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0029892494
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of special interest. Epistasis experiments show that Mad functions downstream of Dpp receptors and is required for receptor signaling. The authors identify Smad1, a vertebrate homolog of Mad, and show that Smad1 accumulates in the nucleus and becomes phosphorylated in reponse to BMP2.
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Hoodless PA, Haerry T, Abdollah S, Stapleton M, O'Connor MB, Attisano L, Wrana JL. Madr1, a MAD-related protein that functions in BMP2 signaling pathways. of special interest Cell. 85:1996;489-500 Epistasis experiments show that Mad functions downstream of Dpp receptors and is required for receptor signaling. The authors identify Smad1, a vertebrate homolog of Mad, and show that Smad1 accumulates in the nucleus and becomes phosphorylated in reponse to BMP2.
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Hoodless, P.A.1
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O'Connor, M.B.5
Attisano, L.6
Wrana, J.L.7
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Wiersdorff, V.1
Lecuit, T.2
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Caenorhabditis elegans genes sma-2, sma-3, and sma-4 define a conserved family of transforming growth factor beta pathway components
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of special interest. Identification of C. elegans genes, sma-2, sma-3 and sma-4, which have similar mutant phenotypes to those of daf-4, indicating that they are involved in TGF-β signaling. sma-2 is shown to function in the same cells as daf-4.
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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 beta pathway components. of special interest Proc Natl Acad Sci USA. 93:1996;790-794 Identification of C. elegans genes, sma-2, sma-3 and sma-4, which have similar mutant phenotypes to those of daf-4, indicating that they are involved in TGF-β signaling. sma-2 is shown to function in the same cells as daf-4.
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Proc Natl Acad Sci USA
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Savage, C.1
Das, P.2
Finelli, A.3
Townsend, S.4
Sun, C.5
Baird, S.6
Padgett, R.7
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24
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0029931509
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Human Smad1, a mediator of BMP signals, is a transcriptional activator
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of outstanding interest. Smad1 is here shown to have transcriptional activity when fused to a heterologous DNA-binding domain; this activity is increased by the addition of BMP4 AND BMP type I and type II receptors. The carboxy-terminal domain of Smad1 is shown to be important in transcriptional activation. Overexpression of Smad1 in Xenopus ectoderm induces the formation of ventral mesoderm.
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Liu F, Hata A, Baker JC, Doody J, Carcamo J, Harland RM, Massagúe J. Human Smad1, a mediator of BMP signals, is a transcriptional activator. of outstanding interest Nature. 381:1996;620-623 Smad1 is here shown to have transcriptional activity when fused to a heterologous DNA-binding domain; this activity is increased by the addition of BMP4 AND BMP type I and type II receptors. The carboxy-terminal domain of Smad1 is shown to be important in transcriptional activation. Overexpression of Smad1 in Xenopus ectoderm induces the formation of ventral mesoderm.
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Nature
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Liu, F.1
Hata, A.2
Baker, J.C.3
Doody, J.4
Carcamo, J.5
Harland, R.M.6
Massagúe, J.7
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25
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0029829230
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A novel mesoderm inducer, Madr2, functions in the activin signal transduction pathway
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of outstanding interest. Mouse Smad2 is here identified by expression cloning in the Xenopus ectoderm. Smad2 induces mesoderm from Xenopus ectoderm and can induce a secondary axis. Smad2 translocates into the nucleus in response to activin signaling. The carboxy-terminal domain of Smad2 translocates into the nucleus independently of activin signaling and is more potent at inducing mesoderm than the full-length protein.
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Baker JC, Harland RM. A novel mesoderm inducer, Madr2, functions in the activin signal transduction pathway. of outstanding interest Genes Dev. 10:1996;1880-1889 Mouse Smad2 is here identified by expression cloning in the Xenopus ectoderm. Smad2 induces mesoderm from Xenopus ectoderm and can induce a secondary axis. Smad2 translocates into the nucleus in response to activin signaling. The carboxy-terminal domain of Smad2 translocates into the nucleus independently of activin signaling and is more potent at inducing mesoderm than the full-length protein.
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(1996)
Genes Dev
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Baker, J.C.1
Harland, R.M.2
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26
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0029940972
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Xenopus mad proteins transduce distinct subsets of signals for the TGF-β Superfamily
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of special interest. Identification and functional analysis of Xenopus Smad1 and Smad2. Smad1 is shown to induce ventral mesoderm from Xenopus ectoderm, whereas Smad2 is shown to induce dorsal mesoderm from Xenopus ectoderm.
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Graff JM, Bansal A, Melton DA. Xenopus mad proteins transduce distinct subsets of signals for the TGF-β Superfamily. of special interest Cell. 85:1996;479-487 Identification and functional analysis of Xenopus Smad1 and Smad2. Smad1 is shown to induce ventral mesoderm from Xenopus ectoderm, whereas Smad2 is shown to induce dorsal mesoderm from Xenopus ectoderm.
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(1996)
Cell
, vol.85
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Graff, J.M.1
Bansal, A.2
Melton, D.A.3
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27
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0029834231
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Xenopus mothers against decapentaplegic is an embryonic ventralizing agent that acts downstream of the BMP 2/4 receptor
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Thomsen GH. Xenopus mothers against decapentaplegic is an embryonic ventralizing agent that acts downstream of the BMP 2/4 receptor. Development. 122:1996;2359-2366.
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Thomsen, G.H.1
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Smad5 induces ventral fates in Xenopus embryos
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Suzuki, A.1
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Hemmati-Brivanlou, A.5
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29
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0029834067
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Partnership between DPC4 and SMAD proteins in TGF-beta signaling pathways
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of outstanding interest. DPC4 is essential for the function of Smad1 and Smad2 during transcriptional responses in mammalian cells and in Xenopus mesodermal induction and patterning. DPC4 forms heterodimers with Smad1 in response to BMP and with Smad2 in response to activin or TGF-β.
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Lagna G, Hata A, Hemmati-Brivanlou A, Massagué J. Partnership between DPC4 and SMAD proteins in TGF-beta signaling pathways. of outstanding interest Nature. 383:1996;832-836 DPC4 is essential for the function of Smad1 and Smad2 during transcriptional responses in mammalian cells and in Xenopus mesodermal induction and patterning. DPC4 forms heterodimers with Smad1 in response to BMP and with Smad2 in response to activin or TGF-β.
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(1996)
Nature
, vol.383
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Lagna, G.1
Hata, A.2
Hemmati-Brivanlou, A.3
Massagué, J.4
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30
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16044369574
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Madr2 maps to 18q21 and encodes a TGF-β-regulated Mad-related protein that is functionally mutated in colorectal carcinoma
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of special interest. Smad2 is shown to be phosphorylated by TGF-β signaling. Mutational analysis of Smad2 in tumor cells identified four missense mutations in colorectal carcinomas.
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Eppert K, Scherer SW, Ozcelik H, Pirone R, Hoodless P, Kim H, Tsui LC, Bapat B, Gallinger S, Andrulis IL, et al. Madr2 maps to 18q21 and encodes a TGF-β-regulated Mad-related protein that is functionally mutated in colorectal carcinoma. of special interest Cell. 86:1996;543-552 Smad2 is shown to be phosphorylated by TGF-β signaling. Mutational analysis of Smad2 in tumor cells identified four missense mutations in colorectal carcinomas.
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(1996)
Cell
, vol.86
, pp. 543-552
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Eppert, K.1
Scherer, S.W.2
Ozcelik, H.3
Pirone, R.4
Hoodless, P.5
Kim, H.6
Tsui, L.C.7
Bapat, B.8
Gallinger, S.9
Andrulis, I.L.10
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31
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Mammalian dwarfins are phosphorylated in response to TGF-β And are implicated in control of cell growth
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Yingling JM, Das P, Savage C, Xhang C, Padgett RW. Mammalian dwarfins are phosphorylated in response to TGF-β and are implicated in control of cell growth. Proc Natl Acad Sci USA. 93:1996;8940-8944.
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Yingling, J.M.1
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Savage, C.3
Xhang, C.4
Padgett, R.W.5
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32
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0030300115
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MADR2 is a substrate of the TGF-β receptor and its phosphorylation is required for nuclear accumulation and signaling
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of outstanding interest. Three serines in the carboxyl terminus of Smad2 are shown to be critical for phosphorylation, nuclear localization and TGF-β signaling. Smad2 is shown to interact with receptors transiently and requires the activation of the type I receptor by the type II receptor.
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Macias-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 signaling. of outstanding interest Cell. 87:1996;1215-1224 Three serines in the carboxyl terminus of Smad2 are shown to be critical for phosphorylation, nuclear localization and TGF-β signaling. Smad2 is shown to interact with receptors transiently and requires the activation of the type I receptor by the type II receptor.
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(1996)
Cell
, vol.87
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MacIas-Silva, M.1
Abdollah, S.2
Hoodless, P.A.3
Pirone, R.4
Attisano, L.5
Wrana, J.L.6
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33
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0030911104
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The TGF-β family mediator Smad1 is phosphorylated directly and activated functionally by the BMP receptor kinase
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of outstanding interest. Smad1 contains three carboxy-terminal serines that are essential for phosphorylation, association with DPC4, accumulation in the nucleus, and transcriptional activity in response to BMP signaling. Smad2, but not DPC4, has similar carboxy-terminal serines which are required for phosphorylation and association with DPC4 in response to TGF-β signaling.
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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. of outstanding interest Genes Dev. 11:1997;984-995 Smad1 contains three carboxy-terminal serines that are essential for phosphorylation, association with DPC4, accumulation in the nucleus, and transcriptional activity in response to BMP signaling. Smad2, but not DPC4, has similar carboxy-terminal serines which are required for phosphorylation and association with DPC4 in response to TGF-β signaling.
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Genes Dev
, vol.11
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Kretzschmar, M.1
Liu, F.2
Hata, A.3
Doody, J.4
Massagué, J.5
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34
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0029786212
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Receptor-associated Mad homologues synergize as effectors of the TGF-β response
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of special interest. Identification and analysis of Smad3 and Smad4, which are shown to synergize to induce TGF-β-like responses in mammalian cells. Smad3 associates with and is phosphorylated by the TGF-β receptor complex.
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Zhang Y, Feng X-H, Wu RY, Derynck R. Receptor-associated Mad homologues synergize as effectors of the TGF-β response. of special interest Nature. 383:1996;168-172 Identification and analysis of Smad3 and Smad4, which are shown to synergize to induce TGF-β-like responses in mammalian cells. Smad3 associates with and is phosphorylated by the TGF-β receptor complex.
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Nature
, vol.383
, pp. 168-172
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Zhang, Y.1
Feng, X.-H.2
Wu, R.Y.3
Derynck, R.4
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35
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0029802485
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A transcriptional partner for MAD proteins in TGF-β signalling
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of outstanding interest. FAST-1 is identified as a winged-helix transcription factor which interacts with the ARE in the Mix.2 promoter. FAST-1 forms a complex with Smad2 in an activin-dependent fashion that generates an ARE-binding complex.
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Chen X, Rubock MJ, Whitman M. A transcriptional partner for MAD proteins in TGF-β signalling. of outstanding interest Nature. 383:1996;691-696 FAST-1 is identified as a winged-helix transcription factor which interacts with the ARE in the Mix.2 promoter. FAST-1 forms a complex with Smad2 in an activin-dependent fashion that generates an ARE-binding complex.
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Nature
, vol.383
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Chen, X.1
Rubock, M.J.2
Whitman, M.3
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A conserved system for dorsal-ventral patterning in insects and vertebrates involving sog and chordin
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Hoffman, F.M.6
Ferguson, E.L.7
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Human BMP sequences can confer normal dorsal-ventral patterning in the Drosophila embryo
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