메뉴 건너뛰기




Volumn 9, Issue 1, 1998, Pages 49-61

Signal transduction by bone morphogenetic proteins

Author keywords

Bone morphogenetic protein; Drosophila; Serine threonine kinase receptor; Signal transduction; Smad

Indexed keywords

BONE MORPHOGENETIC PROTEIN;

EID: 0032029606     PISSN: 13596101     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1359-6101(97)00036-1     Document Type: Article
Times cited : (468)

References (119)
  • 1
    • 34250019537 scopus 로고
    • Bone: Formation by autoinduction
    • Urist MR, Bone: formation by autoinduction. Science 1965, 150, 893-899.
    • (1965) Science , vol.150 , pp. 893-899
    • Urist, M.R.1
  • 3
    • 0031105160 scopus 로고    scopus 로고
    • Bone morphogenetic proteins: An unconventional approach to isolation of first mammalian morphogens
    • Reddi AH. Bone morphogenetic proteins: an unconventional approach to isolation of first mammalian morphogens. Cytokine Growth Factor Rev 1997, 8, 11-20.
    • (1997) Cytokine Growth Factor Rev , vol.8 , pp. 11-20
    • Reddi, A.H.1
  • 4
    • 0029737070 scopus 로고    scopus 로고
    • Bone morphogenetic proteins: Multifunctional regulators of vertebrate development
    • Hogan BLM. Bone morphogenetic proteins: multifunctional regulators of vertebrate development. Genes Dev 1996, 10, 1580-1594.
    • (1996) Genes Dev , vol.10 , pp. 1580-1594
    • Hogan, B.L.M.1
  • 5
    • 0028180315 scopus 로고
    • The TGF-β superfamily: New members, new receptors, and new genetic tests of function in different organisms
    • Kingsley DM. The TGF-β superfamily: new members, new receptors, and new genetic tests of function in different organisms. Genes Dev 1994, 8, 133-146.
    • (1994) Genes Dev , vol.8 , pp. 133-146
    • Kingsley, D.M.1
  • 6
    • 0027161383 scopus 로고
    • Drosophila transforming growth factor β superfamily proteins induce endochondral bone formation in mammals
    • Sampath TK, Rashka KE, Doctor JS, Tucker RF, Hoffmann FM. Drosophila transforming growth factor β superfamily proteins induce endochondral bone formation in mammals. Proc Natl Acad Sci USA 1993, 90, 6004-6008.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 6004-6008
    • Sampath, T.K.1    Rashka, K.E.2    Doctor, J.S.3    Tucker, R.F.4    Hoffmann, F.M.5
  • 7
    • 0027403003 scopus 로고
    • Human BMP sequences can confer normal dorsal-ventral patterning in the Drosophila embryo
    • Padgett RW, Wozney JM, Gelbart WM. Human BMP sequences can confer normal dorsal-ventral patterning in the Drosophila embryo. Proc Natl Acad Sci USA 1993, 90, 2905-2909.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 2905-2909
    • Padgett, R.W.1    Wozney, J.M.2    Gelbart, W.M.3
  • 8
    • 0029149656 scopus 로고
    • Bone morphogenetic protein-4 is required for mesoderm formation and patterning in the mouse
    • Winnier G, Blessing M, Labosky PA, Hogan BLM. Bone morphogenetic protein-4 is required for mesoderm formation and patterning in the mouse. Genes Dev 1995, 9, 2105-2116.
    • (1995) Genes Dev , vol.9 , pp. 2105-2116
    • Winnier, G.1    Blessing, M.2    Labosky, P.A.3    Hogan, B.L.M.4
  • 9
    • 0029850112 scopus 로고    scopus 로고
    • Mice deficient for BMP2 are nonviable and have defects in amnion/chorion and cardiac development
    • Zhang H, Bradley A. Mice deficient for BMP2 are nonviable and have defects in amnion/chorion and cardiac development. Development 1996, 122, 2977-2986.
    • (1996) Development , vol.122 , pp. 2977-2986
    • Zhang, H.1    Bradley, A.2
  • 10
    • 0028832707 scopus 로고
    • A requirement for bone morphogenetic protein-7 during development of the mammalian kidney and eye
    • Dudley AT, Lyons KM, Robertson EJ. A requirement for bone morphogenetic protein-7 during development of the mammalian kidney and eye. Genes Dev 1995, 9, 2795-2807.
    • (1995) Genes Dev , vol.9 , pp. 2795-2807
    • Dudley, A.T.1    Lyons, K.M.2    Robertson, E.J.3
  • 11
    • 0028882261 scopus 로고
    • BMP-7 is an inducer of nephrogenesis, and is also required for eye development and skeletal patterning
    • Luo G, Hofmann C, Bronckers ALJJ, Sohocki M, Bradley, A, Karsenty G. BMP-7 is an inducer of nephrogenesis, and is also required for eye development and skeletal patterning. Genes Dev 1995, 9, 2808-2820.
    • (1995) Genes Dev , vol.9 , pp. 2808-2820
    • Luo, G.1    Hofmann, C.2    Bronckers, A.L.J.J.3    Sohocki, M.4    Bradley, A.5    Karsenty, G.6
  • 12
    • 0029775560 scopus 로고    scopus 로고
    • The gene encoding bone morphogenetic protein 8B is required for the initiation and maintenance of spermatogenesis in the mouse
    • Zhao G-Q, Deng K, Labosky PA, Liaw L, Hogan BLM. The gene encoding bone morphogenetic protein 8B is required for the initiation and maintenance of spermatogenesis in the mouse. Genes Dev 1996, 10, 1657-1669.
    • (1996) Genes Dev , vol.10 , pp. 1657-1669
    • Zhao, G.-Q.1    Deng, K.2    Labosky, P.A.3    Liaw, L.4    Hogan, B.L.M.5
  • 13
    • 0026440993 scopus 로고
    • The mouse short ear skeletal morphogenesis locus is associated with defects in a bone morphogenetic member of the TGFβ superfamily
    • Kingsley DM, Bland AE, Grubber JM, Marker PC, Russell LB, Copeland NG, Jenkins NA. The mouse short ear skeletal morphogenesis locus is associated with defects in a bone morphogenetic member of the TGFβ superfamily. Cell 1992, 71, 399-410.
    • (1992) Cell , vol.71 , pp. 399-410
    • Kingsley, D.M.1    Bland, A.E.2    Grubber, J.M.3    Marker, P.C.4    Russell, L.B.5    Copeland, N.G.6    Jenkins, N.A.7
  • 14
    • 0028068362 scopus 로고
    • Specificity of bone morphogenetic protein-related factors: Cell fate and gene expression changes in Drosophila embryos induced by Decapentaplegic, but not 60A
    • Staehling-Hampton K, Jackson PD, Clark MJ, Brand AH, Hoffmann FM. Specificity of bone morphogenetic protein-related factors: cell fate and gene expression changes in Drosophila embryos induced by Decapentaplegic, but not 60A. Cell Growth Differ 1994, 5, 585-593.
    • (1994) Cell Growth Differ , vol.5 , pp. 585-593
    • Staehling-Hampton, K.1    Jackson, P.D.2    Clark, M.J.3    Brand, A.H.4    Hoffmann, F.M.5
  • 15
    • 0028232724 scopus 로고
    • Limb alterations in brachypodism mice due to mutations in a new member of the TGFβ-superfamily
    • Storm EE, Huynh TV, Copeland NG, Jenkins NA, Kingsley DM, Lee S-J. Limb alterations in brachypodism mice due to mutations in a new member of the TGFβ-superfamily. Nature 1994, 368, 639-643.
    • (1994) Nature , vol.368 , pp. 639-643
    • Storm, E.E.1    Huynh, T.V.2    Copeland, N.G.3    Jenkins, N.A.4    Kingsley, D.M.5    Lee, S.-J.6
  • 16
    • 0028126646 scopus 로고
    • Cartilage-derived morphogenetic proteins. New members of the transforming growth factor-β superfamily predominantly expressed in long bones during human embryonic development
    • Chang SC, Hoang B, Thomas JT, Vukicevic S, Luyten FP, Ryba NJ, Kozak CA, Reddi AH, Moos M. Cartilage-derived morphogenetic proteins. New members of the transforming growth factor-β superfamily predominantly expressed in long bones during human embryonic development. J Biol Chem 1994, 269, 28227-28234.
    • (1994) J Biol Chem , vol.269 , pp. 28227-28234
    • Chang, S.C.1    Hoang, B.2    Thomas, J.T.3    Vukicevic, S.4    Luyten, F.P.5    Ryba, N.J.6    Kozak, C.A.7    Reddi, A.H.8    Moos, M.9
  • 22
    • 0031010050 scopus 로고    scopus 로고
    • Regulation of skeletal muscle mass in mice by a new TGF-β superfamily member
    • McPherron AC, Lawler AM, Lee SJ. Regulation of skeletal muscle mass in mice by a new TGF-β superfamily member. Nature 1997, 387, 83-90.
    • (1997) Nature , vol.387 , pp. 83-90
    • McPherron, A.C.1    Lawler, A.M.2    Lee, S.J.3
  • 24
    • 0029861824 scopus 로고    scopus 로고
    • Growth differentiation factor-9 is required during early ovarian folliculogenesis
    • Dong J, Albertini DF, Nishimori K, Kumar TR, Lu N, Matzuk MM. Growth differentiation factor-9 is required during early ovarian folliculogenesis. Nature 1996, 383, 531-535.
    • (1996) Nature , vol.383 , pp. 531-535
    • Dong, J.1    Albertini, D.F.2    Nishimori, K.3    Kumar, T.R.4    Lu, N.5    Matzuk, M.M.6
  • 27
    • 0028135238 scopus 로고
    • The screw gene encodes a ubiquitously expressed member of the TGF-β family required for specification of dorsal cell fates in the Drosophila embryo
    • Arora K, Levine MS, O'Connor MB. The screw gene encodes a ubiquitously expressed member of the TGF-β family required for specification of dorsal cell fates in the Drosophila embryo. Genes Dev 1994, 8, 2588-2601.
    • (1994) Genes Dev , vol.8 , pp. 2588-2601
    • Arora, K.1    Levine, M.S.2    O'Connor, M.B.3
  • 28
    • 0030598829 scopus 로고    scopus 로고
    • The Spemann organizer signal noggin binds and inactivates bone morphogenetic protein 4
    • Zimmerman LB, De Jesus-Escobar JM, Harland RM. The Spemann organizer signal noggin binds and inactivates bone morphogenetic protein 4. Cell 1996, 86, 599-606.
    • (1996) Cell , vol.86 , pp. 599-606
    • Zimmerman, L.B.1    De Jesus-Escobar, J.M.2    Harland, R.M.3
  • 29
    • 0030598867 scopus 로고    scopus 로고
    • Dorsoventral patterning in Xenopus: Inhibition of ventral signals by direct binding of chordin to BMP-4
    • Piccolo S, Sasai Y, Lu B, De Robertis EM. Dorsoventral patterning in Xenopus: inhibition of ventral signals by direct binding of chordin to BMP-4. Cell 1996, 86, 589-598.
    • (1996) Cell , vol.86 , pp. 589-598
    • Piccolo, S.1    Sasai, Y.2    Lu, B.3    De Robertis, E.M.4
  • 32
    • 0028918915 scopus 로고
    • Multiple defects and perinatal death in mice deficient in follistatin
    • Matzuk MM, Lu N, Vogel H, Sellheyer K, Roop DR, Bradley A. Multiple defects and perinatal death in mice deficient in follistatin. Nature 1995, 374, 360-363.
    • (1995) Nature , vol.374 , pp. 360-363
    • Matzuk, M.M.1    Lu, N.2    Vogel, H.3    Sellheyer, K.4    Roop, D.R.5    Bradley, A.6
  • 33
    • 0029944441 scopus 로고    scopus 로고
    • Signaling via heterooligomeric complex of type I and type II serine/threonine kinase receptors
    • ten Dijke P, Miyazono K, Heldin C-H. Signaling via heterooligomeric complex 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
  • 35
    • 0029022221 scopus 로고
    • GS domain mutations that constitutively activate TβR-I, the downstream signaling component in the TGF-β receptor complex
    • Wieser R, Wrana JL, Massagué J. GS domain mutations that constitutively activate TβR-I, the downstream signaling 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    Massagué, J.3
  • 36
    • 0029786480 scopus 로고    scopus 로고
    • Characterization of the interaction of FKBP12 with the transforming growth factor-β type I receptor in vivo
    • Okadome T, Oeda E, Saitoh M, Ichijo H, Moses HL, Miyazono K, Kawabata M. Characterization of the interaction of FKBP12 with the transforming growth factor-β type I receptor in vivo. J Biol Chem 1996, 271, 21687- 21690.
    • (1996) J Biol Chem , vol.271 , pp. 21687-21690
    • Okadome, T.1    Oeda, E.2    Saitoh, M.3    Ichijo, H.4    Moses, H.L.5    Miyazono, K.6    Kawabata, M.7
  • 37
    • 0029836237 scopus 로고    scopus 로고
    • FKBP-12 recognition is dispensable for signal generation by type I transforming growth factor-β receptors
    • Charng MJ, Kinnunen P, Hawker J, Brand T, Schneider MD. FKBP-12 recognition is dispensable for signal generation by type I transforming growth factor-β receptors. J Biol Chem 1996, 271, 22941-22944.
    • (1996) J Biol Chem , vol.271 , pp. 22941-22944
    • Charng, M.J.1    Kinnunen, P.2    Hawker, J.3    Brand, T.4    Schneider, M.D.5
  • 39
    • 0030926004 scopus 로고    scopus 로고
    • Mechanisms of TGFβ receptor inhibition by FKBP12
    • Chen YG, Liu F, Massagué J. Mechanisms of TGFβ receptor inhibition by FKBP12. EMBO J 1997, 16, 3866-3876.
    • (1997) EMBO J , vol.16 , pp. 3866-3876
    • Chen, Y.G.1    Liu, F.2    Massagué, J.3
  • 41
    • 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
  • 42
    • 0028931238 scopus 로고
    • Cloning of a novel type II serine/threonine kinase receptor through interaction with the type I transforming growth factor-β receptor
    • Kawabata M, Chytil A, Moses HL. Cloning of a novel type II serine/threonine kinase receptor through interaction with the type I transforming growth factor-β receptor. J Biol Chem 1995, 270, 5625-5630.
    • (1995) J Biol Chem , vol.270 , pp. 5625-5630
    • Kawabata, M.1    Chytil, A.2    Moses, H.L.3
  • 43
    • 0029008597 scopus 로고
    • Human type II receptor for bone morphogenic 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 morphogenic proteins (BMPs): extension of the two-kinase receptor model to the BMPs. Mol Cell Biol 1995, 15, 3479-3486.
    • (1995) Mol Cell Biol , vol.15 , pp. 3479-3486
    • Liu, F.1    Ventura, F.2    Doody, J.3    Massagué, J.4
  • 44
    • 17444441924 scopus 로고    scopus 로고
    • cDNA cloning and genomic organization of the mouse BMP type II receptor
    • Beppu H, Minowa O, Miyazono K, Kawabata M. cDNA cloning and genomic organization of the mouse BMP type II receptor. Biochem Biophys Res Commun 1997, 235, 499-504.
    • (1997) Biochem Biophys Res Commun , vol.235 , pp. 499-504
    • Beppu, H.1    Minowa, O.2    Miyazono, K.3    Kawabata, M.4
  • 45
    • 0028866028 scopus 로고
    • Truncated type II receptor for BMP-4 induces secondary axial structures in Xenopus embryos
    • Ishikawa T, Yoshioka H, Ohuchi H, Noji S, Nohno T. Truncated type II receptor for BMP-4 induces secondary axial structures in Xenopus embryos. Biochem Biophys Res Commun 1995, 216, 26-33.
    • (1995) Biochem Biophys Res Commun , vol.216 , pp. 26-33
    • Ishikawa, T.1    Yoshioka, H.2    Ohuchi, H.3    Noji, S.4    Nohno, T.5
  • 48
    • 0029666256 scopus 로고    scopus 로고
    • Fetuin/α2-HS glycoprotein is a transforming growth factor-β type II receptor mimic and cytokine antagonist
    • Demetriou M, Binkert C, Sukhu B, Tenenbaum HC, Dennis JW. Fetuin/α2-HS glycoprotein is a transforming growth factor-β type II receptor mimic and cytokine antagonist. J Biol Chem 1996, 271, 12755-12761.
    • (1996) J Biol Chem , vol.271 , pp. 12755-12761
    • Demetriou, M.1    Binkert, C.2    Sukhu, B.3    Tenenbaum, H.C.4    Dennis, J.W.5
  • 49
    • 0028929864 scopus 로고
    • Different phenotypes for mice deficient in either activins or activin receptor type II
    • Matzuk MM, Kumar TR, Bradley A. Different phenotypes for mice deficient in either activins or activin receptor type II. Nature 1995, 374, 356-360.
    • (1995) Nature , vol.374 , pp. 356-360
    • Matzuk, M.M.1    Kumar, T.R.2    Bradley, A.3
  • 50
    • 0030837018 scopus 로고    scopus 로고
    • The signaling pathway mediated by the type IIB activin receptor controls axial patterning and lateral asymmetry in the mouse
    • Oh SP, Li E. The signaling pathway mediated by the type IIB activin receptor controls axial patterning and lateral asymmetry in the mouse. Genes Dev 1997, 11, 1812-1826.
    • (1997) Genes Dev , vol.11 , pp. 1812-1826
    • Oh, S.P.1    Li, E.2
  • 53
    • 0028923022 scopus 로고
    • An absolute requirement for both the type II and type I receptors, punt and thick veins, for dpp signaling 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 signaling 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
  • 57
    • 0028091791 scopus 로고
    • A truncated bone morphogenetic protein receptor affects dorsal-ventral patterning in the early Xenopus embryo
    • Suzuki A, Thies RS, Yamaji N, Song JJ, Wozney JM, Murakami K, Ueno N. A truncated bone morphogenetic protein receptor affects dorsal-ventral patterning in the early Xenopus embryo. Proc Natl Acad Sci USA 1994, 91, 10255-10259.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 10255-10259
    • Suzuki, A.1    Thies, R.S.2    Yamaji, N.3    Song, J.J.4    Wozney, J.M.5    Murakami, K.6    Ueno, N.7
  • 59
    • 0030826702 scopus 로고    scopus 로고
    • A kinase domain-truncated type I receptor blocks bone morphogenetic protein-2-induced signal transduction in C2C12 myoblasts
    • Namiki M, Akiyama S, Katagiri T, Suzuki A, Ueno N, Yamaji N, Rosen V, Wozney JM, Suda T. A kinase domain-truncated type I receptor blocks bone morphogenetic protein-2-induced signal transduction in C2C12 myoblasts. J Biol Chem 1997, 272, 22046-22052.
    • (1997) J Biol Chem , vol.272 , pp. 22046-22052
    • Namiki, M.1    Akiyama, S.2    Katagiri, T.3    Suzuki, A.4    Ueno, N.5    Yamaji, N.6    Rosen, V.7    Wozney, J.M.8    Suda, T.9
  • 64
    • 0030899939 scopus 로고    scopus 로고
    • A chimeric serine/threonine kinase receptor system reveals the potential of multiple type II receptors to cooperate with transforming growth factor-β type I receptor
    • Muramatsu M, Yan J, Eto K, Tomoda T, Yamada R, Arai K-i. A chimeric serine/threonine kinase receptor system reveals the potential of multiple type II receptors to cooperate with transforming growth factor-β type I receptor. Mol Biol Cell 1997, 8, 469-480.
    • (1997) Mol Biol Cell , vol.8 , pp. 469-480
    • Muramatsu, M.1    Yan, J.2    Eto, K.3    Tomoda, T.4    Yamada, R.5    Arai, K.-I.6
  • 65
    • 0030761239 scopus 로고    scopus 로고
    • Transforming growth factor (TGF-β)-specific signaling by chimeric TGF-β type II receptor with intracellular domain of activin type IIB receptor
    • Persson U, Souchelnytskyi S, Franzén P, Miyazono K, ten Dijke P, Heldin C-H. Transforming growth factor (TGF-β)-specific signaling by chimeric TGF-β type II receptor with intracellular domain of activin type IIB receptor. J Biol Chem 1997, 272, 21187-21194.
    • (1997) J Biol Chem , vol.272 , pp. 21187-21194
    • Persson, U.1    Souchelnytskyi, S.2    Franzén, P.3    Miyazono, K.4    Ten Dijke, P.5    Heldin, C.-H.6
  • 66
    • 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
  • 67
    • 0030995947 scopus 로고    scopus 로고
    • Interaction between soluble type I receptor for bone morphogenetic protein and bone morphogenetic protein-4
    • Natsume T, Tomita S, Iemura S, Kinto N, Yamaguchi A, Ueno N. Interaction between soluble type I receptor for bone morphogenetic protein and bone morphogenetic protein-4. J Biol Chem 1997, 272, 11535-11540.
    • (1997) J Biol Chem , vol.272 , pp. 11535-11540
    • Natsume, T.1    Tomita, S.2    Iemura, S.3    Kinto, N.4    Yamaguchi, A.5    Ueno, N.6
  • 68
    • 0028170038 scopus 로고
    • Studies with a Xenopus BMP receptor suggest that ventral mesoderm-inducing signals override dorsal signals in vivo
    • Graff JM, Thies RS, Song JJ, Celeste AJ, Melton DA. Studies with a Xenopus BMP receptor suggest that ventral mesoderm-inducing signals override dorsal signals in vivo. Cell 1994, 79, 169-179.
    • (1994) Cell , vol.79 , pp. 169-179
    • Graff, J.M.1    Thies, R.S.2    Song, J.J.3    Celeste, A.J.4    Melton, D.A.5
  • 69
    • 0029876835 scopus 로고    scopus 로고
    • Requirement for BMP signaling in interdigital apoptosis and scale formation
    • Zou H, Niswander L. Requirement for BMP signaling in interdigital apoptosis and scale formation. Science 1996, 272, 738-741.
    • (1996) Science , vol.272 , pp. 738-741
    • Zou, H.1    Niswander, L.2
  • 71
    • 6244256053 scopus 로고
    • Bmpr encodes a type I bone morphogenetic protein receptor that is essential for gastrulation during mouse embryogenesis
    • Mishina Y, Suzuki A, Ueno N, Behringer RR. Bmpr encodes a type I bone morphogenetic protein receptor that is essential for gastrulation during mouse embryogenesis. Genes Dev 1995, 9, 3027-3037.
    • (1995) Genes Dev , vol.9 , pp. 3027-3037
    • Mishina, Y.1    Suzuki, A.2    Ueno, N.3    Behringer, R.R.4
  • 72
    • 0027953772 scopus 로고
    • Receptor serine/threonine kinases implicated in the control of Drosophila body pattern by decapentaplegic
    • Nellen D, Affolter M, Basler K. Receptor serine/threonine 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
  • 73
    • 0030926005 scopus 로고    scopus 로고
    • A kinase subdomain of transforming growth factor-β (TGF-β) type I receptor determines the TGF-β intracellular signaling specificity
    • Feng X-H, Derynck R. A kinase subdomain of transforming growth factor-β (TGF-β) type I 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
  • 75
    • 0028893294 scopus 로고
    • Genetic screens to identify elements of the decapentaplegic signaling pathway in Drosophila
    • Raftery LA, Twombly V, Wharton K, Gelbart WM. Genetic screens to identify elements of the decapentaplegic signaling pathway in Drosophila. 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
  • 76
    • 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
  • 77
    • 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 AL, Townsend SR, Sun CY, Baird SE, Padgett RW. 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.L.3    Townsend, S.R.4    Sun, C.Y.5    Baird, S.E.6    Padgett, R.W.7
  • 78
    • 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, 2099-2018.
    • (1996) Development , vol.122 , pp. 2099-12018
    • Newfeld, S.J.1    Chartoff, E.H.2    Graff, J.M.3    Melton, D.A.4    Gelbart, W.M.5
  • 79
    • 0030037438 scopus 로고    scopus 로고
    • Mad acts downstream of Dpp receptors, revealing a differential requirement for dpp signaling in initiation 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 signaling in initiation 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
  • 82
    • 0029829230 scopus 로고    scopus 로고
    • A novel mesoderm inducer, Madr2, functions in the activin signal transduction pathway
    • Baker JC, Harland RM. 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.M.2
  • 83
    • 0030300115 scopus 로고    scopus 로고
    • MADR2 is a substrate of the TGFβ receptor and its phosphorylation is required for nuclear accumulation and signaling
    • Macías-Silva M, Abdollah S, Hoodless PA, Pirone R, Attisano L, Wrana JL. MADR2 is a substrate of the TGFβ receptor and its phosphorylation is required for nuclear accumulation and signaling. 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
  • 84
    • 0030613262 scopus 로고    scopus 로고
    • Phosphorylation of Ser-465 and Ser-467 in the C-terminus of Smad2 mediates interaction with Smad4 and is required for TGF-β signaling
    • Souchelnytski S, Tamaki K, Engström U, Wernstedt C, ten Pijke P, Heldin C-H. Phosphorylation of Ser-465 and Ser-467 in the C-terminus of Smad2 mediates interaction with Smad4 and is required for TGF-β signaling. J Biol Chem 1997, 272, 28107-28115.
    • (1997) J Biol Chem , vol.272 , pp. 28107-28115
    • Souchelnytski, S.1    Tamaki, K.2    Engström, U.3    Wernstedt, C.4    Ten Pijke, P.5    Heldin, C.-H.6
  • 85
    • 0030911104 scopus 로고    scopus 로고
    • The TGF-β family mediator Smad1 is phosphorylated directly and activated functionally by the BMP receptor kinase
    • Kretzschmar 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
    • Kretzschmar, M.1    Liu, F.2    Hata, A.3    Doody, J.4    Massagué, J.5
  • 86
    • 0030886059 scopus 로고    scopus 로고
    • Concentration-dependent patterning of the Xenopus ectoderm by BMP4 and its signal transducer Smad1
    • Wilson PA, Lagna G, Suzuki A, Hemmati-Brivanlou A. Concentration-dependent patterning of the Xenopus ectoderm by BMP4 and its signal transducer Smad1. Development 1997, 124, 3177-3184.
    • (1997) Development , vol.124 , pp. 3177-3184
    • Wilson, P.A.1    Lagna, G.2    Suzuki, A.3    Hemmati-Brivanlou, A.4
  • 90
    • 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
  • 91
    • 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
  • 95
    • 0029940972 scopus 로고    scopus 로고
    • Xenopus Mad proteins transduce distinct subsets of signals for the TGFβ superfamily
    • Graff JM, Bansal A, Melton DA. Xenopus Mad proteins transduce distinct subsets of signals for the TGFβ superfamily. Cell 1996, 85, 479-487.
    • (1996) Cell , vol.85 , pp. 479-487
    • Graff, J.M.1    Bansal, A.2    Melton, D.A.3
  • 96
    • 0029834231 scopus 로고    scopus 로고
    • Xenopus mothers against decapentaplegic is an embryonic ventralizing agent that acts downstream of the BMP-2/4 receptor
    • Thomsen GH. Xenopus mothers against decapentaplegic is an embryonic ventralizing agent that acts downstream of the BMP-2/4 receptor. Development 1996, 122, 2359-2366.
    • (1996) Development , vol.122 , pp. 2359-2366
    • Thomsen, G.H.1
  • 97
    • 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
  • 99
    • 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
  • 100
    • 0030825516 scopus 로고    scopus 로고
    • Mutations increasing autoinhibition inactivate tumour suppressors Smad2 and Smad4
    • Hata A, Lo RS, Wotton D, Lagna G, Massagué J. Mutations increasing autoinhibition inactivate 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
  • 102
    • 0030885190 scopus 로고    scopus 로고
    • Mothers against dpp participates in a DPP/TGF-β responsive serine-threonine kinase signal transduction cascade
    • Newfeld SJ, Mehra A, Singer MA, Wrana JL, Attisano L, Gelbart WM. Mothers against dpp participates 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    Gelbart, W.M.6
  • 103
    • 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
  • 105
    • 0026334362 scopus 로고
    • Identification of regulatory sequences in the type 1 plasminogen activator inhibitor gene responsive to transforming growth factor β
    • Keeton MR, Curriden SA, van Zonneveld AJ, Loskutoff DJ. Identification of regulatory sequences in the type 1 plasminogen activator inhibitor gene responsive to transforming growth factor β. J Biol Chem 1991, 266, 23048-23052.
    • (1991) J Biol Chem , vol.266 , pp. 23048-23052
    • Keeton, M.R.1    Curriden, S.A.2    Van Zonneveld, A.J.3    Loskutoff, D.J.4
  • 107
    • 0028829465 scopus 로고
    • Functional analysis of the transforming growth factor β responsive elements in the WAF1/Cip1/p21 promoter
    • Datto MB, Yu Y, Wang X-F. Functional analysis of the transforming growth factor β responsive elements in the WAF1/Cip1/p21 promoter. J Biol Chem 1995, 270, 28623-28628.
    • (1995) J Biol Chem , vol.270 , pp. 28623-28628
    • Datto, M.B.1    Yu, Y.2    Wang, X.-F.3
  • 108
    • 0029585862 scopus 로고
    • Molecular mechanisms of Spemann's organizer formation: Conserved growth factor synergy between Xenopus and mouse
    • Watabe T, Kim S, Candia A, Rothbacher U, Hashimoto C, Inoue K, Cho KW. Molecular mechanisms of Spemann's organizer formation: conserved growth factor synergy between Xenopus and mouse. Genes Dev 1995, 9, 3038-3050.
    • (1995) Genes Dev , vol.9 , pp. 3038-3050
    • Watabe, T.1    Kim, S.2    Candia, A.3    Rothbacher, U.4    Hashimoto, C.5    Inoue, K.6    Cho, K.W.7
  • 109
    • 0030724014 scopus 로고    scopus 로고
    • Osteogenic protein-1 upregulation of the collagen X promoter activity is mediated by a MEF-2 like sequence and requires an adjacent AP-1 sequence
    • Harada S-i, Sampath TK, Aubin JE, Rodan GA. Osteogenic protein-1 upregulation of the collagen X promoter activity is mediated by a MEF-2 like sequence and requires an adjacent AP-1 sequence. Mol Endocrinol 1997, 11, 1832-1845.
    • (1997) Mol Endocrinol , vol.11 , pp. 1832-1845
    • S-i, H.1    Sampath, T.K.2    Aubin, J.E.3    Rodan, G.A.4
  • 110
    • 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
  • 112
    • 0030872367 scopus 로고    scopus 로고
    • Drosophila Mad binds to DNA and directly mediates activation of vestigial by Decepentaplegic
    • Kim J, Johnson K, Chen HJ, Carroll S, Laughon A. Drosophila Mad binds to DNA and directly mediates activation of vestigial by Decepentaplegic. Nature 1997, 388, 304-308.
    • (1997) Nature , vol.388 , pp. 304-308
    • Kim, J.1    Johnson, K.2    Chen, H.J.3    Carroll, S.4    Laughon, A.5
  • 113
    • 0029072998 scopus 로고
    • The Drosophila schnurri gene acts in the Dpp/TGFβ 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/TGFβ 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
  • 114
    • 0028990126 scopus 로고
    • Schnurri is required for Drosophila Dpp signaling 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 signaling 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
  • 115
    • 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
  • 117
    • 0030579203 scopus 로고    scopus 로고
    • TGF-β receptor type II deficiency results in defects of yolk sac hematopoiesis and vasculogenesis
    • Oshima M, Oshima H, Taketo MM. TGF-β receptor type II deficiency results in defects of yolk sac hematopoiesis and vasculogenesis. Dev Biol 1996, 179, 297-302.
    • (1996) Dev Biol , vol.179 , pp. 297-302
    • Oshima, M.1    Oshima, H.2    Taketo, M.M.3
  • 118
    • 0029658831 scopus 로고    scopus 로고
    • Genetic analysis of the Müllerian-inhibiting substance signal transduction pathway in mammalian sexual differentiation
    • Mishina Y, Rey R, Finegold MJ, Matzuk MM, Josso N, Cate RL, Behringer RR. Genetic analysis of the Müllerian-inhibiting substance signal transduction pathway in mammalian sexual differentiation. Genes Dev 1996, 10, 2577-2587.
    • (1996) Genes Dev , vol.10 , pp. 2577-2587
    • Mishina, Y.1    Rey, R.2    Finegold, M.J.3    Matzuk, M.M.4    Josso, N.5    Cate, R.L.6    Behringer, R.R.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.