메뉴 건너뛰기




Volumn 33, Issue 12, 2013, Pages 2388-2401

LoXL4 is induced by transforming growth factor β1 through Smad and JunB/Fra2 and contributes to vascular matrix remodeling

Author keywords

[No Author keywords available]

Indexed keywords

LYSYL OXIDASE LIKE 4; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE 1; PROTEIN LYSINE 6 OXIDASE; SMAD2 PROTEIN; SMAD3 PROTEIN; TRANSCRIPTION FACTOR AP 1; TRANSCRIPTION FACTOR FRA 2; TRANSCRIPTION FACTOR JUNB; TRANSCRIPTION FACTOR SP1; TRANSFORMING GROWTH FACTOR BETA1; UNCLASSIFIED DRUG;

EID: 84878981312     PISSN: 02707306     EISSN: 10985549     Source Type: Journal    
DOI: 10.1128/MCB.00036-13     Document Type: Article
Times cited : (80)

References (72)
  • 1
    • 61749097816 scopus 로고    scopus 로고
    • Tgf-beta superfamily signaling in embryonic development and homeostasis
    • Wu MY, Hill CS. 2009. Tgf-beta superfamily signaling in embryonic development and homeostasis. Dev. Cell 16:329-343.
    • (2009) Dev. Cell , vol.16 , pp. 329-343
    • Wu, M.Y.1    Hill, C.S.2
  • 2
    • 0037204990 scopus 로고    scopus 로고
    • Signal transduction by the TGF-beta superfamily
    • Attisano L, Wrana JL. 2002. Signal transduction by the TGF-beta superfamily. Science 296:1646-1647.
    • (2002) Science , vol.296 , pp. 1646-1647
    • Attisano, L.1    Wrana, J.L.2
  • 3
    • 2142646426 scopus 로고    scopus 로고
    • TGF-beta signaling and the fibrotic response
    • Leask A, Abraham DJ. 2004. TGF-beta signaling and the fibrotic response. FASEB J. 18:816-827.
    • (2004) FASEB J. , vol.18 , pp. 816-827
    • Leask, A.1    Abraham, D.J.2
  • 6
    • 0024550419 scopus 로고
    • The fibrillar nature and structure of isoproterenol-induced myocardial fibrosis in the rat
    • Pick R, Jalil JE, Janicki JS, Weber KT. 1989. The fibrillar nature and structure of isoproterenol-induced myocardial fibrosis in the rat. Am. J. Pathol. 134:365-371.
    • (1989) Am. J. Pathol. , vol.134 , pp. 365-371
    • Pick, R.1    Jalil, J.E.2    Janicki, J.S.3    Weber, K.T.4
  • 8
    • 80052942225 scopus 로고    scopus 로고
    • Collagens, suprastructures, and collagen fibril assembly
    • Springer-Verlag, Berlin, Germany
    • Birk DE, Bruckner P. 2011. Collagens, suprastructures, and collagen fibril assembly, p 1-39. In Mecham RP (ed), The extracellular matrix: an overview. Springer-Verlag, Berlin, Germany.
    • (2011) Mecham RP (ed), The extracellular matrix: an overview , pp. 1-39
    • Birk, D.E.1    Bruckner, P.2
  • 9
    • 67149096234 scopus 로고    scopus 로고
    • Lysyl oxidases in mammalian development and certain pathological conditions
    • Maki JM. 2009. Lysyl oxidases in mammalian development and certain pathological conditions. Histol. Histopathol. 24:651- 660.
    • (2009) Histol. Histopathol. , vol.24
    • Maki, J.M.1
  • 11
    • 0037027504 scopus 로고    scopus 로고
    • Inactivation of the lysyl oxidase gene Lox leads to aortic aneurysms, cardiovascular dysfunction, and perinatal death in mice
    • Maki JM, Rasanen J, Tikkanen H, Sormunen R, Makikallio K, Kivirikko KI, Soininen R. 2002. Inactivation of the lysyl oxidase gene Lox leads to aortic aneurysms, cardiovascular dysfunction, and perinatal death in mice. Circulation 106:2503-2509.
    • (2002) Circulation , vol.106 , pp. 2503-2509
    • Maki, J.M.1    Rasanen, J.2    Tikkanen, H.3    Sormunen, R.4    Makikallio, K.5    Kivirikko, K.I.6    Soininen, R.7
  • 12
    • 0038801663 scopus 로고    scopus 로고
    • Functional cooperation between Smad proteins and activator protein-1 regulates transforming growth factor-beta-mediated induction of endothelin-1 expression
    • Rodriguez-Pascual F, Redondo-Horcajo M, Lamas S. 2003. Functional cooperation between Smad proteins and activator protein-1 regulates transforming growth factor-beta-mediated induction of endothelin-1 expression. Circ. Res. 92:1288-1295.
    • (2003) Circ. Res. , vol.92 , pp. 1288-1295
    • Rodriguez-Pascual, F.1    Redondo-Horcajo, M.2    Lamas, S.3
  • 15
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski P, Sacchi N. 1987. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162:156-159.
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 16
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) method
    • Livak KJ, Schmittgen TD. 2001. Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) method. Methods 25:402- 408.
    • (2001) Methods , vol.25
    • Livak, K.J.1    Schmittgen, T.D.2
  • 20
    • 0024380087 scopus 로고
    • Rapid detection of octamer binding proteins with 'mini-extracts', prepared from a small number of cells
    • Schreiber E, Matthias P, Muller MM, Schaffner W. 1989. Rapid detection of octamer binding proteins with 'mini-extracts', prepared from a small number of cells. Nucleic Acids Res. 17:6419.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 6419
    • Schreiber, E.1    Matthias, P.2    Muller, M.M.3    Schaffner, W.4
  • 21
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels
    • Shevchenko A, Wilm M, Vorm O, Mann M. 1996. Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels. Anal. Chem. 68:850-858.
    • (1996) Anal. Chem. , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 23
    • 77956959151 scopus 로고    scopus 로고
    • Imaging cells in three-dimensional collagen matrix
    • Unit 1018.1- 10.18.20.
    • Artym VV, Matsumoto K. 2010. Imaging cells in three-dimensional collagen matrix. Curr. Protoc. Cell Biol. Chapter 10:Unit 10.18.1- 10.18.20.
    • (2010) Curr. Protoc. Cell Biol. Chapter , vol.10
    • Artym, V.V.1    Matsumoto, K.2
  • 24
    • 0037081128 scopus 로고    scopus 로고
    • A fluorometric assay for detection of lysyl oxidase enzyme activity in biological samples
    • Palamakumbura AH, Trackman PC. 2002. A fluorometric assay for detection of lysyl oxidase enzyme activity in biological samples. Anal. Biochem. 300:245-251.
    • (2002) Anal. Biochem. , vol.300 , pp. 245-251
    • Palamakumbura, A.H.1    Trackman, P.C.2
  • 25
    • 58149197042 scopus 로고    scopus 로고
    • Functional analysis of the 5= flanking domain of the LOXL4 gene in head and neck squamous cell carcinoma cells
    • Gorogh T, Holtmeier C, Weise JB, Hoffmann M, Ambrosch P, Laudien M, Csiszar K. 2008. Functional analysis of the 5= flanking domain of the LOXL4 gene in head and neck squamous cell carcinoma cells. Int. J. Oncol. 33:1091-1098.
    • (2008) Int. J. Oncol. , vol.33 , pp. 1091-1098
    • Gorogh, T.1    Holtmeier, C.2    Weise, J.B.3    Hoffmann, M.4    Ambrosch, P.5    Laudien, M.6    Csiszar, K.7
  • 28
    • 0030047646 scopus 로고    scopus 로고
    • An AP-1 binding sequence is essential for regulation of the human 2(I) collagen (COL1A2) promoter activity by transforming growth factor
    • Chung K-Y, Agarwal A, Uitto J, Mauviel A. 1996. An AP-1 binding sequence is essential for regulation of the human 2(I) collagen (COL1A2) promoter activity by transforming growth factor. J. Biol. Chem. 271:3272- 3278.
    • (1996) J. Biol. Chem. , vol.271
    • Chung, K.-Y.1    Agarwal, A.2    Uitto, J.3    Mauviel, A.4
  • 29
    • 0027960055 scopus 로고
    • Sp1 sites in the mouse aprt gene promoter are required to prevent methylation of the CpG island
    • Macleod D, Charlton J, Mullins J, Bird AP. 1994. Sp1 sites in the mouse aprt gene promoter are required to prevent methylation of the CpG island. Genes Dev. 8:2282-2292.
    • (1994) Genes Dev. , vol.8 , pp. 2282-2292
    • Macleod, D.1    Charlton, J.2    Mullins, J.3    Bird, A.P.4
  • 30
    • 0142104985 scopus 로고    scopus 로고
    • Smad-dependent and Smad-independent pathways in TGF-beta family signalling
    • Derynck R, Zhang YE. 2003. Smad-dependent and Smad-independent pathways in TGF-beta family signalling. Nature 425:577-584.
    • (2003) Nature , vol.425 , pp. 577-584
    • Derynck, R.1    Zhang, Y.E.2
  • 31
    • 34047264014 scopus 로고    scopus 로고
    • Dominant-negative activator protein 1 (TAM67) targets cyclooxygenase-2 and osteopontin under conditions in which it specifically inhibits tumorigenesis
    • Matthews CP, Birkholz AM, Baker AR, Perella CM, Beck GR Jr, Young MR, Colburn NH. 2007. Dominant-negative activator protein 1 (TAM67) targets cyclooxygenase-2 and osteopontin under conditions in which it specifically inhibits tumorigenesis. Cancer Res. 67:2430-2438.
    • (2007) Cancer Res. , vol.67 , pp. 2430-2438
    • Matthews, C.P.1    Birkholz, A.M.2    Baker, A.R.3    Perella, C.M.4    Beck Jr., G.R.5    Young, M.R.6    Colburn, N.H.7
  • 32
    • 70450187617 scopus 로고    scopus 로고
    • The regulation of TGFbeta signal transduction
    • Moustakas A, Heldin CH. 2009. The regulation of TGFbeta signal transduction. Development 136:3699-3714.
    • (2009) Development , vol.136 , pp. 3699-3714
    • Moustakas, A.1    Heldin, C..H.2
  • 34
    • 73449115656 scopus 로고    scopus 로고
    • Transcription factor fos-related antigen-2 induces progressive peripheral vasculopathy in mice closely resembling human systemic sclerosis
    • Maurer B, Busch N, Jungel A, Pileckyte M, Gay RE, Michel BA, Schett G, Gay S, Distler J, Distler O. 2009. Transcription factor fos-related antigen-2 induces progressive peripheral vasculopathy in mice closely resembling human systemic sclerosis. Circulation 120:2367-2376.
    • (2009) Circulation , vol.120 , pp. 2367-2376
    • Maurer, B.1    Busch, N.2    Jungel, A.3    Pileckyte, M.4    Gay, R.E.5    Michel, B.A.6    Schett, G.7    Gay, S.8    Distler, J.9    Distler, O.10
  • 37
    • 0026571898 scopus 로고
    • Mechanism of specificity in the Fos-Jun oncoprotein heterodimer
    • O'Shea EK, Rutkowski R, Kim PS. 1992. Mechanism of specificity in the Fos-Jun oncoprotein heterodimer. Cell 68:699-708.
    • (1992) Cell , vol.68 , pp. 699-708
    • O'Shea, E.K.1    Rutkowski, R.2    Kim, P.S.3
  • 38
    • 0031009072 scopus 로고    scopus 로고
    • Phosphorylation and high level expression of Fra-2 in v-src transformed cells: a pathway of activation of endogenous AP-1
    • Murakami M, Sonobe MH, Ui M, Kabuyama Y, Watanabe H, Wada T, Handa H, Iba H. 1997. Phosphorylation and high level expression of Fra-2 in v-src transformed cells: a pathway of activation of endogenous AP-1. Oncogene 14:2435-2444.
    • (1997) Oncogene , vol.14 , pp. 2435-2444
    • Murakami, M.1    Sonobe, M.H.2    Ui, M.3    Kabuyama, Y.4    Watanabe, H.5    Wada, T.6    Handa, H.7    Iba, H.8
  • 39
    • 0032975216 scopus 로고    scopus 로고
    • Fra-2-positive autoregulatory loop triggered by mitogen-activated protein kinase (MAPK) and Fra-2 phosphorylation sites by MAPK
    • Murakami M, Ui M, Iba H. 1999. Fra-2-positive autoregulatory loop triggered by mitogen-activated protein kinase (MAPK) and Fra-2 phosphorylation sites by MAPK. Cell Growth Differ. 10:333-342.
    • (1999) Cell Growth Differ. , vol.10 , pp. 333-342
    • Murakami, M.1    Ui, M.2    Iba, H.3
  • 40
    • 84860011592 scopus 로고    scopus 로고
    • Dephosphorylation of cardiac proteins in vitro-a matter of phosphatase specificity
    • Husberg C, Agnetti G, Holewinski RJ, Christensen G, Van Eyk JE. 2012. Dephosphorylation of cardiac proteins in vitro-a matter of phosphatase specificity. Proteomics 12:973-978.
    • (2012) Proteomics , vol.12 , pp. 973-978
    • Husberg, C.1    Agnetti, G.2    Holewinski, R.J.3    Christensen, G.4    Van Eyk, J.E.5
  • 42
    • 0034749471 scopus 로고    scopus 로고
    • A novel human lysyl oxidase-like gene (LOXL4) on chromosome 10q24 has an altered scavenger receptor cysteine rich domain
    • Asuncion L, Fogelgren B, Fong KS, Fong SF, Kim Y, Csiszar K. 2001. A novel human lysyl oxidase-like gene (LOXL4) on chromosome 10q24 has an altered scavenger receptor cysteine rich domain. Matrix Biol. 20:487-491.
    • (2001) Matrix Biol. , vol.20 , pp. 487-491
    • Asuncion, L.1    Fogelgren, B.2    Fong, K.S.3    Fong, S.F.4    Kim, Y.5    Csiszar, K.6
  • 43
    • 0035968314 scopus 로고    scopus 로고
    • Molecular cloning and biological activity of a novel lysyl oxidase- related gene expressed in cartilage
    • Ito H, Akiyama H, Iguchi H, Iyama K, Miyamoto M, Ohsawa K, Nakamura T. 2001. Molecular cloning and biological activity of a novel lysyl oxidase- related gene expressed in cartilage. J. Biol. Chem. 276:24023-24029.
    • (2001) J. Biol. Chem. , vol.276 , pp. 24023-24029
    • Ito, H.1    Akiyama, H.2    Iguchi, H.3    Iyama, K.4    Miyamoto, M.5    Ohsawa, K.6    Nakamura, T.7
  • 44
    • 0034751557 scopus 로고    scopus 로고
    • Cloning and characterization of a fifth human lysyl oxidase isoenzyme: the third member of the lysyl oxidase-related subfamily with four scavenger receptor cysteine-rich domains
    • Maki JM, Tikkanen H, Kivirikko KI. 2001. Cloning and characterization of a fifth human lysyl oxidase isoenzyme: the third member of the lysyl oxidase-related subfamily with four scavenger receptor cysteine-rich domains. Matrix Biol. 20:493- 496.
    • (2001) Matrix Biol. , vol.20 , pp. 493-496
    • Maki, J.M.1    Tikkanen, H.2    Kivirikko, K.I.3
  • 45
    • 84864350704 scopus 로고    scopus 로고
    • The rationale for targeting the LOX family in cancer
    • Barker HE, Cox TR, Erler JT. 2012. The rationale for targeting the LOX family in cancer. Nat. Rev. Cancer 12:540-552.
    • (2012) Nat. Rev. Cancer , vol.12 , pp. 540-552
    • Barker, H.E.1    Cox, T.R.2    Erler, J.T.3
  • 47
    • 0030933804 scopus 로고    scopus 로고
    • Transcriptional and post-transcriptional control of lysyl oxidase expression in vascular smooth muscle cells: effects of TGF-Î21 and serum deprivation
    • Gacheru SN, Thomas KM, Murray SA, Csiszar K, Smith-Mungo LI, Kagan HM. 1997. Transcriptional and post-transcriptional control of lysyl oxidase expression in vascular smooth muscle cells: effects of TGF-Î21 and serum deprivation. J. Cell. Biochem. 65:395-407.
    • (1997) J. Cell. Biochem. , vol.65 , pp. 395-407
    • Gacheru, S.N.1    Thomas, K.M.2    Murray, S.A.3    Csiszar, K.4    Smith-Mungo, L.I.5    Kagan, H.M.6
  • 49
    • 80052616166 scopus 로고    scopus 로고
    • Transforming growth factor-beta induces extracellular matrix protein cross-linking lysyl oxidase (LOX) genes in human trabecular meshwork cells
    • Sethi A, Mao W, Wordinger RJ, Clark AF. 2011. Transforming growth factor-beta induces extracellular matrix protein cross-linking lysyl oxidase (LOX) genes in human trabecular meshwork cells. Invest. Ophthalmol. Vis. Sci. 52:5240-5250.
    • (2011) Invest. Ophthalmol. Vis. Sci. , vol.52 , pp. 5240-5250
    • Sethi, A.1    Mao, W.2    Wordinger, R.J.3    Clark, A.F.4
  • 50
    • 54349112351 scopus 로고    scopus 로고
    • Activator protein-1 and Smad proteins synergistically regulate human follicle-stimulating hormone Î2-promoter activity
    • Wang Y, Fortin JRM, Lamba P, Bonomi M, Persani L, Roberson MS, Bernard DJ. 2008. Activator protein-1 and Smad proteins synergistically regulate human follicle-stimulating hormone Î2-promoter activity. Endocrinology 149:5577-5591.
    • (2008) Endocrinology , vol.149 , pp. 5577-5591
    • Wang, Y.1    Fortin, JRM.2    Lamba, P.3    Bonomi, M.4    Persani, L.5    Roberson, M.S.6    Bernard, D.J.7
  • 51
    • 51649101150 scopus 로고    scopus 로고
    • Transforming growth factor-beta-mediated tumor necrosis factor-related apoptosis-inducing ligand expression and apoptosis in hepatoma cells requires functional cooperation between Smad proteins and activator protein-1
    • Herzer K, Grosse-Wilde A, Krammer PH, Galle PR, Kanzler S. 2008. Transforming growth factor-beta-mediated tumor necrosis factor-related apoptosis-inducing ligand expression and apoptosis in hepatoma cells requires functional cooperation between Smad proteins and activator protein-1. Mol. Cancer Res. 6:1169-1177.
    • (2008) Mol. Cancer Res. , vol.6 , pp. 1169-1177
    • Herzer, K.1    Grosse-Wilde, A.2    Krammer, P.H.3    Galle, P.R.4    Kanzler, S.5
  • 52
    • 58149468095 scopus 로고    scopus 로고
    • Chromatin immunoprecipitation on microarray analysis of Smad2/3 binding sites reveals roles of ETS1 and TFAP2A in transforming growth factor beta signaling
    • Koinuma D, Tsutsumi S, Kamimura N, Taniguchi H, Miyazawa K, Sunamura M, Imamura T, Miyazono K, Aburatani H. 2009. Chromatin immunoprecipitation on microarray analysis of Smad2/3 binding sites reveals roles of ETS1 and TFAP2A in transforming growth factor beta signaling. Mol. Cell. Biol. 29:172-186.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 172-186
    • Koinuma, D.1    Tsutsumi, S.2    Kamimura, N.3    Taniguchi, H.4    Miyazawa, K.5    Sunamura, M.6    Imamura, T.7    Miyazono, K.8    Aburatani, H.9
  • 53
    • 0035986888 scopus 로고    scopus 로고
    • Evolution of transcription factor binding sites in mammalian gene regulatory regions: conservation and turnover
    • Dermitzakis ET, Clark AG. 2002. Evolution of transcription factor binding sites in mammalian gene regulatory regions: conservation and turnover. Mol. Biol. Evol. 19:1114-1121.
    • (2002) Mol. Biol. Evol. , vol.19 , pp. 1114-1121
    • Dermitzakis, E.T.1    Clark, A.G.2
  • 56
  • 57
    • 84859986242 scopus 로고    scopus 로고
    • JunB contributes to Id2 repression and the epithelialto-mesenchymal transition in response to transforming growth factorbeta
    • Gervasi M, Bianchi-Smiraglia A, Cummings M, Zheng Q, Wang D, Liu S, Bakin AV. 2012. JunB contributes to Id2 repression and the epithelialto-mesenchymal transition in response to transforming growth factorbeta. J. Cell Biol. 196:589-603.
    • (2012) J. Cell Biol. , vol.196 , pp. 589-603
    • Gervasi, M.1    Bianchi-Smiraglia, A.2    Cummings, M.3    Zheng, Q.4    Wang, D.5    Liu, S.6    Bakin, A.V.7
  • 59
    • 80052851503 scopus 로고    scopus 로고
    • Role of endothelialmesenchymal transition (EndoMT) in the pathogenesis of fibrotic disorders
    • Piera-Velazquez S, Li Z, Jimenez SA. 2011. Role of endothelialmesenchymal transition (EndoMT) in the pathogenesis of fibrotic disorders. Am. J. Pathol. 179:1074-1080.
    • (2011) Am. J. Pathol. , vol.179 , pp. 1074-1080
    • Piera-Velazquez, S.1    Li, Z.2    Jimenez, S.A.3
  • 60
    • 0026453307 scopus 로고
    • Transforming growth factor beta 1 promotes the differentiation of endothelial cells into smooth muscle-like cells in vitro
    • Arciniegas E, Sutton AB, Allen TD, Schor AM. 1992. Transforming growth factor beta 1 promotes the differentiation of endothelial cells into smooth muscle-like cells in vitro. J. Cell Sci. 103:521-529.
    • (1992) J. Cell Sci. , vol.103 , pp. 521-529
    • Arciniegas, E.1    Sutton, A.B.2    Allen, T.D.3    Schor, A.M.4
  • 61
    • 34447504987 scopus 로고    scopus 로고
    • Perspectives on endothelial-to-mesenchymal transition: potential contribution to vascular remodeling in chronic pulmonary hypertension
    • Arciniegas E, Frid MG, Douglas IS, Stenmark KR. 2007. Perspectives on endothelial-to-mesenchymal transition: potential contribution to vascular remodeling in chronic pulmonary hypertension. Am. J. Physiol. Lung Cell. Mol. Physiol. 293:L1-L8.
    • (2007) Am. J. Physiol. Lung Cell. Mol. Physiol. , vol.293
    • Arciniegas, E.1    Frid, M.G.2    Douglas, I.S.3    Stenmark, K.R.4
  • 62
    • 0037076796 scopus 로고    scopus 로고
    • Mature vascular endothelium can give rise to smooth muscle cells via endothelial-mesenchymal transdifferentiation: in vitro analysis
    • Frid MG, Kale VA, Stenmark KR. 2002. Mature vascular endothelium can give rise to smooth muscle cells via endothelial-mesenchymal transdifferentiation: in vitro analysis. Circ. Res. 90:1189-1196.
    • (2002) Circ. Res. , vol.90 , pp. 1189-1196
    • Frid, M.G.1    Kale, V.A.2    Stenmark, K.R.3
  • 63
    • 0037428453 scopus 로고    scopus 로고
    • Human umbilical vein endothelium-derived cells retain potential to differentiate into smooth muscle-like cells
    • Ishisaki A, Hayashi H, Li AJ, Imamura T. 2003. Human umbilical vein endothelium-derived cells retain potential to differentiate into smooth muscle-like cells. J. Biol. Chem. 278:1303-1309.
    • (2003) J. Biol. Chem. , vol.278 , pp. 1303-1309
    • Ishisaki, A.1    Hayashi, H.2    Li, A.J.3    Imamura, T.4
  • 64
  • 70
    • 0020360978 scopus 로고
    • Isolation and characterization of type IV procollagen, laminin, and heparan sulfate proteoglycan from the EHS sarcoma
    • Kleinman HK, McGarvey ML, Liotta LA, Robey PG, Tryggvason K, Martin GR. 1982. Isolation and characterization of type IV procollagen, laminin, and heparan sulfate proteoglycan from the EHS sarcoma. Biochemistry 21:6188-6193.
    • (1982) Biochemistry , vol.21 , pp. 6188-6193
    • Kleinman, H.K.1    McGarvey, M.L.2    Liotta, L.A.3    Robey, P.G.4    Tryggvason, K.5    Martin, G.R.6
  • 71
    • 4043065142 scopus 로고    scopus 로고
    • The scavenger receptor cysteine-rich (SRCR) domain: an ancient and highly conserved protein module of the innate immune system
    • Sarrias MR, Gronlund J, Padilla O, Madsen J, Holmskov U, Lozano F. 2004. The scavenger receptor cysteine-rich (SRCR) domain: an ancient and highly conserved protein module of the innate immune system. Crit. Rev. Immunol. 24:1-37.
    • (2004) Crit. Rev. Immunol. , vol.24 , pp. 1-37
    • Sarrias, M.R.1    Gronlund, J.2    Padilla, O.3    Madsen, J.4    Holmskov, U.5    Lozano, F.6
  • 72
    • 78651102861 scopus 로고    scopus 로고
    • The human lysyl oxidase-like 2 protein functions as an amine oxidase toward collagen and elastin
    • Kim YM, Kim EC, Kim Y. 2011. The human lysyl oxidase-like 2 protein functions as an amine oxidase toward collagen and elastin. Mol. Biol. Rep. 38:145-149.
    • (2011) Mol. Biol. Rep. , vol.38 , pp. 145-149
    • Kim, Y.M.1    Kim, E.C.2    Kim, Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.