACTOR BETA RECEPTOR;

EID: 0031884680     PISSN: 03780392     EISSN: None     Source Type: Journal    
DOI: 10.1159/000057359     Document Type: Review
Times cited : (86)

References (85)
  • 1
    • 0030613249 scopus 로고    scopus 로고
    • TβRI phosphorylation of Smad2 on Ser 465 and 467 is required for Smad2/Smad4 complex formation and signalling
    • in press
    • Abdollah S, Macías-Silva M, Tsukazaki T, Hayashi H, Attisano L, Wrana JL: TβRI phosphorylation of Smad2 on Ser 465 and 467 is required for Smad2/Smad4 complex formation and signalling. J Biol Chem 1997, in press.
    • (1997) J Biol Chem
    • Abdollah, S.1    Macías-Silva, M.2    Tsukazaki, T.3    Hayashi, H.4    Attisano, L.5    Wrana, J.L.6
  • 2
    • 0029072998 scopus 로고
    • The Drosophila schnurri gene acts in the dpp/TGF-β signaling pathway and encodes a transcription factor homologous to the human MBP family
    • Arora K, Dai H, Kazuko SG, Jamal J, O'Connor MB, Letsou A, Warrior R: The Drosophila schnurri gene acts in the dpp/TGF-β signaling pathway and encodes a transcription factor homologous to the human MBP family. Cell 1995;81:781-790.
    • (1995) Cell , vol.81 , pp. 781-790
    • Arora, K.1    Dai, H.2    Kazuko, S.G.3    Jamal, J.4    O'Connor, M.B.5    Letsou, A.6    Warrior, R.7
  • 3
    • 0030427867 scopus 로고    scopus 로고
    • Signal transduction by members of the transforming growth factor-β superfamily
    • Attisano L, Wrana JL: Signal transduction by members of the transforming growth factor-β superfamily. Cytokine Growth Factor Rev 1996;7:327-339.
    • (1996) Cytokine Growth Factor Rev , vol.7 , pp. 327-339
    • Attisano, L.1    Wrana, J.L.2
  • 6
    • 0029829230 scopus 로고    scopus 로고
    • A novel mesoderm inducer, Madr2, functions in the activin signal transduction pathway
    • Baker JC, Harland R: A novel mesoderm inducer, Madr2, functions in the activin signal transduction pathway. Genes Dev 1996;10:1880-1889.
    • (1996) Genes Dev , vol.10 , pp. 1880-1889
    • Baker, J.C.1    Harland, R.2
  • 9
    • 0028937160 scopus 로고
    • Biochemical evidence for the autophosphorylation and transphosphorylation of transforming growth factor β receptor kinases
    • Chen F, Weinberg RA: Biochemical evidence for the autophosphorylation and transphosphorylation of transforming growth factor β receptor kinases. Proc Natl Acad Sci USA 1995;92: 1565-1569.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 1565-1569
    • Chen, F.1    Weinberg, R.A.2
  • 10
    • 0029802485 scopus 로고    scopus 로고
    • A transcriptional partner for MAD proteins in TGF-β signalling
    • Chen X, Rubock MJ, Whitman M: A transcriptional partner for MAD proteins in TGF-β signalling. Nature 1996;383:691-696.
    • (1996) Nature , vol.383 , pp. 691-696
    • Chen, X.1    Rubock, M.J.2    Whitman, M.3
  • 11
    • 0029806078 scopus 로고    scopus 로고
    • Regulation of transforming growth factor β- And activin-induced transcription by mammalian Mad proteins
    • Chen Y, Lebrun J-J, Vale W: Regulation of transforming growth factor β- and activin-induced transcription by mammalian Mad proteins. Proc Natl Acad Sci USA 1998;93:12992-12997.
    • (1998) Proc Natl Acad Sci USA , vol.93 , pp. 12992-12997
    • Chen, Y.1    Lebrun, J.-J.2    Vale, W.3
  • 14
    • 0030897846 scopus 로고    scopus 로고
    • A CREB-binding site as a target for decapentaplegic signalling during Drosophila endoderm induction
    • Eresh S, Riese J, Jackson DB, Bohmann D, Bienz M: A CREB-binding site as a target for decapentaplegic signalling during Drosophila endoderm induction. EMBO J 1997;16:2014-2022.
    • (1997) EMBO J , vol.16 , pp. 2014-2022
    • Eresh, S.1    Riese, J.2    Jackson, D.B.3    Bohmann, D.4    Bienz, M.5
  • 15
    • 0030926005 scopus 로고    scopus 로고
    • A kinase subdomain of transforming growth factor-β (TGF-S) type 1 receptor determines the TGF-β intracellular signaling specificity
    • Feng X-H, Derynck R: A kinase subdomain of transforming growth factor-β (TGF-S) type 1 receptor determines the TGF-β intracellular signaling specificity. EMBO J 1997;16:3912-3923.
    • (1997) EMBO J , vol.16 , pp. 3912-3923
    • Feng, X.-H.1    Derynck, R.2
  • 16
    • 0029114477 scopus 로고
    • Missense mutations of the transforming growth factor β type II receptor in human head and neck squamous carcinoma cells
    • Garrigue-Antar L, Muñoz-Antonia T, Antonia SJ, Gesmonde J, Vellucci VF, Reiss M: Missense mutations of the transforming growth factor β type II receptor in human head and neck squamous carcinoma cells. Cancer Res 1995;55: 3982-3987.
    • (1995) Cancer Res , vol.55 , pp. 3982-3987
    • Garrigue-Antar, L.1    Muñoz-Antonia, T.2    Antonia, S.J.3    Gesmonde, J.4    Vellucci, V.F.5    Reiss, M.6
  • 17
    • 0023732890 scopus 로고
    • Molecular events in the processing of recombinant type I pre-pro-transforming growth factor beta to the mature polypeptide
    • Gentry LE, Liobin MN, Purchio AF, Marquardt H: Molecular events in the processing of recombinant type I pre-pro-transforming growth factor beta to the mature polypeptide. Mol Cell Biol 1988;8:4162-4168.
    • (1988) Mol Cell Biol , vol.8 , pp. 4162-4168
    • Gentry, L.E.1    Liobin, M.N.2    Purchio, A.F.3    Marquardt, H.4
  • 18
    • 0029940972 scopus 로고    scopus 로고
    • Xenopus Mad proteins transduce distinct subsets of signals for the TGF-β superfamily
    • Graff JM, Bansal A, Melton DA: Xenopus Mad proteins transduce distinct subsets of signals for the TGF-β superfamily. Cell 1996;85:479-487.
    • (1996) Cell , vol.85 , pp. 479-487
    • Graff, J.M.1    Bansal, A.2    Melton, D.A.3
  • 19
    • 0028990126 scopus 로고
    • Schnurri is required for Drosophila dpp signalling and encodes a zinc finger protein similar to the mammalian transcription factor PRDII-BF1
    • Grieder NC, Nellen D, Burke R, Basler K, Affolter M: schnurri is required for Drosophila dpp signalling and encodes a zinc finger protein similar to the mammalian transcription factor PRDII-BF1. Cell 1995;81:791-800.
    • (1995) Cell , vol.81 , pp. 791-800
    • Grieder, N.C.1    Nellen, D.2    Burke, R.3    Basler, K.4    Affolter, M.5
  • 21
    • 0030825516 scopus 로고    scopus 로고
    • Mutations increasing autoinhibition inactive tumour suppressors Smad2 and Smad4
    • Hata A, Lo RS, Wotton D, Lagna G, Massagué J: Mutations increasing autoinhibition inactive tumour suppressors Smad2 and Smad4. Nature 1997;388:82-87.
    • (1997) Nature , vol.388 , pp. 82-87
    • Hata, A.1    Lo, R.S.2    Wotton, D.3    Lagna, G.4    Massagué, J.5
  • 24
    • 0028792328 scopus 로고
    • Identification of a potential regulator of early transcriptional responses to mesoderm inducer in the frog embryo
    • Huang H-C, Murtaugh LC, Vize PD, Whitman M: Identification of a potential regulator of early transcriptional responses to mesoderm inducer in the frog embryo. EMBO J 1995;14:5965-5973.
    • (1995) EMBO J , vol.14 , pp. 5965-5973
    • Huang, H.-C.1    Murtaugh, L.C.2    Vize, P.D.3    Whitman, M.4
  • 26
    • 0030872367 scopus 로고    scopus 로고
    • Drosophila Mad binds to DNA and directly mediates activation of vestigial by decapentaplegic
    • Kim J, Johnson K, Chen HJ, Carroll S, Laughon A: Drosophila Mad binds to DNA and directly mediates activation of vestigial by decapentaplegic. Nature 1997;388:304-305.
    • (1997) Nature , vol.388 , pp. 304-305
    • Kim, J.1    Johnson, K.2    Chen, H.J.3    Carroll, S.4    Laughon, A.5
  • 27
    • 0030592517 scopus 로고    scopus 로고
    • Lessons from hereditary colorectal cancer
    • Kinzler KW, Vogelstein B: Lessons from hereditary colorectal cancer. Cell 1996;87:159-170.
    • (1996) Cell , vol.87 , pp. 159-170
    • Kinzler, K.W.1    Vogelstein, B.2
  • 28
    • 0030911104 scopus 로고    scopus 로고
    • The TGF-β family mediator Smad1 is phosphorylated directly and activated functionally by the BMP receptor kinase
    • Kretzchmar M, Liu F, Hata A, Doody J, Massagué J: The TGF-β family mediator Smad1 is phosphorylated directly and activated functionally by the BMP receptor kinase. Genes Dev 1997; 11:984-995.
    • (1997) Genes Dev , vol.11 , pp. 984-995
    • Kretzchmar, M.1    Liu, F.2    Hata, A.3    Doody, J.4    Massagué, J.5
  • 29
    • 0029834067 scopus 로고    scopus 로고
    • Partnership between DPC4 and SMAD proteins in TGF-β signalling pathways
    • Lagna G, Hata A, Hemmati-Brivanlou A, Massagué J: Partnership between DPC4 and SMAD proteins in TGF-β signalling pathways. Nature 1996;383:832-836.
    • (1996) Nature , vol.383 , pp. 832-836
    • Lagna, G.1    Hata, A.2    Hemmati-Brivanlou, A.3    Massagué, J.4
  • 31
    • 0030013242 scopus 로고    scopus 로고
    • Serine phosphorylation, chromosomal localization and transforming growth factor-β signal transduction by human bsp-1
    • Lechleider R, de Caestecker MP, Dehejia A, Polymeropoulos MH, Roberts AB: Serine phosphorylation, chromosomal localization and transforming growth factor-β signal transduction by human bsp-1. J Biol Chem 1996;271: 17617-17620.
    • (1996) J Biol Chem , vol.271 , pp. 17617-17620
    • Lechleider, R.1    De Caestecker, M.P.2    Dehejia, A.3    Polymeropoulos, M.H.4    Roberts, A.B.5
  • 33
    • 0028878041 scopus 로고
    • The soluble exoplasmic domain of the type II transforming growth factor (TGF)-β receptor: A heterogeneously glycosylated protein with high affinity and selectivity for TGF-β ligands
    • Lin HY, Moustakas A, Knaus P, Wells RG, Henis YI, Lodish HF: The soluble exoplasmic domain of the type II transforming growth factor (TGF)-β receptor: A heterogeneously glycosylated protein with high affinity and selectivity for TGF-β ligands. J Biol Chem 1995;270: 2747-2754.
    • (1995) J Biol Chem , vol.270 , pp. 2747-2754
    • Lin, H.Y.1    Moustakas, A.2    Knaus, P.3    Wells, R.G.4    Henis, Y.I.5    Lodish, H.F.6
  • 35
    • 0029008597 scopus 로고
    • Human type II receptor for bone morphogenetic proteins (BMPs): Extension of the two-kinase receptor model to the BMPs
    • Liu F, Ventura F, Doody J, Massagué J: Human type II receptor for bone morphogenetic proteins (BMPs): Extension of the two-kinase receptor model to the BMPs. Mold Cell Biol 1995;15:3479-3486.
    • (1995) Mold Cell Biol , vol.15 , pp. 3479-3486
    • Liu, F.1    Ventura, F.2    Doody, J.3    Massagué, J.4
  • 36
    • 0027276765 scopus 로고
    • Beta-glycan presents ligand to the TGF-β signaling receptor
    • López-Casillas F, Wrana JL, Massagué J: Beta-glycan presents ligand to the TGF-β signaling receptor. Cell 1993;73:1435-1444.
    • (1993) Cell , vol.73 , pp. 1435-1444
    • López-Casillas, F.1    Wrana, J.L.2    Massagué, J.3
  • 37
    • 0029792338 scopus 로고    scopus 로고
    • Signaling by chimeric erythropoietin-TGF-β receptors: Homodimerization of the cytoplasmic domain of the type I TGF-β receptor and heterodimerization with the type II receptor are both required for intracellular signal transduction
    • Luo K, Lodish JF: Signaling by chimeric erythropoietin-TGF-β receptors: Homodimerization of the cytoplasmic domain of the type I TGF-β receptor and heterodimerization with the type II receptor are both required for intracellular signal transduction. EMBO J 1996;15:4485-4496.
    • (1996) EMBO J , vol.15 , pp. 4485-4496
    • Luo, K.1    Lodish, J.F.2
  • 38
    • 0030972496 scopus 로고    scopus 로고
    • Positive and negative regulation of type II TGF-β receptor signal tranduction by autophosphorylation on multiple serine residues
    • Luo K, Lodish HF: Positive and negative regulation of type II TGF-β receptor signal tranduction by autophosphorylation on multiple serine residues. EMBO J 1997;16:1970-1981.
    • (1997) EMBO J , vol.16 , pp. 1970-1981
    • Luo, K.1    Lodish, H.F.2
  • 39
    • 0030300115 scopus 로고    scopus 로고
    • MADR2 is a substrate of the TGF-β receptor and its phosphorylation is required for nuclear accumulation and signalling
    • Macías-Silva M, Abdollah S, Hoodless PA, Pirone R, Attisano L, Wrana JL: MADR2 is a substrate of the TGF-β receptor and its phosphorylation is required for nuclear accumulation and signalling. Cell 1996;87:1215-1224.
    • (1996) Cell , vol.87 , pp. 1215-1224
    • Macías-Silva, M.1    Abdollah, S.2    Hoodless, P.A.3    Pirone, R.4    Attisano, L.5    Wrana, J.L.6
  • 41
    • 0030183051 scopus 로고    scopus 로고
    • Tumor suppressor activity of the TGF-β pathway in human cancers
    • Markowitz SD, Roberts AB: Tumor suppressor activity of the TGF-β pathway in human cancers. Cytokine Growth Factor Rev 1996;7:93-102.
    • (1996) Cytokine Growth Factor Rev , vol.7 , pp. 93-102
    • Markowitz, S.D.1    Roberts, A.B.2
  • 42
    • 0029904671 scopus 로고    scopus 로고
    • Serine/threonine kinase receptors: Mediators of transforming growth factor beta family signals
    • Pawson T, Parker P (eds): London, ICRF Press
    • Massagué J, Weis-Garcia F: Serine/threonine kinase receptors: Mediators of transforming growth factor beta family signals; in Pawson T, Parker P (eds): Cancer Surveys Cell Signalling. London, ICRF Press, 1996, pp 41-64.
    • (1996) Cancer Surveys Cell Signalling , pp. 41-64
    • Massagué, J.1    Weis-Garcia, F.2
  • 47
  • 48
    • 0027953772 scopus 로고
    • Receptor ser/thr kinases implicated in the control of Drosophila body pattern by decapentaplegic
    • Nellen D, Affolter M, Basler K: Receptor ser/thr kinases implicated in the control of Drosophila body pattern by decapentaplegic. Cell 1994;78: 225-237.
    • (1994) Cell , vol.78 , pp. 225-237
    • Nellen, D.1    Affolter, M.2    Basler, K.3
  • 49
    • 0030018425 scopus 로고    scopus 로고
    • Mothers against dpp encodes a conserved cytoplasmic protein required in DPP/TGF-β responsive cells
    • Newfeld SJ, Chartoff EH, Graff JM, Melton DA, Gelbart WM: Mothers against dpp encodes a conserved cytoplasmic protein required in DPP/TGF-β responsive cells. Development 1996;122:2099-2108.
    • (1996) Development , vol.122 , pp. 2099-2108
    • Newfeld, S.J.1    Chartoff, E.H.2    Graff, J.M.3    Melton, D.A.4    Gelbart, W.M.5
  • 50
    • 0030885190 scopus 로고    scopus 로고
    • Mothers against dpp participate in a DPP/TGF-β responsive serine-threonine kinase signal transduction cascade
    • Newfeld SJ, Mehra A, Singer MA, Wrana JL, Attisano L: Mothers against dpp participate in a DPP/TGF-β responsive serine-threonine kinase signal transduction cascade. Development 1997;124:3167-3176.
    • (1997) Development , vol.124 , pp. 3167-3176
    • Newfeld, S.J.1    Mehra, A.2    Singer, M.A.3    Wrana, J.L.4    Attisano, L.5
  • 51
    • 0029153741 scopus 로고
    • Identification of a human type II receptor for bone morphogenetic protein-4 that forms differential heteromeric complexes with bone morphogenetic protein type I receptors
    • Nohno T, Ishikawa T, Saito T, Hosokawa K, Noji S, Wolsing DH, Rosenbaum JS: Identification of a human type II receptor for bone morphogenetic protein-4 that forms differential heteromeric complexes with bone morphogenetic protein type I receptors. J Biol Chem 1995;270: 22522-22526.
    • (1995) J Biol Chem , vol.270 , pp. 22522-22526
    • Nohno, T.1    Ishikawa, T.2    Saito, T.3    Hosokawa, K.4    Noji, S.5    Wolsing, D.H.6    Rosenbaum, J.S.7
  • 52
    • 0008125299 scopus 로고
    • Mutations affecting the pattern of the larval cuticle in Drosophila melanogaster. I. Zygotic loci on the second chromosome
    • Nüsslein-Volhard C, Wieschaus E, Kluding H: Mutations affecting the pattern of the larval cuticle in Drosophila melanogaster. I. Zygotic loci on the second chromosome. Rouxs Arch Dev Biol 1984;183:267-282.
    • (1984) Rouxs Arch Dev Biol , vol.183 , pp. 267-282
    • Nüsslein-Volhard, C.1    Wieschaus, E.2    Kluding, H.3
  • 53
    • 0028556486 scopus 로고
    • Genetic changes in the transforming growth factor β (TGF-β) type II receptor gene in human gastric cancer cells: Correlation with sensitivity to growth inhibition by TGF-β
    • Park K, Kim S-J, Bang Y-J, Park J-G, Kim NK, Roberts AB, Sporn MB: Genetic changes in the transforming growth factor β (TGF-β) type II receptor gene in human gastric cancer cells: Correlation with sensitivity to growth inhibition by TGF-β. Proc Natl Acad Sci USA 1994; 91:8772-8776.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 8772-8776
    • Park, K.1    Kim, S.-J.2    Bang, Y.-J.3    Park, J.-G.4    Kim, N.K.5    Roberts, A.B.6    Sporn, M.B.7
  • 54
    • 0030781148 scopus 로고    scopus 로고
    • Mutant endoglin in hereditary hemorrhagic telangiectasia type 1 is transiently expressed intracellularly and is not a dominant negative
    • in press
    • Pece N, Vera S, Cymerman U, White RI Jr, Wrana JL, Letarte M: Mutant endoglin in hereditary hemorrhagic telangiectasia type 1 is transiently expressed intracellularly and is not a dominant negative. J Clin Invest 1997, in press.
    • (1997) J Clin Invest
    • Pece, N.1    Vera, S.2    Cymerman, U.3    White Jr., R.I.4    Wrana, J.L.5    Letarte, M.6
  • 56
    • 0028893294 scopus 로고
    • Genetic screens to identify elements of the decapentaplegic signaling pathway in Drosophi-la
    • Raftery LA, Twombly V, Wharton K, Gelbart WM: Genetic screens to identify elements of the decapentaplegic signaling pathway in Drosophi-la. Genetics 1995;139:241-254.
    • (1995) Genetics , vol.139 , pp. 241-254
    • Raftery, L.A.1    Twombly, V.2    Wharton, K.3    Gelbart, W.M.4
  • 60
    • 0028923022 scopus 로고
    • An absolute requirement for both the type II and type I receptors, punt and thick veins for dpp signalling in vivo
    • Ruberte E, Marty T, Nellen D, Affolter M, Basler K: An absolute requirement for both the type II and type I receptors, punt and thick veins for dpp signalling in vivo. Cell 1995;80:889-897.
    • (1995) Cell , vol.80 , pp. 889-897
    • Ruberte, E.1    Marty, T.2    Nellen, D.3    Affolter, M.4    Basler, K.5
  • 61
    • 0029853242 scopus 로고    scopus 로고
    • MAD about colorectal cancer
    • Rustgi AK: MAD about colorectal cancer. Gastroenterology 1996;111:1387-1389.
    • (1996) Gastroenterology , vol.111 , pp. 1387-1389
    • Rustgi, A.K.1
  • 62
    • 0030028533 scopus 로고    scopus 로고
    • Identification of important regions in the cytoplasmic juxtamembrane domain of type I receptor that separate signaling pathways of transforming growth factor-β
    • Saitoh M, Nishitoh H, Amagasa T, Miyazono K, Takagi M, Ichijo H: Identification of important regions in the cytoplasmic juxtamembrane domain of type I receptor that separate signaling pathways of transforming growth factor-β. J Biol Chem 1996;271:2769-2775.
    • (1996) J Biol Chem , vol.271 , pp. 2769-2775
    • Saitoh, M.1    Nishitoh, H.2    Amagasa, T.3    Miyazono, K.4    Takagi, M.5    Ichijo, H.6
  • 63
    • 0030058914 scopus 로고    scopus 로고
    • Caenorhabditis elegans genes sma-2, sma-3 and sma-4 define a conserved family of transforming growth factor β pathway components
    • Savage C, Das P, Finelli A, Townsend S, Sun C, Baird S, Padgett R: Caenorhabditis elegans genes sma-2, sma-3 and sma-4 define a conserved family of transforming growth factor β pathway components. Proc Natl Acad Sci USA 1996;93:790-794.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 790-794
    • Savage, C.1    Das, P.2    Finelli, A.3    Townsend, S.4    Sun, C.5    Baird, S.6    Padgett, R.7
  • 64
    • 0028940853 scopus 로고
    • Genetic characterization and cloning of Mothers against dpp, a gene required for decapentaplegic function in Drosophila melanogaster
    • Sekelsky JJ, Newfeld SJ, Raftery LA, Chartoff EH, Gelbart WM: Genetic characterization and cloning of Mothers against dpp, a gene required for decapentaplegic function in Drosophila melanogaster. Genetics 1995;139:1347-1358.
    • (1995) Genetics , vol.139 , pp. 1347-1358
    • Sekelsky, J.J.1    Newfeld, S.J.2    Raftery, L.A.3    Chartoff, E.H.4    Gelbart, W.M.5
  • 65
    • 0030837455 scopus 로고    scopus 로고
    • A structural basis for mutational inactivation of the tumour suppressor Smad4
    • Shi Y, Hata A, Lo RS, Massagué J, Pavletich NP: A structural basis for mutational inactivation of the tumour suppressor Smad4. Nature 1997; 388:87-93.
    • (1997) Nature , vol.388 , pp. 87-93
    • Shi, Y.1    Hata, A.2    Lo, R.S.3    Massagué, J.4    Pavletich, N.P.5
  • 67
    • 0029959774 scopus 로고    scopus 로고
    • Phosphorylation of Serl 65 in TGF-β type I receptor modulates TGF-β1-induced cellular responses
    • Souchelnytskyi S, ten Dijke P, Miyazono K, Heldin C-H: Phosphorylation of Serl 65 in TGF-β type I receptor modulates TGF-β1-induced cellular responses. EMBOJ 1996;15:6231-6240.
    • (1996) EMBOJ , vol.15 , pp. 6231-6240
    • Souchelnytskyi, S.1    Ten Dijke, P.2    Miyazono, K.3    Heldin, C.-H.4
  • 68
    • 0028880508 scopus 로고
    • A Drosophila protein related to the human zinc-finger transcription factor PRDII/MBPI/ HIV-EP1 is required for dpp signaling
    • Staehling-Hampton K, Laughon AS, Hoffmann FM: A Drosophila protein related to the human zinc-finger transcription factor PRDII/MBPI/ HIV-EP1 is required for dpp signaling. Development 1995;121:3393-3403.
    • (1995) Development , vol.121 , pp. 3393-3403
    • Staehling-Hampton, K.1    Laughon, A.S.2    Hoffmann, F.M.3
  • 70
    • 0029944441 scopus 로고    scopus 로고
    • Signaling via hetero-oligomeric complexes of type I and type II serine/threonine kinase receptors
    • Ten Dijke P, Miyazono K, Heldin C-H: Signaling via hetero-oligomeric complexes of type I and type II serine/threonine kinase receptors. Curr Opin Cell Biol 1996;8:139-145.
    • (1996) Curr Opin Cell Biol , vol.8 , pp. 139-145
    • Ten Dijke, P.1    Miyazono, K.2    Heldin, C.-H.3
  • 71
    • 0029834231 scopus 로고    scopus 로고
    • Xenopus Mothers against decapentaplegic is an embryonic ventralizing agent that acts downstream of the BMP2/4 receptor
    • Thomsen GH: Xenopus Mothers against decapentaplegic is an embryonic ventralizing agent that acts downstream of the BMP2/4 receptor. Development 1996;122:2359-2366.
    • (1996) Development , vol.122 , pp. 2359-2366
    • Thomsen, G.H.1
  • 74
    • 0023644206 scopus 로고
    • A maternal mRNA localized to the vegetal hemisphere in Xenopus eggs codes for a growth factor related to TGF-β
    • Weeks DL, Melton DA: A maternal mRNA localized to the vegetal hemisphere in Xenopus eggs codes for a growth factor related to TGF-β. Cell 1987;51:861-867.
    • (1987) Cell , vol.51 , pp. 861-867
    • Weeks, D.L.1    Melton, D.A.2
  • 75
    • 0030037438 scopus 로고    scopus 로고
    • Mad acts downstream of Dpp receptors, revealing a differential requirement for dpp signalling and propagation of morphogenesis in the Drosophila eye
    • Wiersdorff V, Lecuit T, Cohen SM, Mlodzik M: Mad acts downstream of Dpp receptors, revealing a differential requirement for dpp signalling and propagation of morphogenesis in the Drosophila eye. Development 1996;122:2153-2162.
    • (1996) Development , vol.122 , pp. 2153-2162
    • Wiersdorff, V.1    Lecuit, T.2    Cohen, S.M.3    Mlodzik, M.4
  • 76
    • 0027367937 scopus 로고
    • Signalling activity of TGF-β type II receptors lacking specific domains in the cytoplasmic region
    • Wieser R, Attisano L, Wrana JL, Massagué J: Signalling activity of TGF-β type II receptors lacking specific domains in the cytoplasmic region. Mol Cell Biol 1993;13:7239-7247.
    • (1993) Mol Cell Biol , vol.13 , pp. 7239-7247
    • Wieser, R.1    Attisano, L.2    Wrana, J.L.3    Massagué, J.4
  • 77
    • 0029022221 scopus 로고
    • GS domain mutations that constitutively activate TβR-I, the downstream signalling component in the TGF-β receptor complex
    • Wieser R, Wrana JL, Massague J: GS domain mutations that constitutively activate TβR-I, the downstream signalling component in the TGF-β receptor complex. EMBO J 1995;14: 2199-2208.
    • (1995) EMBO J , vol.14 , pp. 2199-2208
    • Wieser, R.1    Wrana, J.L.2    Massague, J.3
  • 80
    • 0030974042 scopus 로고    scopus 로고
    • Heteromeric and homomeric interactions correlate with signaling activity and functional cooperativity of Smad3 and Smad4/DPC4
    • Wu R-Y, Zhang Y, Feng X-H, Derynck R: Heteromeric and homomeric interactions correlate with signaling activity and functional cooperativity of Smad3 and Smad4/DPC4. Mol Cell Biol 1997;17:2521-2528.
    • (1997) Mol Cell Biol , vol.17 , pp. 2521-2528
    • Wu, R.-Y.1    Zhang, Y.2    Feng, X.-H.3    Derynck, R.4
  • 83
    • 0029833909 scopus 로고    scopus 로고
    • Mammalian Dwarfins are phosphorylated in response to TGF-β and are implicated in control of cell growth
    • Yingling JM, Das P, Savage C, Zhang M, Padgett RW, Wang X-F: Mammalian Dwarfins are phosphorylated in response to TGF-β and are implicated in control of cell growth. Proc Natl Acad Sci USA 1996;93:8940-8944.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 8940-8944
    • Yingling, J.M.1    Das, P.2    Savage, C.3    Zhang, M.4    Padgett, R.W.5    Wang, X.-F.6
  • 84
    • 0029786212 scopus 로고    scopus 로고
    • Receptor-associated Mad homologues synergize as effectors of the TGF-β response
    • Zhang Y, Feng X-H, Wu R-Y, Derynck R: Receptor-associated Mad homologues synergize as effectors of the TGF-β response. Nature 1996; 383:168-172.
    • (1996) Nature , vol.383 , pp. 168-172
    • Zhang, Y.1    Feng, X.-H.2    Wu, R.-Y.3    Derynck, R.4
  • 85
    • 0031128153 scopus 로고    scopus 로고
    • The tumor suppressor Smad4/DPC4 as a central mediator of Smad function
    • Zhang Y, Musci T, Derynck R: The tumor suppressor Smad4/DPC4 as a central mediator of Smad function. Curr Biol 1997;7:270-276.
    • (1997) Curr Biol , vol.7 , pp. 270-276
    • Zhang, Y.1    Musci, T.2    Derynck, R.3


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