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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 signalling pathways. Cell. 85:1996;489-500.
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Mad acts downstream of Dpp receptors, revealing a differential requirement for dpp signalling and propagation of morphogenesis in the Drosophila eye
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Wiersdorff, V.1
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Mothers against dpp encodes a conserved cytoplasmic protein required in DPP/TGFβ responsive cells
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Newfeld SJ, Chartoff EH, Graff JM, Melton DA, Gelbart WM. Mothers against dpp encodes a conserved cytoplasmic protein required in DPP/TGFβ responsive cells. Development. 122:1996;2099-2108.
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Savage C, Das P, Finelli A, Townsend S, Sun C, Baird S, Padgett R. The C. elegans sma-2, sma-3 and sma-4 genes define a novel conserved family of TGF-β pathway components. Proc Natl Acad Sci USA. 93:1996;790-794.
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0030837455
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A structural basis for mutational inactivation of the tumour suppressor Smad4
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of special interest. This paper describes the crystal structure of the MH2 domain, thus providing a look at the three-dimensional structure of a domain conserved in all Smad family members.
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Shi Y, Hata A, Lo RS, Massagué J, Pavletich NP. A structural basis for mutational inactivation of the tumour suppressor Smad4. of special interest Nature. 388:1997;87-93 This paper describes the crystal structure of the MH2 domain, thus providing a look at the three-dimensional structure of a domain conserved in all Smad family members.
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Nature
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Shi, Y.1
Hata, A.2
Lo, R.S.3
Massagué, J.4
Pavletich, N.P.5
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Baker JC, Harland R. A novel mesoderm inducer, Madr2, functions in the activin signal transduction pathway. Genes Dev. 10:1996;1880-1889.
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Baker, J.C.1
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Hata A, Lo RS, Wotton D, Lagna G, Massagué J. Mutations increasing autoinhibition inactivate tumour suppressors Smad2 and Smad4. Nature. 388:1997;82-87.
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Nature
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Hata, A.1
Lo, R.S.2
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Massagué, J.5
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10
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0031044107
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The C-terminal domain of Mad-like signal transducers is sufficient for biological activity in the Xenopus embryo and transcription activation
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Meersseman G, Verschueren K, Nelles L, Blumenstock C, Kraft H, Wuytens G, Remacle J, Kozak CA, Tylzanowski P, Niehrs C, Huylebroeck D. The C-terminal domain of Mad-like signal transducers is sufficient for biological activity in the Xenopus embryo and transcription activation. Mech Dev. 61:1997;127-140.
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Meersseman, G.1
Verschueren, K.2
Nelles, L.3
Blumenstock, C.4
Kraft, H.5
Wuytens, G.6
Remacle, J.7
Kozak, C.A.8
Tylzanowski, P.9
Niehrs, C.10
Huylebroeck, D.11
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11
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0030974042
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Heteromeric and homomeric interactions correlate with signaling activity and functional cooperativity of Smad3 and Smad4/DPC4
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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. 17:1997;2521-2528.
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Wu R-Y1
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Zhang Y, Musci T, Derynck R. The tumor suppressor Smad4/DPC4 as a central mediator of Smad function. Curr Biol. 7:1997;270-276.
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Zhang, Y.1
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Characterization of functional domains with Smad4/DPC4
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de Caestecker MP, Hemmati P, Larisch-Bloch S, Ajmera R, Roberts AB, Lechleider RJ. Characterization of functional domains with Smad4/DPC4. J Biol Chem. 272:1997;13690-13696.
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De Caestecker, M.P.1
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Ajmera, R.4
Roberts, A.B.5
Lechleider, R.J.6
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0030781598
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WW (WWP) domains: From structure to function
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Pawson A.S. Berlin: Springer-Verlag
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Rotin D. WW (WWP) domains: from structure to function. Pawson A.S. Current Topics in Microbiology and Immunology. 228:1997;115-133 Springer-Verlag, Berlin.
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Rotin, D.1
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Chen Y, Bhushan A, Vale W. Smad8 mediates the signalling of the receptor serine kinase. Proc Natl Acad Sci USA. 94:1997;12938-12943.
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Chen, Y.1
Bhushan, A.2
Vale, W.3
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16
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16044369574
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MADR2 maps to 18q21 and encodes a TGFβ MAD-related protein that is functionally mutated in colorectal carcinoma
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Eppert K, Scherer SW, Ozcelik H, Pirone R, Hoodless P, Kim H, Tsui L-C, Bapat B, Gallinger S, Andrulis I, et al. MADR2 maps to 18q21 and encodes a TGFβ MAD-related protein that is functionally mutated in colorectal carcinoma. Cell. 86:1996;543-552.
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Eppert, K.1
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Pirone, R.4
Hoodless, P.5
Kim, H.6
Tsui L-C7
Bapat, B.8
Gallinger, S.9
Andrulis, I.10
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17
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0030911104
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The TGF-β family mediator Smad 1 is phosphorylated directly and activated functionally by the BMP receptor kinase
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Kretzschmar M, Liu F, Hata A, Doody J, Massagué J. The TGF-β family mediator Smad 1 is phosphorylated directly and activated functionally by the BMP receptor kinase. Genes Dev. 11:1997;984-995.
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Kretzschmar, M.1
Liu, F.2
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Doody, J.4
Massagué, J.5
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18
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0030013242
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Serine phosphorylation, chromosomal localization and transforming growth factor-β signal transduction by human bsp-1
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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. 271:1996;17617-17620.
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Lechleider, R.1
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Dehejia, A.3
Polymeropoulos, M.H.4
Roberts, A.B.5
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19
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0030886204
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Transforming growth factor β-induced phosphorylation of Smad3 is required for growth inhibition and transcriptional induction in epithelial cells
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Liu X, Sun Y, Constantinescu SN, Karam E, Weinberg RA, Lodish HF. Transforming growth factor β-induced phosphorylation of Smad3 is required for growth inhibition and transcriptional induction in epithelial cells. Proc Natl Acad Sci USA. 94:1997;10669-10764.
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Liu, X.1
Sun, Y.2
Constantinescu, S.N.3
Karam, E.4
Weinberg, R.A.5
Lodish, H.F.6
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20
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0031034589
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Identification of Smad2, a human Mad-related protein in the transforming growth factor β is signaling pathway
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Nakao A, Rsijer E, Imamura T, Souchelnytskyi S, Stenman G, Heldin C-H, ten Dijke P. Identification of Smad2, a human Mad-related protein in the transforming growth factor β is signaling pathway. J Biol Chem. 272:1997;2896-2900.
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Nakao, A.1
Rsijer, E.2
Imamura, T.3
Souchelnytskyi, S.4
Stenman, G.5
Heldin C-H6
Ten Dijke, P.7
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21
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0029833909
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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, 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. 93:1996;8940-8944.
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Proc Natl Acad Sci USA
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Yingling, J.M.1
Das, P.2
Savage, C.3
Zhang, M.4
Padgett, R.W.5
Wang X-F6
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22
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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. This paper demonstrates for the first time that a receptor-regulated Smad, Smad3, synergistically interacts with Smad4 to mediate TGFβ signalling. A direct interaction of Smad3 with the TGFβ receptor complex is also demonstrated.
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Zhang Y, Feng X-H, Wu R-Y, Derynck R. Receptor-associated Mad homologues synergize as effectors of the TGF-β response. of special interest Nature. 383:1996;168-172 This paper demonstrates for the first time that a receptor-regulated Smad, Smad3, synergistically interacts with Smad4 to mediate TGFβ signalling. A direct interaction of Smad3 with the TGFβ receptor complex is also demonstrated.
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Nature
, vol.383
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Zhang, Y.1
Feng X-H2
Wu R-Y3
Derynck, R.4
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23
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A human Mad protein acting as BMP-regulated transcriptional activator
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Liu F, Hata A, Baker J, Doody J, Cárcamo J, Harland R, Massagué J. A human Mad protein acting as BMP-regulated transcriptional activator. Nature. 381:1996;620-623.
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Nature
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Liu, F.1
Hata, A.2
Baker, J.3
Doody, J.4
Cárcamo, J.5
Harland, R.6
Massagué, J.7
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24
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0030300115
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MADR2 is substrate of the TGFβ receptor and its phosphorylation is required for nuclear accumulation and signalling
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of outstanding interest. This paper demonstrated that Smads are substrates of the type I receptor, identified the SSXS motif as the target of phosphorylation and showed that phosphorylation at this site was required to induce nuclear accumulation of Smads. This work defined the role of receptor-regulated Smads in transmitting signals directly from the receptor kinase into the nucleus.
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Maclas-Silva M, Abdollah S, Hoodless PA, Pirone R, Attisano L, Wrana JL. MADR2 is substrate of the TGFβ receptor and its phosphorylation is required for nuclear accumulation and signalling. of outstanding interest Cell. 87:1996;1215-1224 This paper demonstrated that Smads are substrates of the type I receptor, identified the SSXS motif as the target of phosphorylation and showed that phosphorylation at this site was required to induce nuclear accumulation of Smads. This work defined the role of receptor-regulated Smads in transmitting signals directly from the receptor kinase into the nucleus.
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(1996)
Cell
, vol.87
, pp. 1215-1224
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MacLas-Silva, M.1
Abdollah, S.2
Hoodless, P.A.3
Pirone, R.4
Attisano, L.5
Wrana, J.L.6
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25
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0030768644
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TGF-β receptor-mediated signalling through Smad2, Smad3 and Smad4
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Nakao A, Imamura T, Souchelnytskyi S, Kawabata M, Ishisaki A, Oeda E, Tamaki K, Hanai J-I, Heldin C-H, Miyazono K, et al. TGF-β receptor-mediated signalling through Smad2, Smad3 and Smad4. EMBO J. 16:1997;5353-5362.
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EMBO J
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Nakao, A.1
Imamura, T.2
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Kawabata, M.4
Ishisaki, A.5
Oeda, E.6
Tamaki, K.7
Hanai J-I8
Heldin C-H9
Miyazono, K.10
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26
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0030885190
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Mothers against dpp participates in a DPP/TGF-β responsive serine-threonine kinase signal transduction cascade
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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. 124:1997;3167-3176.
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Development
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Newfeld, S.J.1
Mehra, A.2
Singer, M.A.3
Wrana, J.L.4
Attisano, L.5
Gelbart, W.M.6
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27
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0029940972
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Xenopus Mad porteins transduce distinct subsets of signals for the TGFβ superfamily
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of outstanding interest. This paper showed that expression of Smad1 and Smad2 in Xenopus oocytes leads to distinct biological responses associated with BMP and TGFβ/activin respectively, thus providing the first indication the Smads provide specificity in signalling by the TGFβ superfamily.
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Graff JM, Bansal A, Melton DA. Xenopus Mad porteins transduce distinct subsets of signals for the TGFβ superfamily. of outstanding interest Cell. 85:1996;479-487 This paper showed that expression of Smad1 and Smad2 in Xenopus oocytes leads to distinct biological responses associated with BMP and TGFβ/activin respectively, thus providing the first indication the Smads provide specificity in signalling by the TGFβ superfamily.
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(1996)
Cell
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Graff, J.M.1
Bansal, A.2
Melton, D.A.3
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28
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0031569819
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Smad5 induces ventral fates in Xenopus embryo
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Suzuki A, Chang C, Yingling J, Wang X-F, Hemmati-Brivanlou A. Smad5 induces ventral fates in Xenopus embryo. Dev Biol. 184:1997;402-405.
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Dev Biol
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Suzuki, A.1
Chang, C.2
Yingling, J.3
Wang X-F4
Hemmati-Brivanlou, A.5
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29
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0029834231
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Xenopus mothers against decapentaplegic is an embryonic ventralizing agent that acts downstream of the BMP2/4 receptor
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Thomsen GH. Xenopus mothers against decapentaplegic is an embryonic ventralizing agent that acts downstream of the BMP2/4 receptor. Development. 122:1996;2359-2366.
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Development
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Thomsen, G.H.1
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30
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0030613249
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Tβ R1 phosphorylation of Smad2 on Ser 465 and 467 is required for Smad2/Smad4 complex formation and signalling
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Abdollah S, Maclas-Silva M, Tsukazaki T, Hayashi H, Attisano L, Wrana JL. Tβ R1 phosphorylation of Smad2 on Ser 465 and 467 is required for Smad2/Smad4 complex formation and signalling. J Biol Chem. 272:1997;27678-27685.
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J Biol Chem
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Abdollah, S.1
MacLas-Silva, M.2
Tsukazaki, T.3
Hayashi, H.4
Attisano, L.5
Wrana, J.L.6
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32
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0030926005
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A kinase subdomain of transforming growth factor-β (TGF-β) type 1 receptor determines the TGF-β intracellular signaling specificity
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Feng X-H, Derynck R. A kinase subdomain of transforming growth factor-β (TGF-β) type 1 receptor determines the TGF-β intracellular signaling specificity. EMBO J. 16:1997;3912-3923.
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EMBO J
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Feng X-H1
Derynck, R.2
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33
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0029834067
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Partnership between DPC4 and SMAD proteins in TGF-β signalling pathways
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of outstanding interest. This paper demonstrates biochemically and biologically, using a Xenopus assay, that Smad4 is an essential mediator of both TGFβ/activin and BMP signals. The authors show that Smad4 forms heteromeric complexes with Smad1 and Smad2 and thus may function as a common mediator of all TGFβ superfamily signals.
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Lagna G, Hata A, Hemmati-Brivanlou A, Massagué J. Partnership between DPC4 and SMAD proteins in TGF-β signalling pathways. of outstanding interest Nature. 383:1996;832-836 This paper demonstrates biochemically and biologically, using a Xenopus assay, that Smad4 is an essential mediator of both TGFβ/activin and BMP signals. The authors show that Smad4 forms heteromeric complexes with Smad1 and Smad2 and thus may function as a common mediator of all TGFβ superfamily signals.
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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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34
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0030690337
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Dual role of the Smad4/DPC4 tumor suppressor in TGFβ-inducible transcriptional complexes
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Liu F, Pouponnot C, Massagué J. Dual role of the Smad4/DPC4 tumor suppressor in TGFβ-inducible transcriptional complexes. Genes Dev. 11:1997;3157-3167.
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Liu, F.1
Pouponnot, C.2
Massagué, J.3
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35
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0030663881
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Cellular interpretation of multiple TGF-β signals: Intracellular antagonism between activin/BVg1 and BMP-2/4 signalling mediated by Smads
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Candia AF, Watabe T, Hawley SB, Onichtchouk D, Zhang Y, Derynck R, Niehrs C, Cho KY. Cellular interpretation of multiple TGF-β signals: intracellular antagonism between activin/BVg1 and BMP-2/4 signalling mediated by Smads. Development. 124:1997;4467-4480.
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Development
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Candia, A.F.1
Watabe, T.2
Hawley, S.B.3
Onichtchouk, D.4
Zhang, Y.5
Derynck, R.6
Niehrs, C.7
Cho, K.Y.8
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36
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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. This paper describes the identification of a novel forkhead-containing transcription factor from Xenopus, named and FAST1. FAST1 was shown to bind to an activin-rsponse element in the Mix.2 promoter and form a transcriptional activation complex, together with Smad2. Thus, it is the first demonstration of a nuclear target for Smad2.
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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 This paper describes the identification of a novel forkhead-containing transcription factor from Xenopus, named and FAST1. FAST1 was shown to bind to an activin-rsponse element in the Mix.2 promoter and form a transcriptional activation complex, together with Smad2. Thus, it is the first demonstration of a nuclear target for Smad2.
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(1996)
Nature
, vol.383
, pp. 691-696
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Chen, X.1
Rubock, M.J.2
Whitman, M.3
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37
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0030961168
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Smad4 and FAST-1 in the assembly of activin-responsive factor
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Chen X, Weisberg E, Fridmacher V, Watanabe M, Naco G, Whitman M. Smad4 and FAST-1 in the assembly of activin-responsive factor. Nature. 389:1997;85-89.
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(1997)
Nature
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Chen, X.1
Weisberg, E.2
Fridmacher, V.3
Watanabe, M.4
Naco, G.5
Whitman, M.6
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38
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0031463308
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XSmad2 directly activates the activin-inducible dorsal mesoderm gene XFKH1 in Xenopus embryos
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Howell M, Hill C. XSmad2 directly activates the activin-inducible dorsal mesoderm gene XFKH1 in Xenopus embryos. EMBO J. 16:1997;7411-7421.
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EMBO J
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Howell, M.1
Hill, C.2
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39
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0030872367
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Drosophila Mad binds to DNA and directly mediates activation of vestigial by decapentaplegic
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of special interest. This paper characterized a Dpp-responsive element in the quadrant enhancer of the vestigial gene and showed that the MH1 domain of Mad can directly bind to the element. Mutations that block binding of Mad prevented activation of the element in vivo, thereby poviding evidence that Smads can directly bind DNA to activate transcription.
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Kim J, Johnson K, Chen HJ, Carroll S, Laughon A. Drosophila Mad binds to DNA and directly mediates activation of vestigial by decapentaplegic. of special interest Nature. 388:1997;304-308 This paper characterized a Dpp-responsive element in the quadrant enhancer of the vestigial gene and showed that the MH1 domain of Mad can directly bind to the element. Mutations that block binding of Mad prevented activation of the element in vivo, thereby poviding evidence that Smads can directly bind DNA to activate transcription.
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(1997)
Nature
, vol.388
, pp. 304-308
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Kim, J.1
Johnson, K.2
Chen, H.J.3
Carroll, S.4
Laughon, A.5
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40
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0030897846
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A CREB-binding site as a target for decapentaplegic signalling during Drosophila endoderm induction
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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. 16:1997;2014-2022.
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(1997)
EMBO J
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Eresh, S.1
Riese, J.2
Jackson, D.B.3
Bohmann, D.4
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