메뉴 건너뛰기




Volumn 385, Issue 8, 2004, Pages 697-710

Molecular recognition in bone morphogenetic protein (BMP)/receptor interaction

Author keywords

Binding determinants; Functional epitope; Modulator protein; Muteins; Receptor ectodomain; TGF like protein

Indexed keywords

BONE MORPHOGENETIC PROTEIN; BONE MORPHOGENETIC PROTEIN 2; BONE MORPHOGENETIC PROTEIN RECEPTOR; EPITOPE; NOGGIN; TRANSFORMING GROWTH FACTOR BETA; TRANSFORMING GROWTH FACTOR BETA RECEPTOR; TRANSFORMING GROWTH FACTOR BETA2;

EID: 4544286802     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: 10.1515/BC.2004.086     Document Type: Review
Times cited : (128)

References (129)
  • 1
    • 0036051343 scopus 로고    scopus 로고
    • Connective-tissue growth factor (CTGF) modulates cell signalling by BMP and TGF-β
    • Abreu, J. G., Ketpura, N. I., Reversade, B., and De Robertis, E. M. (2002). Connective-tissue growth factor (CTGF) modulates cell signalling by BMP and TGF-β. Nat. Cell. Biol 4, 599-604.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 599-604
    • Abreu, J.G.1    Ketpura, N.I.2    Reversade, B.3    De Robertis, E.M.4
  • 2
    • 0347916881 scopus 로고    scopus 로고
    • Comparative genomic analysis of the eight-membered ring cystine knot-containing bone morphogenetic protein antagonists
    • Avsian-Kretchmer, O., and Hsueh, A. J. (2004). Comparative genomic analysis of the eight-membered ring cystine knot-containing bone morphogenetic protein antagonists. Mol. Enclocrinol. 18, 1-12.
    • (2004) Mol. Endocrinol. , vol.18 , pp. 1-12
    • Avsian-Kretchmer, O.1    Hsueh, A.J.2
  • 3
    • 0036399170 scopus 로고    scopus 로고
    • Extracellular regulation of BMP signaling in vertebrates: A cocktail of modulators
    • Balemans, W., and Van Hul, W. (2002). Extracellular regulation of BMP signaling in vertebrates: a cocktail of modulators. Dev. Biol. 250, 231-250.
    • (2002) Dev. Biol. , vol.250 , pp. 231-250
    • Balemans, W.1    Van Hul, W.2
  • 4
    • 0033966734 scopus 로고    scopus 로고
    • Combinatorial signaling through BMP receptor IB and GDF5: Shaping of the distal mouse limb and the genetics of distal limb diversity
    • Baur, S. T., Mai, J. J., and Dymecki, S. M. (2000). Combinatorial signaling through BMP receptor IB and GDF5: shaping of the distal mouse limb and the genetics of distal limb diversity. Development 127, 605-619.
    • (2000) Development , vol.127 , pp. 605-619
    • Baur, S.T.1    Mai, J.J.2    Dymecki, S.M.3
  • 5
    • 0037417787 scopus 로고    scopus 로고
    • Determination of the energetics governing the regulatory step in growth hormone-induced receptor homodimerization
    • Bernat, B., Pal, G., Sun, M., and Kossiakoff, A. A. (2003). Determination of the energetics governing the regulatory step in growth hormone-induced receptor homodimerization. Proc. Natl. Acad. Sci. USA 100, 952-957.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 952-957
    • Bernat, B.1    Pal, G.2    Sun, M.3    Kossiakoff, A.A.4
  • 6
    • 0029834634 scopus 로고    scopus 로고
    • Overexpression of bone morphogenetic protein-6 (BMP-6) in the epidermis of transgenic mice: Inhibition or stimulation of proliferation depending on the pattern of transgene expression and formation of psoriatic lesions
    • Blessing, M., Schirmacher, P., and Kaiser, S. (1996). Overexpression of bone morphogenetic protein-6 (BMP-6) in the epidermis of transgenic mice: inhibition or stimulation of proliferation depending on the pattern of transgene expression and formation of psoriatic lesions. J. Cell Biol. 135, 227-239.
    • (1996) J. Cell Biol. , vol.135 , pp. 227-239
    • Blessing, M.1    Schirmacher, P.2    Kaiser, S.3
  • 7
    • 0036069143 scopus 로고    scopus 로고
    • The 1.1 Å crystal structure of human TGF-β type II receptor ligand binding domain
    • Boesen, C. C., Radaev, S., Motyka, S. A., Patamawenu, A., and Sun, P. D. (2002). The 1.1 Å crystal structure of human TGF-β type II receptor ligand binding domain. Structure 10, 913-919.
    • (2002) Structure , vol.10 , pp. 913-919
    • Boesen, C.C.1    Radaev, S.2    Motyka, S.A.3    Patamawenu, A.4    Sun, P.D.5
  • 9
    • 0242668869 scopus 로고    scopus 로고
    • Bone morphogenetic proteins, their antagonists, and the skeleton
    • Canalis, E., Economides, A. N., and Gazzerro, E. (2003). Bone morphogenetic proteins, their antagonists, and the skeleton. Endocr. Rev. 24, 218-235.
    • (2003) Endocr. Rev. , vol.24 , pp. 218-235
    • Canalis, E.1    Economides, A.N.2    Gazzerro, E.3
  • 10
    • 0032540358 scopus 로고    scopus 로고
    • Structural and functional analysis of the 1:1 growth hormone: Receptor complex reveals the molecular basis for receptor affinity
    • Clackson, T., Ultsch, M. H., Wells, J. A., and de Vos, A. M. (1998). Structural and functional analysis of the 1:1 growth hormone: receptor complex reveals the molecular basis for receptor affinity. J. Mol. Biol. 277, 1111-1128.
    • (1998) J. Mol. Biol. , vol.277 , pp. 1111-1128
    • Clackson, T.1    Ultsch, M.H.2    Wells, J.A.3    de Vos, A.M.4
  • 11
    • 0028916599 scopus 로고
    • A hot spot of binding energy in a hormone-receptor interface
    • Clackson, T., and Wells, J. A. (1995). A hot spot of binding energy in a hormone-receptor interface. Science 267, 383-386.
    • (1995) Science , vol.267 , pp. 383-386
    • Clackson, T.1    Wells, J.A.2
  • 12
    • 0027132013 scopus 로고
    • Comparison of a structural and a functional epitope
    • [Erratum published in J. Mol. Biol. 237 (1994), p. 513]
    • Cunningham, B. C., and Wells, J. A. (1993). Comparison of a structural and a functional epitope. J. Mol. Biol. 234, 554-563. [Erratum published in J. Mol. Biol. 237 (1994), p. 513]
    • (1993) J. Mol. Biol. , vol.234 , pp. 554-563
    • Cunningham, B.C.1    Wells, J.A.2
  • 13
    • 0027122245 scopus 로고
    • Crystal structure of transforming growth factor-β2: An unusual fold for the superfamily
    • Daopin, S., Piez, K. A., Ogawa, Y., and Davies, D. R. (1992). Crystal structure of transforming growth factor-β2: an unusual fold for the superfamily. Science 257, 369-373.
    • (1992) Science , vol.257 , pp. 369-373
    • Daopin, S.1    Piez, K.A.2    Ogawa, Y.3    Davies, D.R.4
  • 14
    • 0026598960 scopus 로고
    • Human growth hormone and extracellular domain of its receptor: Crystal structure of the complex
    • de Vos, A. M., Ultsch, M., and Kossiakoff, A. A. (1992). Human growth hormone and extracellular domain of its receptor: crystal structure of the complex. Science 255, 306-312.
    • (1992) Science , vol.255 , pp. 306-312
    • de Vos, A.M.1    Ultsch, M.2    Kossiakoff, A.A.3
  • 15
    • 0042825676 scopus 로고    scopus 로고
    • Solution structure and backbone dynamics of the TGFβ type II receptor extracellular domain
    • Deep, S., Walker, K. P., 3rd, Shu, Z., and Hinck, A. P. (2003). Solution structure and backbone dynamics of the TGFβ type II receptor extracellular domain. Biochemistry 42, 10126-10139.
    • (2003) Biochemistry , vol.42 , pp. 10126-10139
    • Deep, S.1    Walker III, K.P.2    Shu, Z.3    Hinck, A.P.4
  • 16
    • 0034652207 scopus 로고    scopus 로고
    • Efficient studies of long-distance Bmp5 gene regulation using bacterial artificial chromosomes
    • DiLeone, R. J., Marcus, G. A., Johnson, M. D., and Kingsley, D. M. (2000). Efficient studies of long-distance Bmp5 gene regulation using bacterial artificial chromosomes. Proc. Natl. Acad. Sci. USA 97, 1612-1617.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 1612-1617
    • DiLeone, R.J.1    Marcus, G.A.2    Johnson, M.D.3    Kingsley, D.M.4
  • 17
    • 0029861824 scopus 로고    scopus 로고
    • Growth differentiation factor-9 is required during early ovarian folliculogenesis
    • Dong, J., Albertini, D. F., Nishimori, K., Kumar, T. R., Lu, N., and Matzuk, M. M. (1996). Growth differentiation factor-9 is required during early ovarian folliculogenesis. Nature 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
  • 18
    • 0032873465 scopus 로고    scopus 로고
    • Connective tissue growth factor mediates transforming growth factor beta-induced collagen synthesis: Down-regulation by cAMP
    • Duncan, M. R., Frazier, K. S., Abramson, S., Williams, S., Klapper, H., Huang, X., and Grotendorst, G. R. (1999). Connective tissue growth factor mediates transforming growth factor beta-induced collagen synthesis: down-regulation by cAMP. FASEB J. 13, 1774-1786.
    • (1999) FASEB J. , vol.13 , pp. 1774-1786
    • Duncan, M.R.1    Frazier, K.S.2    Abramson, S.3    Williams, S.4    Klapper, H.5    Huang, X.6    Grotendorst, G.R.7
  • 19
    • 0035065478 scopus 로고    scopus 로고
    • How does the mouse get its trunk?
    • Dunn, N. R., and Hogan, B. L. (2001). How does the mouse get its trunk? Nat. Genet. 27, 351-352.
    • (2001) Nat. Genet. , vol.27 , pp. 351-352
    • Dunn, N.R.1    Hogan, B.L.2
  • 20
  • 21
    • 0030989670 scopus 로고    scopus 로고
    • X-ray structure of glial cell-derived neurotrophic factor at 1.9 Å resolution and implications for receptor binding
    • Eigenbrot, C., and Gerber, N. (1997). X-ray structure of glial cell-derived neurotrophic factor at 1.9 Å resolution and implications for receptor binding. Nat. Struct. Biol. 4, 435-438.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 435-438
    • Eigenbrot, C.1    Gerber, N.2
  • 22
    • 0344423815 scopus 로고    scopus 로고
    • Distinct structural elements in GDNF mediate binding to GFRα1 and activation of the GFRα1-c-Ret receptor complex
    • Eketjall, S., Fainzilber, M., Murray Rust, J., and Ibanez, C. F. (1999). Distinct structural elements in GDNF mediate binding to GFRα1 and activation of the GFRα1-c-Ret receptor complex. EMBO J. 18, 5901-5910.
    • (1999) EMBO J. , vol.18 , pp. 5901-5910
    • Eketjall, S.1    Fainzilber, M.2    Murray Rust, J.3    Ibanez, C.F.4
  • 23
    • 0035105355 scopus 로고    scopus 로고
    • Three-dimensional structure of human follicle-stimulating hormone
    • Fox, K. M., Dias, J. A., and Van Roey, P. (2001). Three-dimensional structure of human follicle-stimulating hormone. Mol. Endocrinol. 15, 378-389.
    • (2001) Mol. Endocrinol. , vol.15 , pp. 378-389
    • Fox, K.M.1    Dias, J.A.2    Van Roey, P.3
  • 24
    • 0345426298 scopus 로고    scopus 로고
    • Three different noggin genes antagonize the activity of bone morphogenetic proteins in the zebrafish embryo
    • Furthauer, M., Thisse, B., and Thisse, C. (1999). Three different noggin genes antagonize the activity of bone morphogenetic proteins in the zebrafish embryo. Dev. Biol. 214, 181-196.
    • (1999) Dev. Biol. , vol.214 , pp. 181-196
    • Furthauer, M.1    Thisse, B.2    Thisse, C.3
  • 26
    • 0037012541 scopus 로고    scopus 로고
    • Chordin-like CR domains and the regulation of evolutionarily conserved extracellular signaling systems
    • Garcia Abreu, J., Coffinier, C., Larrain, J., Oelgeschlager, M., and De Robertis, E. M. (2002). Chordin-like CR domains and the regulation of evolutionarily conserved extracellular signaling systems. Gene 287, 39-47.
    • (2002) Gene , vol.287 , pp. 39-47
    • Garcia Abreu, J.1    Coffinier, C.2    Larrain, J.3    Oelgeschlager, M.4    De Robertis, E.M.5
  • 27
    • 0032559594 scopus 로고    scopus 로고
    • Oligomeric structure of type I and type II transforming growth factor β receptors: Homodimers form in the ER and persist at the plasma membrane
    • Gilboa, L., Wells, R. G., Lodish, H. F., and Henis, Y. I. (1998). Oligomeric structure of type I and type II transforming growth factor β receptors: homodimers form in the ER and persist at the plasma membrane. J. Cell Biol. 140, 767-777.
    • (1998) J. Cell Biol. , vol.140 , pp. 767-777
    • Gilboa, L.1    Wells, R.G.2    Lodish, H.F.3    Henis, Y.I.4
  • 28
    • 0034021776 scopus 로고    scopus 로고
    • Bone morphogenetic protein receptor complexes on the surface of live cells: A new oligomerization mode for serine/threonine kinase receptors
    • Gilboa, L., Nohe, A., Geissendorfer, T., Sebald, W., Henis, Y. I., and Knaus, P. (2000). Bone morphogenetic protein receptor complexes on the surface of live cells: a new oligomerization mode for serine/threonine kinase receptors. Mol. Biol. Cell 11, 1023-1035.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 1023-1035
    • Gilboa, L.1    Nohe, A.2    Geissendorfer, T.3    Sebald, W.4    Henis, Y.I.5    Knaus, P.6
  • 29
    • 0037170462 scopus 로고    scopus 로고
    • Antagonism of activin by inhibin and inhibin receptors: A functional role for betaglycan
    • Gray, P. C., Bilezikjian, L. M., and Vale, W. (2002). Antagonism of activin by inhibin and inhibin receptors: a functional role for betaglycan. Mol. Cell. Endocrinol. 188, 254-260.
    • (2002) Mol. Cell Endocrinol. , vol.188 , pp. 254-260
    • Gray, P.C.1    Bilezikjian, L.M.2    Vale, W.3
  • 30
    • 0032899751 scopus 로고    scopus 로고
    • Three-finger toxin fold for the extracellular ligand-binding domain of the type II activin receptor serine kinase
    • Greenwald, J., Fischer, W. H., Vale, W. W., and Choe, S. (1999). Three-finger toxin fold for the extracellular ligand-binding domain of the type II activin receptor serine kinase. Nat. Struct. Biol. 6, 18-22.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 18-22
    • Greenwald, J.1    Fischer, W.H.2    Vale, W.W.3    Choe, S.4
  • 31
    • 0037351880 scopus 로고    scopus 로고
    • The BMP7/ActRII extracellular domain complex provides new insights into the cooperative nature of receptor assembly
    • Greenwald, J., Groppe, J., Gray, P., Wiater, E., Kwiatkowski, W., Vale, W., and Choe, S. (2003). The BMP7/ActRII extracellular domain complex provides new insights into the cooperative nature of receptor assembly. Mol. Cell 11, 605-617.
    • (2003) Mol. Cell , vol.11 , pp. 605-617
    • Greenwald, J.1    Groppe, J.2    Gray, P.3    Wiater, E.4    Kwiatkowski, W.5    Vale, W.6    Choe, S.7
  • 32
    • 0030042590 scopus 로고    scopus 로고
    • Three-dimensional structure of recombinant human osteogenic protein 1: Structural paradigm for the transforming growth factor β superfamily
    • Griffith, D. L., Keck, P. C., Sampath, T. K., Rueger, D. C., and Carlson, W. D. (1996). Three-dimensional structure of recombinant human osteogenic protein 1: structural paradigm for the transforming growth factor β superfamily. Proc. Natl. Acad. Sci. USA 93, 878-883.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 878-883
    • Griffith, D.L.1    Keck, P.C.2    Sampath, T.K.3    Rueger, D.C.4    Carlson, W.D.5
  • 34
    • 0031225015 scopus 로고    scopus 로고
    • Connective tissue growth factor: A mediator of TGF-β action on fibroblasts
    • Grotendorst, G. R. (1997). Connective tissue growth factor: a mediator of TGF-β action on fibroblasts. Cytokine Growth Factor Rev. 8, 171-179.
    • (1997) Cytokine. Growth Factor Rev. , vol.8 , pp. 171-179
    • Grotendorst, G.R.1
  • 37
    • 0141833839 scopus 로고    scopus 로고
    • A role for connective tissue growth factor in the pathogenesis of choroidal neovascularization
    • He, S., Jin, M. L., Worpel, V., and Hinton, D. R. (2003). A role for connective tissue growth factor in the pathogenesis of choroidal neovascularization. Arch. Ophthalmol. 121, 1283-1288.
    • (2003) Arch. Ophthalmol. , vol.121 , pp. 1283-1288
    • He, S.1    Jin, M.L.2    Worpel, V.3    Hinton, D.R.4
  • 38
    • 0028838012 scopus 로고
    • Dimerization of cell surface receptors in signal transduction
    • Heldin, C. H. (1995). Dimerization of cell surface receptors in signal transduction. Cell 80, 213-223.
    • (1995) Cell , vol.80 , pp. 213-223
    • Heldin, C.H.1
  • 39
    • 0030183048 scopus 로고    scopus 로고
    • Ligand-induced dimerization of growth factor receptors: Variations on the theme
    • Heldin, C. H., and Ostman, A. (1996). Ligand-induced dimerization of growth factor receptors: variations on the theme. Cytokine Growth Factor Rev. 7, 3-10.
    • (1996) Cytokine. Growth Factor Rev. , vol.7 , pp. 3-10
    • Heldin, C.H.1    Ostman, A.2
  • 40
    • 0031438047 scopus 로고    scopus 로고
    • TGF-β signalling from cell membrane to nucleus through SMAD proteins
    • Heldin, C. H., Miyazono, K., and ten Dijke, P. (1997). TGF-β signalling from cell membrane to nucleus through SMAD proteins. Nature 390, 465-471.
    • (1997) Nature , vol.390 , pp. 465-471
    • Heldin, C.H.1    Miyazono, K.2    ten Dijke, P.3
  • 41
    • 0028291369 scopus 로고
    • The types II and III transforming growth factor-β receptors form homo-oligomers
    • Henis, Y. I., Moustakas, A., Lin, H. Y., and Lodish, H. F. (1994). The types II and III transforming growth factor-β receptors form homo-oligomers. J. Cell Biol. 126, 139-154.
    • (1994) J. Cell Biol. , vol.126 , pp. 139-154
    • Henis, Y.I.1    Moustakas, A.2    Lin, H.Y.3    Lodish, H.F.4
  • 43
    • 0030218004 scopus 로고    scopus 로고
    • Bone morphogenetic proteins in development
    • Hogan, B. L. (1996). Bone morphogenetic proteins in development. Curr. Opin. Genet. Dev. 6, 432-438.
    • (1996) Curr. Opin. Genet. Dev. , vol.6 , pp. 432-438
    • Hogan, B.L.1
  • 44
    • 0039797251 scopus 로고    scopus 로고
    • Transforming growth factor β peptide antagonists and their conversion to partial agonists
    • Huang, S. S., Liu, Q., Johnson, F. E., Konish, Y., and Huang, J. S. (1997). Transforming growth factor β peptide antagonists and their conversion to partial agonists. J. Biol. Chem. 272, 27155-27159.
    • (1997) J. Biol. Chem. , vol.272 , pp. 27155-27159
    • Huang, S.S.1    Liu, Q.2    Johnson, F.E.3    Konish, Y.4    Huang, J.S.5
  • 45
    • 0033524943 scopus 로고    scopus 로고
    • Crystal structure of the cytoplasmic domain of the type I TGFβ receptor in complex with FKBP12
    • Huse, M., Chen, Y. G., Massague, J., and Kuriyan, J. (1999). Crystal structure of the cytoplasmic domain of the type I TGFβ receptor in complex with FKBP12. Cell 96, 425-436.
    • (1999) Cell , vol.96 , pp. 425-436
    • Huse, M.1    Chen, Y.G.2    Massague, J.3    Kuriyan, J.4
  • 46
    • 0031860389 scopus 로고    scopus 로고
    • Skeletal abnormalities in doubly heterozygous Bmp4 and Bmp7 mice
    • Katagiri, T., Boorla, S., Frendo, J. L., Hogan, B. L., and Karsenty, G. (1998). Skeletal abnormalities in doubly heterozygous Bmp4 and Bmp7 mice. Dev. Genet. 22, 340-348.
    • (1998) Dev. Genet. , vol.22 , pp. 340-348
    • Katagiri, T.1    Boorla, S.2    Frendo, J.L.3    Hogan, B.L.4    Karsenty, G.5
  • 48
    • 0042681786 scopus 로고    scopus 로고
    • Bidirectional transmembrane signaling by cytoplasmic domain separation in integrins
    • Kim, M., Carman, C. V., and Springer, T. A. (2003). Bidirectional transmembrane signaling by cytoplasmic domain separation in integrins. Science 301, 1720-1725.
    • (2003) Science , vol.301 , pp. 1720-1725
    • Kim, M.1    Carman, C.V.2    Springer, T.A.3
  • 49
    • 0027976891 scopus 로고
    • What do BMPs do in mammals? Clues from the mouse short-ear mutation
    • Kingsley, D. M. (1994). What do BMPs do in mammals? Clues from the mouse short-ear mutation. Trends Genet. 10, 16-21.
    • (1994) Trends Genet. , vol.10 , pp. 16-21
    • Kingsley, D.M.1
  • 50
    • 0034600953 scopus 로고    scopus 로고
    • BMP-2 antagonists emerge from alterations in the low-affinity binding epitope for receptor BMPR-II
    • Kirsch, T., Nickel, J., and Sebald, W. (2000a). BMP-2 antagonists emerge from alterations in the low-affinity binding epitope for receptor BMPR-II. EMBO J. 19, 3314-3324.
    • (2000) EMBO J. , vol.19 , pp. 3314-3324
    • Kirsch, T.1    Nickel, J.2    Sebald, W.3
  • 51
    • 0034043106 scopus 로고    scopus 로고
    • Crystal structure of the BMP-2-BRIA ectodomain complex
    • Kirsch, T., Sebald, W., and Dreyer, M. K. (2000b). Crystal structure of the BMP-2-BRIA ectodomain complex. Nat. Struct. Biol. 7, 492-496.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 492-496
    • Kirsch, T.1    Sebald, W.2    Dreyer, M.K.3
  • 52
    • 0034826931 scopus 로고    scopus 로고
    • Cooperativity of binding epitopes and receptor chains in the BMP/TGFβ superfamily
    • Knaus, P., and Sebald, W. (2001). Cooperativity of binding epitopes and receptor chains in the BMP/TGFβ superfamily. Biol. Chem. 382, 1189-1195.
    • (2001) Biol. Chem. , vol.382 , pp. 1189-1195
    • Knaus, P.1    Sebald, W.2
  • 54
    • 0038267120 scopus 로고    scopus 로고
    • Sclerostin is a novel secreted osteoclast-derived bone morphogenetic protein antagonist with unique ligand specificity
    • Kusu, N., Laurikkala, J., Imanishi, M., Usui, H., Konishi, M., Miyake, A., Thesleff, I., and Itoh, N. (2003). Sclerostin is a novel secreted osteoclast-derived bone morphogenetic protein antagonist with unique ligand specificity. J. Biol. Chem. 278, 24113-24117.
    • (2003) J. Biol. Chem. , vol.278 , pp. 24113-24117
    • Kusu, N.1    Laurikkala, J.2    Imanishi, M.3    Usui, H.4    Konishi, M.5    Miyake, A.6    Thesleff, I.7    Itoh, N.8
  • 56
    • 0034010982 scopus 로고    scopus 로고
    • BMP-binding modules in chordin: A model for signalling regulation in the extracellular space
    • Larrain, J., Bachiller, D., Lu, B., Agius, E., Piccolo, S., and De Robertis, E. M. (2000). BMP-binding modules in chordin: a model for signalling regulation in the extracellular space. Development 127, 821-830.
    • (2000) Development , vol.127 , pp. 821-830
    • Larrain, J.1    Bachiller, D.2    Lu, B.3    Agius, E.4    Piccolo, S.5    De Robertis, E.M.6
  • 57
    • 0035205079 scopus 로고    scopus 로고
    • Proteolytic cleavage of Chordin as a switch for the dual activities of Twisted gastrulation in BMP signaling
    • Larrain, J., Oelgeschlager, M., Ketpura, N. I., Reversade, B., Zakin, L., and De Robertis, E. M. (2001). Proteolytic cleavage of Chordin as a switch for the dual activities of Twisted gastrulation in BMP signaling. Development 128, 4439-4447.
    • (2001) Development , vol.128 , pp. 4439-4447
    • Larrain, J.1    Oelgeschlager, M.2    Ketpura, N.I.3    Reversade, B.4    Zakin, L.5    De Robertis, E.M.6
  • 58
    • 0035979253 scopus 로고    scopus 로고
    • Regulation of myostatin activity and muscle growth
    • Lee, S. J., and McPherron, A. C. (2001). Regulation of myostatin activity and muscle growth. Proc. Natl. Acad. Sci. USA 98, 9306-9311.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 9306-9311
    • Lee, S.J.1    McPherron, A.C.2
  • 59
    • 0032188943 scopus 로고    scopus 로고
    • The interleukin-4 site-2 epitope determining binding of the common receptor γ chain
    • Letzelter, F., Wang, Y., and Sebald, W. (1998). The interleukin-4 site-2 epitope determining binding of the common receptor γ chain. Eur. J. Biochem. 257, 11-20.
    • (1998) Eur. J. Biochem. , vol.257 , pp. 11-20
    • Letzelter, F.1    Wang, Y.2    Sebald, W.3
  • 60
  • 61
    • 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., and Massague, J. (1995). Human type II receptor for bone morphogenic proteins (BMPs): extension of the two-kinase receptor model to the BMPs. Mol. Cell. Biol. 15, 3479-3486.
    • (1995) Mol. Cell Biol. , vol.15 , pp. 3479-3486
    • Liu, F.1    Ventura, F.2    Doody, J.3    Massague, J.4
  • 62
    • 0033548259 scopus 로고    scopus 로고
    • Crystallographic evidence for preformed dimers of erythropoietin receptor before ligand activation
    • Livnah, O., Stura, E. A., Middleton, S. A., Johnson, D. L., Jolliffe, L. K., and Wilson, I. A. (1999). Crystallographic evidence for preformed dimers of erythropoietin receptor before ligand activation. Science 283, 987-990.
    • (1999) Science , vol.283 , pp. 987-990
    • Livnah, O.1    Stura, E.A.2    Middleton, S.A.3    Johnson, D.L.4    Jolliffe, L.K.5    Wilson, I.A.6
  • 63
    • 0033257926 scopus 로고    scopus 로고
    • Ubiquitin-dependent degradation of TGF-β-activated smad2
    • Lo, R. S., and Massague, J. (1999). Ubiquitin-dependent degradation of TGF-β-activated smad2. Nat. Cell Biol. 1, 472-478.
    • (1999) Nat. Cell Biol. , vol.1 , pp. 472-478
    • Lo, R.S.1    Massague, J.2
  • 64
    • 0030972496 scopus 로고    scopus 로고
    • Positive and negative regulation of type II TGF-β receptor signal transduction by autophosphorylation on multiple serine residues
    • Luo, K., and Lodish, H. F. (1997). Positive and negative regulation of type II TGF-β receptor signal transduction by autophosphorylation on multiple serine residues. EMBO J. 16, 1970-1981.
    • (1997) EMBO J. , vol.16 , pp. 1970-1981
    • Luo, K.1    Lodish, H.F.2
  • 65
    • 0032475884 scopus 로고    scopus 로고
    • Specific activation of Smad1 signaling pathways by the BMP7 type I receptor, ALK2
    • Macias-Silva, M., Hoodless, P. A., Tang, S. J., Buchwald, M., and Wrana, J. L. (1998). Specific activation of Smad1 signaling pathways by the BMP7 type I receptor, ALK2. J. Biol. Chem. 273, 25628-25636.
    • (1998) J. Biol. Chem. , vol.273 , pp. 25628-25636
    • Macias-Silva, M.1    Hoodless, P.A.2    Tang, S.J.3    Buchwald, M.4    Wrana, J.L.5
  • 66
    • 0031685620 scopus 로고    scopus 로고
    • TGF-β signal transduction
    • Massague, J. (1998). TGF-β signal transduction. Annu. Rev. Biochem. 67, 753-791.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 753-791
    • Massague, J.1
  • 67
    • 0034654497 scopus 로고    scopus 로고
    • Controlling TGF-β signaling
    • Massague, J., and Chen, Y. G. (2000). Controlling TGF-β signaling. Genes Dev. 14, 627-644.
    • (2000) Genes Dev. , vol.14 , pp. 627-644
    • Massague, J.1    Chen, Y.G.2
  • 68
    • 0028179120 scopus 로고
    • The TGF-β family and its composite receptors
    • Massague, J., Attisano, L., and Wrana, J. L. (1994). The TGF-β family and its composite receptors. Trends Cell Biol. 4, 172-178.
    • (1994) Trends Cell Biol. , vol.4 , pp. 172-178
    • Massague, J.1    Attisano, L.2    Wrana, J.L.3
  • 69
    • 0034644472 scopus 로고    scopus 로고
    • TGF-β signaling in growth control, cancer, and heritable disorders
    • Massague, J., Blain, S. W., and Lo, R. S. (2000). TGF-β signaling in growth control, cancer, and heritable disorders. Cell 103, 295-309.
    • (2000) Cell , vol.103 , pp. 295-309
    • Massague, J.1    Blain, S.W.2    Lo, R.S.3
  • 70
    • 0027251256 scopus 로고
    • A structural superfamily of growth factors containing a cystine knot motif
    • McDonald, N. Q., and Hendrickson, W. A. (1993). A structural superfamily of growth factors containing a cystine knot motif. Cell 73, 421-424.
    • (1993) Cell , vol.73 , pp. 421-424
    • McDonald, N.Q.1    Hendrickson, W.A.2
  • 71
    • 0025986121 scopus 로고
    • New protein fold revealed by a 2.3-Å resolution crystal structure of nerve growth factor
    • McDonald, N. Q., Lapatto, R., Murray-Rust, J., Gunning, J., Wlodawer, A., and Blundell, T. L. (1991). New protein fold revealed by a 2.3-Å resolution crystal structure of nerve growth factor. Nature 354, 411-414.
    • (1991) Nature , vol.354 , pp. 411-414
    • McDonald, N.Q.1    Lapatto, R.2    Murray-Rust, J.3    Gunning, J.4    Wlodawer, A.5    Blundell, T.L.6
  • 72
    • 0029943464 scopus 로고    scopus 로고
    • The crystal structure of TGF-β 3 and comparison to TGF-β 2: Implications for receptor binding
    • Mittl, P. R., Priestle, J. P., Cox, D. A., McMaster, G., Cerletti, N., and Grutter, M. G. (1996). The crystal structure of TGF-β 3 and comparison to TGF-β 2: implications for receptor binding. Protein Sci. 5, 1261-1271.
    • (1996) Protein Sci. , vol.5 , pp. 1261-1271
    • Mittl, P.R.1    Priestle, J.P.2    Cox, D.A.3    McMaster, G.4    Cerletti, N.5    Grutter, M.G.6
  • 73
    • 0035032914 scopus 로고    scopus 로고
    • Divergence and convergence of TGF-β/BMP signaling
    • Miyazono, K., Kusanagi, K., and Inoue, H. (2001). Divergence and convergence of TGF-β/BMP signaling. J. Cell Physiol. 187, 265-276.
    • (2001) J. Cell Physiol. , vol.187 , pp. 265-276
    • Miyazono, K.1    Kusanagi, K.2    Inoue, H.3
  • 75
    • 0141519291 scopus 로고    scopus 로고
    • A general approach for identifying distant regulatory elements applied to the Gdf6 gene
    • Mortlock, D. P., Guenther, C., and Kingsley, D. M. (2003). A general approach for identifying distant regulatory elements applied to the Gdf6 gene. Genome Res. 13, 2069-2081.
    • (2003) Genome Res. , vol.13 , pp. 2069-2081
    • Mortlock, D.P.1    Guenther, C.2    Kingsley, D.M.3
  • 76
    • 0035694910 scopus 로고    scopus 로고
    • Smad regulation in TGF-β signal transduction
    • Moustakas, A., Souchelnytskyi, S., and Heldin, C. H. (2001). Smad regulation in TGF-β signal transduction. J. Cell Sci. 114, 4359-4369.
    • (2001) J. Cell Sci. , vol.114 , pp. 4359-4369
    • Moustakas, A.1    Souchelnytskyi, S.2    Heldin, C.H.3
  • 77
    • 0030795733 scopus 로고    scopus 로고
    • Vascular endothelial growth factor: Crystal structure and functional mapping of the kinase domain receptor binding site
    • Muller, Y. A., Li, B., Christinger, H. W., Wells, J. A., Cunningham, B. C., and de Vos, A. M. (1997). Vascular endothelial growth factor: crystal structure and functional mapping of the kinase domain receptor binding site. Proc. Natl. Acad. Sci. USA 94, 7192-7197.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 7192-7197
    • Muller, Y.A.1    Li, B.2    Christinger, H.W.3    Wells, J.A.4    Cunningham, B.C.5    de Vos, A.M.6
  • 78
    • 0033178337 scopus 로고    scopus 로고
    • p38 mitogen-activated protein kinase functionally contributes to chondrogenesis induced by growth/differentiation factor-5 in ATDC5 cells
    • Nakamura, K., Shirai, T., Morishita, S., Uchida, S., Saeki-Miura, K., and Makishima, F. (1999). p38 mitogen-activated protein kinase functionally contributes to chondrogenesis induced by growth/differentiation factor-5 in ATDC5 cells. Exp. Cell Res. 250, 351-363.
    • (1999) Exp. Cell Res. , vol.250 , pp. 351-363
    • Nakamura, K.1    Shirai, T.2    Morishita, S.3    Uchida, S.4    Saeki-Miura, K.5    Makishima, F.6
  • 79
    • 0032979875 scopus 로고    scopus 로고
    • Molecular evolution of a developmental pathway: Phylogenetic analyses of transforming growth factor-β family ligands, receptors and Smad signal transducers
    • Newfeld, S. J., Wisotzkey, R. G., and Kumar, S. (1999). Molecular evolution of a developmental pathway: phylogenetic analyses of transforming growth factor-β family ligands, receptors and Smad signal transducers. Genetics 152, 783-795.
    • (1999) Genetics , vol.152 , pp. 783-795
    • Newfeld, S.J.1    Wisotzkey, R.G.2    Kumar, S.3
  • 81
    • 0037085287 scopus 로고    scopus 로고
    • The mode of bone morphogenetic protein (BMP) receptor oligomerization determines different BMP-2 signaling pathways
    • Nohe, A., Hassel, S., Ehrlich, M., Neubauer, F., Sebald, W., Henis, Y. I., and Knaus, P. (2002). The mode of bone morphogenetic protein (BMP) receptor oligomerization determines different BMP-2 signaling pathways. J. Biol. Chem. 277, 5330-5338.
    • (2002) J. Biol. Chem. , vol.277 , pp. 5330-5338
    • Nohe, A.1    Hassel, S.2    Ehrlich, M.3    Neubauer, F.4    Sebald, W.5    Henis, Y.I.6    Knaus, P.7
  • 82
    • 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, D. H., and Rosenbaum, J. S. (1995). 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. 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
  • 84
    • 0037022121 scopus 로고    scopus 로고
    • Action range of BMP is defined by its N-terminal basic amino acid core
    • Ohkawara, B., Iemura, S., ten Dijke, P., and Ueno, N. (2002). Action range of BMP is defined by its N-terminal basic amino acid core. Curr. Biol. 12, 205-209.
    • (2002) Curr. Biol. , vol.12 , pp. 205-209
    • Ohkawara, B.1    Iemura, S.2    ten Dijke, P.3    Ueno, N.4
  • 86
    • 0030987103 scopus 로고    scopus 로고
    • Growth factors and diabetic retinopathy
    • Paques, M., Massin, P., and Gaudric, A. (1997). Growth factors and diabetic retinopathy. Diabetes Metab. 23, 125-130.
    • (1997) Diabetes Metab. , vol.23 , pp. 125-130
    • Paques, M.1    Massin, P.2    Gaudric, A.3
  • 87
    • 0033985464 scopus 로고    scopus 로고
    • TGF β-related pathways. Roles in Caenorhabditis elegans development
    • Patterson, G. I., and Padgett, R. W. (2000). TGF β-related pathways. Roles in Caenorhabditis elegans development. Trends Genet. 16, 27-33.
    • (2000) Trends Genet. , vol.16 , pp. 27-33
    • Patterson, G.I.1    Padgett, R.W.2
  • 88
    • 0032990886 scopus 로고    scopus 로고
    • Functional antagonism between activin and osteogenic protein-1 in human embryonal carcinoma cells
    • Piek, E., Afrakhte, M., Sampath, K., van Zoelen, E. J., Heldin, C. H., and ten Dijke, P. (1999). Functional antagonism between activin and osteogenic protein-1 in human embryonal carcinoma cells. J. Cell Physiol. 180, 141-149.
    • (1999) J. Cell Physiol. , vol.180 , pp. 141-149
    • Piek, E.1    Afrakhte, M.2    Sampath, K.3    van Zoelen, E.J.4    Heldin, C.H.5    ten Dijke, P.6
  • 89
    • 0141864365 scopus 로고    scopus 로고
    • Myostatin signals through a transforming growth factor β-like signaling pathway to block adipogenesis
    • Rebbapragada, A., Benchabane, H., Wrana, J. L., Celeste, A. J., and Attisano, L. (2003). Myostatin signals through a transforming growth factor β-like signaling pathway to block adipogenesis. Mol. Cell. Biol. 23, 7230-7242.
    • (2003) Mol. Cell Biol. , vol.23 , pp. 7230-7242
    • Rebbapragada, A.1    Benchabane, H.2    Wrana, J.L.3    Celeste, A.J.4    Attisano, L.5
  • 90
    • 0031909665 scopus 로고    scopus 로고
    • Role of morphogenetic proteins in skeletal tissue engineering and regeneration
    • Reddi, A. H. (1998). Role of morphogenetic proteins in skeletal tissue engineering and regeneration. Nat. Biotechnol. 16, 247-252.
    • (1998) Nat. Biotechnol. , vol.16 , pp. 247-252
    • Reddi, A.H.1
  • 91
    • 0026575663 scopus 로고
    • The BMP proteins in bone formation and repair
    • Rosen, V., and Thies, R. S. (1992). The BMP proteins in bone formation and repair. Trends Genet. 8, 97-102.
    • (1992) Trends Genet. , vol.8 , pp. 97-102
    • Rosen, V.1    Thies, R.S.2
  • 92
    • 0035254335 scopus 로고    scopus 로고
    • Type III TGF-β receptor-independent signalling of TGF-β2 via TβRII-B, an alternatively spliced TGF-β type II receptor
    • Rotzer, D., Roth, M., Lutz, M., Lindemann, D., Sebald, W., and Knaus, P. (2001). Type III TGF-β receptor-independent signalling of TGF-β2 via TβRII-B, an alternatively spliced TGF-β type II receptor. EMBO J. 20, 480-490.
    • (2001) EMBO J. , vol.20 , pp. 480-490
    • Rotzer, D.1    Roth, M.2    Lutz, M.3    Lindemann, D.4    Sebald, W.5    Knaus, P.6
  • 93
    • 0029985256 scopus 로고    scopus 로고
    • Human bone morphogenetic protein 2 contains a heparin-binding site which modifies its biological activity
    • Ruppert, R., Hoffmann, E., and Sebald, W. (1996). Human bone morphogenetic protein 2 contains a heparin-binding site which modifies its biological activity. Eur. J. Biochem. 237, 295-302.
    • (1996) Eur. J. Biochem. , vol.237 , pp. 295-302
    • Ruppert, R.1    Hoffmann, E.2    Sebald, W.3
  • 94
    • 0033582942 scopus 로고    scopus 로고
    • Crystal structure of human bone morphogenetic protein-2 at 2.7 Å resolution
    • Scheufler, C., Sebald, W., and Hulsmeyer, M. (1999). Crystal structure of human bone morphogenetic protein-2 at 2.7 Å resolution. J. Mol. Biol. 287, 103-115.
    • (1999) J. Mol. Biol. , vol.287 , pp. 103-115
    • Scheufler, C.1    Sebald, W.2    Hulsmeyer, M.3
  • 95
    • 0023686033 scopus 로고
    • Signal transduction by allosteric receptor oligomerization
    • Schlessinger, J. (1988). Signal transduction by allosteric receptor oligomerization. Trends Biochem. Sci. 13, 443-447.
    • (1988) Trends Biochem. Sci. , vol.13 , pp. 443-447
    • Schlessinger, J.1
  • 96
    • 0028825543 scopus 로고
    • Regulation of growth factor activation by proteoglycans: What is the role of the low affinity receptors?
    • Schlessinger, J., Lax, I., and Lemmon, M. (1995). Regulation of growth factor activation by proteoglycans: what is the role of the low affinity receptors? Cell 83, 357-360.
    • (1995) Cell , vol.83 , pp. 357-360
    • Schlessinger, J.1    Lax, I.2    Lemmon, M.3
  • 97
    • 0026633842 scopus 로고
    • An unusual feature revealed by the crystal structure at 2.2 Å resolution of human transforming growth factor-β 2
    • Schlunegger, M. P., and Grutter, M. G. (1992). An unusual feature revealed by the crystal structure at 2.2 Å resolution of human transforming growth factor-β 2. Nature 358, 430-434.
    • (1992) Nature , vol.358 , pp. 430-434
    • Schlunegger, M.P.1    Grutter, M.G.2
  • 98
    • 0642285636 scopus 로고    scopus 로고
    • The interaction of BMP-7 and ActRII implicates a new mode of receptor assembly
    • Sebald, W., and Mueller, T. D. (2003). The interaction of BMP-7 and ActRII implicates a new mode of receptor assembly. Trends Biochem. Sci. 28, 518-521.
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 518-521
    • Sebald, W.1    Mueller, T.D.2
  • 99
    • 0037330644 scopus 로고    scopus 로고
    • Multiple joint and skeletal patterning defects caused by single and double mutations in the mouse Gdf6 and Gdf5 genes
    • Settle, S. H., Jr., Rountree, R. B., Sinha, A., Thacker, A., Higgins, K., and Kingsley, D. M. (2003). Multiple joint and skeletal patterning defects caused by single and double mutations in the mouse Gdf6 and Gdf5 genes. Dev. Biol. 254, 116-130.
    • (2003) Dev. Biol. , vol.254 , pp. 116-130
    • Settle Jr., S.H.1    Rountree, R.B.2    Sinha, A.3    Thacker, A.4    Higgins, K.5    Kingsley, D.M.6
  • 100
    • 0038682002 scopus 로고    scopus 로고
    • Mechanisms of TGF-β signaling from cell membrane to the nucleus
    • Shi, Y., and Massague, J. (2003). Mechanisms of TGF-β signaling from cell membrane to the nucleus. Cell 113, 685-700.
    • (2003) Cell , vol.113 , pp. 685-700
    • Shi, Y.1    Massague, J.2
  • 101
    • 0032915460 scopus 로고    scopus 로고
    • Early embryonic lethality in Bmp5;Bmp7 double mutant mice suggests functional redundancy within the 60A subgroup
    • Solloway, M. J., and Robertson, E. J. (1999). Early embryonic lethality in Bmp5;Bmp7 double mutant mice suggests functional redundancy within the 60A subgroup. Development 126, 1753-1768.
    • (1999) Development , vol.126 , pp. 1753-1768
    • Solloway, M.J.1    Robertson, E.J.2
  • 102
    • 0036633294 scopus 로고    scopus 로고
    • TGF-β signaling from a three-dimensional perspective: Insight into selection of partners
    • Souchelnytskyi, S., Moustakas, A., and Heldin, C. H. (2002). TGF-β signaling from a three-dimensional perspective: insight into selection of partners. Trends Cell Biol. 12, 304-307.
    • (2002) Trends Cell Biol. , vol.12 , pp. 304-307
    • Souchelnytskyi, S.1    Moustakas, A.2    Heldin, C.H.3
  • 103
    • 0027328343 scopus 로고
    • The alphas, betas, and kinases of cytokine receptor complexes
    • Stahl, N., and Yancopoulos, G. D. (1993). The alphas, betas, and kinases of cytokine receptor complexes. Cell 74, 587-590.
    • (1993) Cell , vol.74 , pp. 587-590
    • Stahl, N.1    Yancopoulos, G.D.2
  • 105
    • 0030481707 scopus 로고    scopus 로고
    • Joint patterning defects caused by single and double mutations in members of the bone morphogenetic protein (BMP) family
    • Storm, E. E., and Kingsley, D. M. (1996). Joint patterning defects caused by single and double mutations in members of the bone morphogenetic protein (BMP) family. Development 122, 3969-3979.
    • (1996) Development , vol.122 , pp. 3969-3979
    • Storm, E.E.1    Kingsley, D.M.2
  • 108
    • 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., and Heldin, C. H. (1996). Signaling via hetero-oligomeric complexes of type I and type II serine/threonine kinase receptors. Curr. Opin. Cell Biol. 8, 139-145.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 139-145
    • ten Dijke, P.1    Miyazono, K.2    Heldin, C.H.3
  • 110
    • 0345269804 scopus 로고    scopus 로고
    • Structures of an ActRIIB: Activin A complex reveal a novel binding mode for TGF-β ligand: Receptor interactions
    • Thompson, T. B., Woodruff, T. K., and Jardetzky, T. S. (2003). Structures of an ActRIIB:activin A complex reveal a novel binding mode for TGF-β ligand:receptor interactions. EMBO J. 22, 1555-1566.
    • (2003) EMBO J. , vol.22 , pp. 1555-1566
    • Thompson, T.B.1    Woodruff, T.K.2    Jardetzky, T.S.3
  • 113
    • 0030030373 scopus 로고    scopus 로고
    • Complementation between kinase-defective and activation-defective TGF-β receptors reveals a novel form of receptor cooperativity essential for signaling
    • Weis Garcia, F., and Massague, J. (1996). Complementation between kinase-defective and activation-defective TGF-β receptors reveals a novel form of receptor cooperativity essential for signaling. EMBO J. 15, 276-289.
    • (1996) EMBO J. , vol.15 , pp. 276-289
    • Weis Garcia, F.1    Massague, J.2
  • 115
    • 0037424231 scopus 로고    scopus 로고
    • Inhibin is an antagonist of bone morphogenetic protein signaling
    • Wiater, E., and Vale, W. (2003). Inhibin is an antagonist of bone morphogenetic protein signaling. J. Biol. Chem. 278, 7934-7941.
    • (2003) J. Biol. Chem. , vol.278 , pp. 7934-7941
    • Wiater, E.1    Vale, W.2
  • 116
    • 0029022221 scopus 로고
    • GS domain mutations that constitutively activate T β R-I, the downstream signaling component in the TGF-β receptor complex
    • Wieser, R., Wrana, J. L., and Massague, J. (1995). GS domain mutations that constitutively activate T β R-I, the downstream signaling component in the TGF-β receptor complex. EMBO J. 14, 2199-2208.
    • (1995) EMBO J. , vol.14 , pp. 2199-2208
    • Wieser, R.1    Wrana, J.L.2    Massague, J.3
  • 118
    • 0029860206 scopus 로고    scopus 로고
    • A single tyrosine residue in the membrane-proximal domain of the granulocyte-macrophage colony-stimulating factor, interleukin (IL)-3, and IL-5 receptor common β-chain is necessary and sufficient for high affinity binding and signaling by all three ligands
    • Woodcock, J. M., Bagley, C. J., Zacharakis, B., and Lopez, A. F. (1996). A single tyrosine residue in the membrane-proximal domain of the granulocyte-macrophage colony-stimulating factor, interleukin (IL)-3, and IL-5 receptor common β-chain is necessary and sufficient for high affinity binding and signaling by all three ligands. J. Biol. Chem. 271, 25999-26006.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25999-26006
    • Woodcock, J.M.1    Bagley, C.J.2    Zacharakis, B.3    Lopez, A.F.4
  • 120
  • 122
    • 0037023363 scopus 로고    scopus 로고
    • Crystal structure of the extracellular segment of integrin αVβ3 in complex with an Arg-Gly-Asp ligand
    • Xiong, J. P., Stehle, T., Zhang, R., Joachimiak, A., Frech, M., Goodman, S. L., and Arnaout, M. A. (2002). Crystal structure of the extracellular segment of integrin αVβ3 in complex with an Arg-Gly-Asp ligand. Science 296, 151-155.
    • (2002) Science , vol.296 , pp. 151-155
    • Xiong, J.P.1    Stehle, T.2    Zhang, R.3    Joachimiak, A.4    Frech, M.5    Goodman, S.L.6    Arnaout, M.A.7
  • 124
    • 0033960316 scopus 로고    scopus 로고
    • The type I BMP receptor BMPRIB is required for chondrogenesis in the mouse limb
    • Yi, S. E., Daluiski, A., Pederson, R., Rosen, V., and Lyons, K. M. (2000). The type I BMP receptor BMPRIB is required for chondrogenesis in the mouse limb. Development 127, 621-630.
    • (2000) Development , vol.127 , pp. 621-630
    • Yi, S.E.1    Daluiski, A.2    Pederson, R.3    Rosen, V.4    Lyons, K.M.5
  • 126
    • 0037153157 scopus 로고    scopus 로고
    • The morphogenesis of feathers
    • Yu, M., Wu, P., Widelitz, R. B., and Chuong, C. M. (2002). The morphogenesis of feathers. Nature 420, 308-312.
    • (2002) Nature , vol.420 , pp. 308-312
    • Yu, M.1    Wu, P.2    Widelitz, R.B.3    Chuong, C.M.4
  • 127
    • 0033549789 scopus 로고    scopus 로고
    • A SMAD ubiquitin ligase targets the BMP pathway and affects embryonic pattern formation
    • Zhu, H., Kavsak, P., Abdollah, S., Wrana, J. L., and Thomsen, G. H. (1999). A SMAD ubiquitin ligase targets the BMP pathway and affects embryonic pattern formation. Nature 400, 687-693.
    • (1999) Nature , vol.400 , pp. 687-693
    • Zhu, H.1    Kavsak, P.2    Abdollah, S.3    Wrana, J.L.4    Thomsen, G.H.5
  • 128
    • 0030598829 scopus 로고    scopus 로고
    • The Spemann organizer signal noggin binds and inactivates bone morphogenetic protein 4
    • Zimmerman, L. B., De Jesus Escobar, J. M., and Harland, R. M. (1996). The Spemann organizer signal noggin binds and inactivates bone morphogenetic protein 4. Cell 86, 599-606.
    • (1996) Cell , vol.86 , pp. 599-606
    • Zimmerman, L.B.1    De Jesus Escobar, J.M.2    Harland, R.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.