메뉴 건너뛰기




Volumn 14, Issue 5, 2004, Pages 389-399

Overexpression of the tissue inhibitor of metalloproteinase-3 during Xenopus embryogenesis affects head and axial tissue formation

Author keywords

Neurulation; TIMP 3; Transgenesis; Xenopus

Indexed keywords

XENOPUS LAEVIS;

EID: 16644394106     PISSN: 10010602     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.cr.7290239     Document Type: Article
Times cited : (9)

References (53)
  • 1
    • 0031038238 scopus 로고    scopus 로고
    • Autosomal recessive Sorsby fundus dystrophy revisited: Molecular evidence for dominant inheritance
    • Felbor U, Suvanto EA, Forsius HR, Eriksson AW, Weber BH. Autosomal recessive Sorsby fundus dystrophy revisited: molecular evidence for dominant inheritance. Am. J. Hum. Genet. 1997; 60:57-62.
    • (1997) Am. J. Hum. Genet. , vol.60 , pp. 57-62
    • Felbor, U.1    Suvanto, E.A.2    Forsius, H.R.3    Eriksson, A.W.4    Weber, B.H.5
  • 2
    • 0031656460 scopus 로고    scopus 로고
    • Matrix metalloproteinases: Structures, evolution, and diversification
    • Massova I, Kotra LP, Fridman R, Mobashery S. Matrix metalloproteinases: structures, evolution, and diversification. FASEB J 1998; 12:1075-95.
    • (1998) FASEB J , vol.12 , pp. 1075-1095
    • Massova, I.1    Kotra, L.P.2    Fridman, R.3    Mobashery, S.4
  • 3
    • 0032574627 scopus 로고    scopus 로고
    • Cloning and developmental regulation of tissue inhibitor of metalloproteinase-3 (TIMP3) in Xenopus laevis early embryos
    • Yang M, Kurkinen M. Cloning and developmental regulation of tissue inhibitor of metalloproteinase-3 (TIMP3) in Xenopus laevis early embryos. Gene 1998; 211:95-100.
    • (1998) Gene , vol.211 , pp. 95-100
    • Yang, M.1    Kurkinen, M.2
  • 4
    • 0033618337 scopus 로고    scopus 로고
    • Matrix Metalloproteinases
    • Nagase H, Woessner JF. Matrix Metalloproteinases. J Biol Chem 1999; 274:21491-94.
    • (1999) J Biol Chem , vol.274 , pp. 21491-21494
    • Nagase, H.1    Woessner, J.F.2
  • 5
    • 0033597726 scopus 로고    scopus 로고
    • The stromal proteinase MMP3/stromelysin-1 promotes mammary carcinogenesis
    • Sternlicht MD, Lochter A, Sympson CJ, et al. The stromal proteinase MMP3/stromelysin-1 promotes mammary carcinogenesis. Cell 1999; 98:137-146.
    • (1999) Cell , vol.98 , pp. 137-146
    • Sternlicht, M.D.1    Lochter, A.2    Sympson, C.J.3
  • 6
    • 0030785485 scopus 로고    scopus 로고
    • Coordinate expression of matrix metalloproteinase family members in the uterus of normal, matrilysin-deficient, and stromely sin-1-deficient mice
    • Rudolph-Owen LA, Hulboy DL, Wilson CL, Mudgett J, Matrisian LM. Coordinate expression of matrix metalloproteinase family members in the uterus of normal, matrilysin-deficient, and stromely sin-1-deficient mice. Endocrinology 1997; 138:4902-11.
    • (1997) Endocrinology , vol.138 , pp. 4902-4911
    • Rudolph-Owen, L.A.1    Hulboy, D.L.2    Wilson, C.L.3    Mudgett, J.4    Matrisian, L.M.5
  • 7
    • 0033398801 scopus 로고    scopus 로고
    • Accelerated neointima formation after vascular injury in mice with stromelysin-3 (MMP-11) gene inactivation
    • Lijnen HR, Van Hoef B, Vanlinthout I, et al. Accelerated neointima formation after vascular injury in mice with stromelysin-3 (MMP-11) gene inactivation. Arterioscler Thromb Vasc Biol 1999; 19:2863-70.
    • (1999) Arterioscler Thromb Vasc Biol , vol.19 , pp. 2863-2870
    • Lijnen, H.R.1    Van Hoef, B.2    Vanlinthout, I.3
  • 8
    • 0035234269 scopus 로고    scopus 로고
    • Models for gain-of-function and loss-of-function of MMPs. Transgenic and gene targeted mice
    • Coussens LM, Shapiro SD, Soloway PD, Werb Z. Models for gain-of-function and loss-of-function of MMPs. Transgenic and gene targeted mice. Methods Mol Biol 2001; 151:149-79.
    • (2001) Methods Mol Biol , vol.151 , pp. 149-179
    • Coussens, L.M.1    Shapiro, S.D.2    Soloway, P.D.3    Werb, Z.4
  • 9
    • 0035035030 scopus 로고    scopus 로고
    • Overexpression of matrix metalloproteinases leads to lethality in transgenic Xenopus laevis: Implications for tissue-dependent functions of matrix metalloproteinases during late embryonic development
    • Damjanovski S, Amano T, Li Q, Pei DQ, Shi YB. Overexpression of matrix metalloproteinases leads to lethality in transgenic Xenopus laevis: Implications for tissue-dependent functions of matrix metalloproteinases during late embryonic development. Dev Dyn 2001; 221:37-47.
    • (2001) Dev Dyn , vol.221 , pp. 37-47
    • Damjanovski, S.1    Amano, T.2    Li, Q.3    Pei, D.Q.4    Shi, Y.B.5
  • 10
    • 0034697144 scopus 로고    scopus 로고
    • Binding of active (57 kD) membrane type 1-matrix metalloproteinase (MT1-MMP) to tissue inhibitor of metalloproteinase (TIMP)-2 regulates MT1-MMP processing and pro-MMP-2 activation
    • Hernandez-Barrantes S, Toth M, Bernardo MM, et al. Binding of active (57 kD) membrane type 1-matrix metalloproteinase (MT1-MMP) to tissue inhibitor of metalloproteinase (TIMP)-2 regulates MT1-MMP processing and pro-MMP-2 activation. J. Biol. Chem. 2000; 275:12080-9.
    • (2000) J. Biol. Chem. , vol.275 , pp. 12080-12089
    • Hernandez-Barrantes, S.1    Toth, M.2    Bernardo, M.M.3
  • 11
    • 0035188727 scopus 로고    scopus 로고
    • How matrix metalloproteinases regulate cell behaviour
    • Sternlicht MD, Werb Z. How matrix metalloproteinases regulate cell behaviour. Annu. Rev. Dev. Biol. 2000; 17:463-516.
    • (2000) Annu. Rev. Dev. Biol. , vol.17 , pp. 463-516
    • Sternlicht, M.D.1    Werb, Z.2
  • 12
    • 0034833362 scopus 로고    scopus 로고
    • Spontaneous air space enlargement in the lungs of mice lacking tissue inhibitor of metalloproteinases-3 (TIMP-3)
    • Leco KJ, Waterhouse P, Sanchez OH, et al. Spontaneous air space enlargement in the lungs of mice lacking tissue inhibitor of metalloproteinases-3 (TIMP-3). J Clin Invest 2001; 108: 817-29.
    • (2001) J Clin Invest , vol.108 , pp. 817-829
    • Leco, K.J.1    Waterhouse, P.2    Sanchez, O.H.3
  • 13
    • 0037230181 scopus 로고    scopus 로고
    • Deficiency of TIMP-1 exacerbates LV remodeling after myocardial infarction in mice
    • Creemers EE, Davis JN, Parkhurst AM, et al. Deficiency of TIMP-1 exacerbates LV remodeling after myocardial infarction in mice. Am J Physiol Heart Circ Physiol 2003; 284(1):H364-71.
    • (2003) Am J Physiol Heart Circ Physiol , vol.284 , Issue.1
    • Creemers, E.E.1    Davis, J.N.2    Parkhurst, A.M.3
  • 14
    • 0022339116 scopus 로고
    • Evidence for the role of fibronectin in amphibian gastrulation
    • Boucaut JC, Darribere T, Li SD, et al. Evidence for the role of fibronectin in amphibian gastrulation. J Embryol Exp Morphol 1985; 89:211-27.
    • (1985) J Embryol Exp Morphol , vol.89 , pp. 211-227
    • Boucaut, J.C.1    Darribere, T.2    Li, S.D.3
  • 15
    • 0345935809 scopus 로고
    • Collagenolytic activity in amphibian tissues: A tissue culture assay
    • USA
    • Gross J, Lapiere CM. Collagenolytic activity in amphibian tissues: a tissue culture assay. Proc Natl Acad Sci USA 1962; 48:1014-22.
    • (1962) Proc Natl Acad Sci , vol.48 , pp. 1014-1022
    • Gross, J.1    Lapiere, C.M.2
  • 16
    • 0033142510 scopus 로고    scopus 로고
    • Spatial and temporal expression of collagenases-3, -4, and stromelysin-3 implicates distinct functions in apoptosis and tissue remodeling during frog metamorphosis
    • Damjanovski S, Ishizuya-Oka A, Shi YB. Spatial and temporal expression of collagenases-3, -4, and stromelysin-3 implicates distinct functions in apoptosis and tissue remodeling during frog metamorphosis. Cell Res 1999; 9:91-110.
    • (1999) Cell Res , vol.9 , pp. 91-110
    • Damjanovski, S.1    Ishizuya-Oka, A.2    Shi, Y.B.3
  • 17
    • 0026794057 scopus 로고
    • A new inhibitor of metalloproteinases from chicken: ChIMP-3. A third member of the TIMP family
    • Pavloff N, Staskus PW, Kishnani MS, Hawkes SP. A new inhibitor of metalloproteinases from chicken: ChIMP-3. A third member of the TIMP family. J Biol Chem 1992; 267:17321-26.
    • (1992) J Biol Chem , vol.267 , pp. 17321-17326
    • Pavloff, N.1    Staskus, P.W.2    Kishnani, M.S.3    Hawkes, S.P.4
  • 18
    • 0028244447 scopus 로고
    • Tissue inhibitor of metalloproteinases-3 (TIMP-3) is an extracellular matrix-associated protein with a distinctive pattern of expression in mouse cells and tissues
    • Leco KJ, Khokha R, Pavloff N, Hawkes SP, Edwards DR. Tissue inhibitor of metalloproteinases-3 (TIMP-3) is an extracellular matrix-associated protein with a distinctive pattern of expression in mouse cells and tissues. J Biol Chem 1994; 269:9352-60.
    • (1994) J Biol Chem , vol.269 , pp. 9352-9360
    • Leco, K.J.1    Khokha, R.2    Pavloff, N.3    Hawkes, S.P.4    Edwards, D.R.5
  • 19
    • 0028304454 scopus 로고
    • A novel member of human tissue inhibitor of metalloproteinases (TIMP) gene family is regulated during G1 progression, mitogenic stimulation, differentiation, and senescence
    • Wick M, Burger C, Brusselbach S, Lucibello FC, Muller R. A novel member of human tissue inhibitor of metalloproteinases (TIMP) gene family is regulated during G1 progression, mitogenic stimulation, differentiation, and senescence. J Biol Chem 1994; 269:18953-60.
    • (1994) J Biol Chem , vol.269 , pp. 18953-18960
    • Wick, M.1    Burger, C.2    Brusselbach, S.3    Lucibello, F.C.4    Muller, R.5
  • 20
    • 0030470870 scopus 로고    scopus 로고
    • Regulation of tissue inhibitor of metalloproteinases-3 gene expression by transforming growth factor-b and dexamethasone in bovine and human articular chondrocytes
    • Su S, Dehnade F, Zafarullah M. Regulation of tissue inhibitor of metalloproteinases-3 gene expression by transforming growth factor-b and dexamethasone in bovine and human articular chondrocytes. DNA Cell Biol 1996; 15:1039-48.
    • (1996) DNA Cell Biol , vol.15 , pp. 1039-1048
    • Su, S.1    Dehnade, F.2    Zafarullah, M.3
  • 21
    • 0030019976 scopus 로고    scopus 로고
    • Cloning and expression of the cDNA encoding rat tissue inhibitor of metalloproteinase 3 (TIMP-3)
    • Wu I, Moses MA. Cloning and expression of the cDNA encoding rat tissue inhibitor of metalloproteinase 3 (TIMP-3). Gene 1996; 168:243-6.
    • (1996) Gene , vol.168 , pp. 243-246
    • Wu, I.1    Moses, M.A.2
  • 22
    • 0345465698 scopus 로고    scopus 로고
    • Invertebrate tissue inhibitor of metalloproteinase: Structure and nested gene organization within the synapsin locus is conserved from Drosophila to human
    • Pohar N, GodenschwegeTA, Buchner E. Invertebrate tissue inhibitor of metalloproteinase: structure and nested gene organization within the synapsin locus is conserved from Drosophila to human. Genomics 1999; 57:293-6.
    • (1999) Genomics , vol.57 , pp. 293-296
    • Pohar, N.1    Godenschwege, T.A.2    Buchner, E.3
  • 23
    • 0028355007 scopus 로고
    • Cloning of cDNAs encoding human TIMP-3, a novel member of the tissue inhibitor of metalloproteinase family
    • Silbiger SM, JacobsenVL, CupplesRL, Koski RA. Cloning of cDNAs encoding human TIMP-3, a novel member of the tissue inhibitor of metalloproteinase family. Gene 1994; 141: 293-297.
    • (1994) Gene , vol.141 , pp. 293-297
    • Silbiger, S.M.1    Jacobsen, V.L.2    Cupples, R.L.3    Koski, R.A.4
  • 24
    • 0034613296 scopus 로고    scopus 로고
    • TIMP-3 binds to sulphated glycosaminoglycans of the extracellular matrix
    • Yu W-H, Yu SC, Meng Q, Brew K, Woessner JF. TIMP-3 binds to sulphated glycosaminoglycans of the extracellular matrix. J Biol Chem 2000; 275:31226-32.
    • (2000) J Biol Chem , vol.275 , pp. 31226-31232
    • Yu, W.-H.1    Yu, S.C.2    Meng, Q.3    Brew, K.4    Woessner, J.F.5
  • 25
    • 0026267136 scopus 로고
    • Raising Xenopus in the laboratory
    • Wu M, Gerhart J. Raising Xenopus in the laboratory. Methods Cell Biol 1991; 36: 3-18.
    • (1991) Methods Cell Biol , vol.36 , pp. 3-18
    • Wu, M.1    Gerhart, J.2
  • 27
    • 0023916662 scopus 로고    scopus 로고
    • The entire mesodermal mantle behaves as Spemann's organizer in dorsoanterior enhanced Xenopus laevis embryos
    • Kao KR, Elinson RP. The entire mesodermal mantle behaves as Spemann's organizer in dorsoanterior enhanced Xenopus laevis embryos. Dev Biol 1998; 127:64-77.
    • (1998) Dev Biol , vol.127 , pp. 64-77
    • Kao, K.R.1    Elinson, R.P.2
  • 28
    • 0004136246 scopus 로고    scopus 로고
    • Cold Spring Harbor New York : Cold Spring Harbor Laboratory Press
    • rd ed., Cold Spring Harbor New York : Cold Spring Harbor Laboratory Press, 2000.
    • (2000) rd Ed.
    • Sambrook, J.1    Russell, D.W.2
  • 29
    • 0029806183 scopus 로고    scopus 로고
    • Transgenic Xenopus embryos from sperm nuclear transplantations reveal FGF signaling requirements during gastrulation
    • Kroll KL, Amaya E. Transgenic Xenopus embryos from sperm nuclear transplantations reveal FGF signaling requirements during gastrulation. Development 1996; 122:3173-83.
    • (1996) Development , vol.122 , pp. 3173-3183
    • Kroll, K.L.1    Amaya, E.2
  • 30
    • 0033514439 scopus 로고    scopus 로고
    • Metamorphosis is inhibited in transgenic Xenopus laevis tadpoles that overexpress type III deiodinase
    • USA
    • Huang H, Marsh-Armstrong N, Brown DD. Metamorphosis is inhibited in transgenic Xenopus laevis tadpoles that overexpress type III deiodinase. Proc Natl Acad Sci USA 1999; 96:962-7.
    • (1999) Proc Natl Acad Sci , vol.96 , pp. 962-967
    • Huang, H.1    Marsh-Armstrong, N.2    Brown, D.D.3
  • 31
    • 0026285616 scopus 로고
    • In situ hybridization: An improved whole mount method for Xenopus embryos
    • Harland RM. In situ hybridization: An improved whole mount method for Xenopus embryos. Meth Cell Biol 1991; 36:685-95.
    • (1991) Meth Cell Biol , vol.36 , pp. 685-695
    • Harland, R.M.1
  • 32
    • 0034044314 scopus 로고    scopus 로고
    • The PSIPRED protein structure prediction server
    • McGuffin LJ, Bryson K, Jones DT. The PSIPRED protein structure prediction server. Bioinformatics. 2000; 16:404-5.
    • (2000) Bioinformatics , vol.16 , pp. 404-405
    • McGuffin, L.J.1    Bryson, K.2    Jones, D.T.3
  • 33
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Higgins D, Thompson J, Gibson T, et al. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 1994; 22:4673-80.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Higgins, D.1    Thompson, J.2    Gibson, T.3
  • 34
    • 0035951618 scopus 로고    scopus 로고
    • Cloning and characterization of tissue inhibitor of metalloproteinase-3 (TIMP-3) from shark, Scyliorhinus torazame
    • Kim JT, Kim MS, Bae MK, et al. Cloning and characterization of tissue inhibitor of metalloproteinase-3 (TIMP-3) from shark, Scyliorhinus torazame. Biochim. Biophys. Acta 2001; 1517:311-5
    • (2001) Biochim. Biophys. Acta , vol.1517 , pp. 311-315
    • Kim, J.T.1    Kim, M.S.2    Bae, M.K.3
  • 35
    • 0027967380 scopus 로고
    • Xenopus chordin: A novel dorsalizing factor activated by organizer-specific homeobox genes
    • Sasai Y, Lu B, Steinbeisser H, et al. Xenopus chordin: a novel dorsalizing factor activated by organizer-specific homeobox genes. Cell 1994; 79:779-90
    • (1994) Cell , vol.79 , pp. 779-790
    • Sasai, Y.1    Lu, B.2    Steinbeisser, H.3
  • 36
    • 0035212947 scopus 로고    scopus 로고
    • Conserved cellular and molecular mechanisms in development
    • Giudice G. Conserved cellular and molecular mechanisms in development. Cell Biol Int 2001; 25:1081-90.
    • (2001) Cell Biol Int , vol.25 , pp. 1081-1090
    • Giudice, G.1
  • 37
    • 0014568424 scopus 로고
    • The formation of somites in Xenopus
    • Hamilton L. The formation of somites in Xenopus. J Embryol Exp Morphol 1969; 2:253-64.
    • (1969) J Embryol Exp Morphol , vol.2 , pp. 253-264
    • Hamilton, L.1
  • 38
    • 0030601956 scopus 로고    scopus 로고
    • Activation of Siamois by the Wnt pathway
    • Brannon M, Kimelman D. Activation of Siamois by the Wnt pathway. Dev Biol 1996; 180:344-7.
    • (1996) Dev Biol , vol.180 , pp. 344-347
    • Brannon, M.1    Kimelman, D.2
  • 39
    • 0034011848 scopus 로고    scopus 로고
    • Differential regulation of three thyroid hormone-responsive matrix metalloproteinase genes implicates distinct functions during frog embryogenesis
    • Damjanovski S, Puzianowska-Kuznicka M, Ishuzuya-Oka A, Shi YB. Differential regulation of three thyroid hormone-responsive matrix metalloproteinase genes implicates distinct functions during frog embryogenesis. FASEB J 2000; 3:503-10.
    • (2000) FASEB J , vol.3 , pp. 503-510
    • Damjanovski, S.1    Puzianowska-Kuznicka, M.2    Ishuzuya-Oka, A.3    Shi, Y.B.4
  • 40
    • 0026695885 scopus 로고
    • Distribution of type II collagen mRNA in Xenopus embryos visualized by whole-mount in situ hybridization
    • Bieker JJ, Yazdani-Buicky M. Distribution of type II collagen mRNA in Xenopus embryos visualized by whole-mount in situ hybridization. J Histochem Cytochem 1992; 40: 1117-20.
    • (1992) J Histochem Cytochem , vol.40 , pp. 1117-1120
    • Bieker, J.J.1    Yazdani-Buicky, M.2
  • 41
    • 0024831470 scopus 로고
    • Embryonic lens induction: More than meets the optic vesicle
    • Saha MS, Spann CL, Grainger RM. Embryonic lens induction: more than meets the optic vesicle. Cell Differ Dev 1989; 28:153-71.
    • (1989) Cell Differ Dev , vol.28 , pp. 153-171
    • Saha, M.S.1    Spann, C.L.2    Grainger, R.M.3
  • 42
    • 0026800666 scopus 로고
    • Embryonic lens induction: Shedding light on vertebrate tissue determination
    • Grainger RM. Embryonic lens induction: Shedding light on vertebrate tissue determination. Trends Genet 1992; 8:349-55.
    • (1992) Trends Genet , vol.8 , pp. 349-355
    • Grainger, R.M.1
  • 43
    • 0034063698 scopus 로고    scopus 로고
    • An assay system to study migratory behavior of cranial neural crest cells in Xenopus
    • Borchers A, Epperlein HH, Wedlich D. An assay system to study migratory behavior of cranial neural crest cells in Xenopus. Dev Genes Evol 2000; 210:217-22.
    • (2000) Dev Genes Evol , vol.210 , pp. 217-222
    • Borchers, A.1    Epperlein, H.H.2    Wedlich, D.3
  • 44
    • 0026310868 scopus 로고
    • Analysis of gene function in developing Xenopus embryos
    • Vize PD, Melton DA. Analysis of gene function in developing Xenopus embryos. Meth Cell Biol 1991; 36:367-87.
    • (1991) Meth Cell Biol , vol.36 , pp. 367-387
    • Vize, P.D.1    Melton, D.A.2
  • 46
    • 0023139629 scopus 로고
    • Neural cell adhesion molecule expression in Xenopus embryos
    • Balak K, Jacobson M, Sunshine J, Rutishauser U. Neural cell adhesion molecule expression in Xenopus embryos. Dev Biol 1987; 119:540-50.
    • (1987) Dev Biol , vol.119 , pp. 540-550
    • Balak, K.1    Jacobson, M.2    Sunshine, J.3    Rutishauser, U.4
  • 47
    • 0029851533 scopus 로고    scopus 로고
    • Xenopus cadherins: Sorting out types and functions in embryogenesis
    • Kuhl M, Wedlich D. Xenopus cadherins: Sorting out types and functions in embryogenesis. Dev Dyn 1996; 207:121-34.
    • (1996) Dev Dyn , vol.207 , pp. 121-134
    • Kuhl, M.1    Wedlich, D.2
  • 48
    • 0025275826 scopus 로고
    • The effects of N-cadherin misexpression on morphogenesis in Xenopus embryos
    • Detrick RJ, Dickey D, Kintner CR. The effects of N-cadherin misexpression on morphogenesis in Xenopus embryos. Neuron 1990; 4:493-506.
    • (1990) Neuron , vol.4 , pp. 493-506
    • Detrick, R.J.1    Dickey, D.2    Kintner, C.R.3
  • 49
    • 0025074177 scopus 로고
    • Ectopic expression of N-cadherin perturbs histogenesis in Xenopus embryos
    • Fujimori T, Miyatani S, Takeichi M. Ectopic expression of N-cadherin perturbs histogenesis in Xenopus embryos. Development 1990; 110:97-104.
    • (1990) Development , vol.110 , pp. 97-104
    • Fujimori, T.1    Miyatani, S.2    Takeichi, M.3
  • 51
    • 0000035142 scopus 로고
    • Recent advances in defining the role of the extracellular matrix in neural crest development
    • Penis R, Bronner-Fraser M. Recent advances in defining the role of the extracellular matrix in neural crest development. Commun Dev Neurobiol 1989; 1:61-83.
    • (1989) Commun Dev Neurobiol , vol.1 , pp. 61-83
    • Penis, R.1    Bronner-Fraser, M.2
  • 52
    • 0036922915 scopus 로고    scopus 로고
    • Neural tube closure requires Dishevelled-dependent convergent extension of the midline
    • Wallingford JB, Harland RM. Neural tube closure requires Dishevelled-dependent convergent extension of the midline. Development 2002; 129: 5815-25.
    • (2002) Development , vol.129 , pp. 5815-5825
    • Wallingford, J.B.1    Harland, R.M.2
  • 53
    • 0032521142 scopus 로고
    • Divergent effects of tissue inhibitor of metalloproteinase-1,-2, or-3 overexpression on rat vascular smooth muscle cell invasion, proliferation, and death in vitro. TIMP3 promotes apoptosis
    • Baker AH, Zaltsman AB, George SJ, Newby AC. Divergent effects of tissue inhibitor of metalloproteinase-1,-2, or-3 overexpression on rat vascular smooth muscle cell invasion, proliferation, and death in vitro. TIMP3 promotes apoptosis. J. Clin. Invest. 1988; 101:1478-87.
    • (1988) J. Clin. Invest. , vol.101 , pp. 1478-1487
    • Baker, A.H.1    Zaltsman, A.B.2    George, S.J.3    Newby, A.C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.