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Volumn 14, Issue 8, 2004, Pages 1185-1197

Inhibition of procollagen C-proteinase: Fibrosis and beyond

Author keywords

Bone morphogenetic protein 1; Fibrosis; Mammalian tolloid; Procollagen C proteinase; Tolloid like protein

Indexed keywords

4 MERCAPTOANILINE; ANTIFIBROTIC AGENT; ASTACIN; BIGLYCAN; BONE MORPHOGENETIC PROTEIN; CARBOXYLIC ACID DERIVATIVE; CGS 27023A; CHORDIN; COLLAGEN; COLLAGEN FIBRIL; ENZYME INHIBITOR; GLUTAMIC ACID DERIVATIVE; HYDROXAMIC ACID DERIVATIVE; ISOENZYME; KALININ; MARIMASTAT; MATRIX METALLOPROTEINASE; MATRIX METALLOPROTEINASE INHIBITOR; MATRIX PROTEIN; MYOSTATIN; OXIDOREDUCTASE; PHOSPHINIC ACID DERIVATIVE; PRINOMASTAT; PROCOLLAGEN; PROCOLLAGEN C PROTEINASE; SULFONAMIDE; THIOL DERIVATIVE; TYROSINE HYDROXAMIC ACID; UK 383367; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 4344600469     PISSN: 13543776     EISSN: None     Source Type: Journal    
DOI: 10.1517/13543776.14.8.1185     Document Type: Review
Times cited : (20)

References (64)
  • 1
    • 0033568003 scopus 로고    scopus 로고
    • Mammalian BMP-1/tolloid-related metalloproteinases, including novel family member mammalian tolloid-like 2, have differential enzymatic activities and distributions of expression relevant to patterning and skeletogenesis
    • SCOTT IC, BLITZ IL, PAPPANO WN et al.: Mammalian BMP-1/tolloid-related metalloproteinases, including novel family member mammalian tolloid-like 2, have differential enzymatic activities and distributions of expression relevant to patterning and skeletogenesis. Dev. Biol. (1999) 213(2):283-300.
    • (1999) Dev. Biol. , vol.213 , Issue.2 , pp. 283-300
    • Scott, I.C.1    Blitz, I.L.2    Pappano, W.N.3
  • 2
    • 0028608106 scopus 로고
    • Bone morphogenetic protein-1 and a mammalian tolloid homologue (mTld) are encoded by alternatively spliced transcripts which are differentially expressed in some tissues
    • TAKAHARA K, LYONS GE, GREENSPAN DS: Bone morphogenetic protein-1 and a mammalian tolloid homologue (mTld) are encoded by alternatively spliced transcripts which are differentially expressed in some tissues. J. Biol. Chem. (1994) 269(51):32572-32578.
    • (1994) J. Biol. Chem. , vol.269 , Issue.51 , pp. 32572-32578
    • Takahara, K.1    Lyons, G.E.2    Greenspan, D.S.3
  • 3
    • 0031940912 scopus 로고    scopus 로고
    • Procollagen N-proteinase and procollagen C-proteinase. Two unusual metalloproteinases that are essential for procollagen processing probably have important roles in development and cell signaling
    • PROCKOP DJ, SIERON AL, LI S: Procollagen N-proteinase and procollagen C-proteinase. Two unusual metalloproteinases that are essential for procollagen processing probably have important roles in development and cell signaling. Matrix Biol. (1998) 16:399-408.
    • (1998) Matrix Biol. , vol.16 , pp. 399-408
    • Prockop, D.J.1    Sieron, A.L.2    Li, S.3
  • 4
    • 0015164941 scopus 로고
    • Procollagen peptidase: An enzyme excising the coordination peptides of procollagen
    • LAPIERE CM, LENARERS A, KOHN ID: Procollagen peptidase: an enzyme excising the coordination peptides of procollagen. Proc. Natl. Acad. Sci. USA (1971) 68:3054-3058.
    • (1971) Proc. Natl. Acad. Sci. USA , vol.68 , pp. 3054-3058
    • Lapiere, C.M.1    Lenarers, A.2    Kohn, I.D.3
  • 5
    • 0022392606 scopus 로고
    • Type I procollagen carboxy-terminal proteinase from chick embryo tendons. Purification and characterization
    • HOJIMA Y, VAN DER REST M, PROCKOP DJ: Type I procollagen carboxy-terminal proteinase from chick embryo tendons. Purification and characterization: J. Biol. Chem. (1985) 260:15996-16003.
    • (1985) J. Biol. Chem. , vol.260 , pp. 15996-16003
    • Hojima, Y.1    Van Der Rest, M.2    Prockop, D.J.3
  • 6
    • 0024818507 scopus 로고
    • Type I procollagen C-proteinase from mouse fibroblasts. Purification and demonstration of a 55kD enhancer glycoprotein
    • KESSLER E, ADAR R: Type I procollagen C-proteinase from mouse fibroblasts. Purification and demonstration of a 55kD enhancer glycoprotein. Eur. J. Biochem. (1989) 186:115-121.
    • (1989) Eur. J. Biochem. , vol.186 , pp. 115-121
    • Kessler, E.1    Adar, R.2
  • 7
    • 0029906315 scopus 로고    scopus 로고
    • The C-proteinase that processes procollagens to fibrillar collagens is identical to the protein previously identified as bone morphogenic protein-1
    • Ll S, SIERON AL, FERTALA A, HOJIMA Y, ARNOLD WV: The C-proteinase that processes procollagens to fibrillar collagens is identical to the protein previously identified as bone morphogenic protein-1. Proc. Natl. Acad. Sci. USA (1996) 93:5127-5130.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 5127-5130
    • Li, S.1    Sieron, A.L.2    Fertala, A.3    Hojima, Y.4    Arnold, W.V.5
  • 8
    • 0029929954 scopus 로고    scopus 로고
    • Characterization of a novel gene product (mammalian tolloid-like) with high sequence similarity to mammalian tolloid/bone morphogenetic protein-1
    • TAKAHARA K, BREVARD R, HOFFMAN GG, SUZUKI N, GREENSPAN DS: Characterization of a novel gene product (mammalian tolloid-like) with high sequence similarity to mammalian tolloid/bone morphogenetic protein-1. Genomics (1996) 34:157-165.
    • (1996) Genomics , vol.34 , pp. 157-165
    • Takahara, K.1    Brevard, R.2    Hoffman, G.G.3    Suzuki, N.4    Greenspan, D.S.5
  • 9
    • 0024256133 scopus 로고
    • Novel regulators of bone formation: Molecular clones and activities
    • WOZNEY JM, ROSEN V, CELESTE AJ et al.: Novel regulators of bone formation: molecular clones and activities. Science (1988) 242:1528-1534.
    • (1988) Science , vol.242 , pp. 1528-1534
    • Wozney, J.M.1    Rosen, V.2    Celeste, A.J.3
  • 11
    • 9144243683 scopus 로고    scopus 로고
    • Activation of the latent myostatin by the BMP/tolloid family of metalloproteinases
    • WOLFMAN NM, MCPHERRON AC, PAPPANO WN et al.: Activation of the latent myostatin by the BMP/tolloid family of metalloproteinases. Proc. Natl. Acad. Sci. USA (2003) 100(26):15842-15846.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , Issue.26 , pp. 15842-15846
    • Wolfman, N.M.1    McPherron, A.C.2    Pappano, W.N.3
  • 12
    • 0032040227 scopus 로고    scopus 로고
    • Holy tolloido - Tolloid cleaves SOG/chordin to free DPP/BMPs
    • MULLINS MC: Holy tolloido - tolloid cleaves SOG/chordin to free DPP/BMPs. Trends Genet. (1998) 14(4):127-129.
    • (1998) Trends Genet. , vol.14 , Issue.4 , pp. 127-129
    • Mullins, M.C.1
  • 13
    • 0037705369 scopus 로고    scopus 로고
    • Bone morphogenetic protein-1 (BMP-1) identification of the minimal domain structure for procollagen C-proteinase activity
    • HARTIGAN N, GARRIGUE-ANTAR L, KADLER KE: Bone morphogenetic protein-1 (BMP-1) identification of the minimal domain structure for procollagen C-proteinase activity. J. Biol. Chem. (2003) 278(20):18045-18049.
    • (2003) J. Biol. Chem. , vol.278 , Issue.20 , pp. 18045-18049
    • Hartigan, N.1    Garrigue-Antar, L.2    Kadler, K.E.3
  • 14
    • 0035854824 scopus 로고    scopus 로고
    • Identification of amino acid residues in bone morphogenetic protein-1 important for procollagen C-proteinase activity
    • GARRIGUE-ANTAR L, BARKER C, KADLER KE: Identification of amino acid residues in bone morphogenetic protein-1 important for procollagen C-proteinase activity. J. Biol. Chem. (2001) 276(28):26237-26242.
    • (2001) J. Biol. Chem. , vol.276 , Issue.28 , pp. 26237-26242
    • Garrigue-Antar, L.1    Barker, C.2    Kadler, K.E.3
  • 15
    • 0029016839 scopus 로고
    • The astacin family of metalloendopeptidases
    • BOND JS, BEYNON RJ: The astacin family of metalloendopeptidases. Protein Sci. (1995) 4:1247-1261.
    • (1995) Protein Sci. , vol.4 , pp. 1247-1261
    • Bond, J.S.1    Beynon, R.J.2
  • 16
    • 0027418428 scopus 로고
    • Refined 1.8 Å X-ray crystal structure of Astacin, a zinc-endopeptidase from the crayfish Astacus astacus L
    • GOMIS-RUTH FX, STOCKER W, HUBER R, ZWILLING R, BODE W: Refined 1.8 Å X-ray crystal structure of Astacin, a zinc-endopeptidase from the crayfish Astacus astacus L. J. Mol. Biol. (1993) 229:945-968.
    • (1993) J. Mol. Biol. , vol.229 , pp. 945-968
    • Gomis-Ruth, F.X.1    Stocker, W.2    Huber, R.3    Zwilling, R.4    Bode, W.5
  • 18
    • 0030802909 scopus 로고    scopus 로고
    • Transforming growth factor-β regulation of bone morphogenetic protein-1/procollagen C-proteinase and related proteins in fibrogenic cells and keratinocytes
    • LEE S, SOLOW-CORDERO DE, KESSLER E, TAKAHARA K, GREENSPAN DS: Transforming growth factor-β regulation of bone morphogenetic protein-1/procollagen C-proteinase and related proteins in fibrogenic cells and keratinocytes. J. Biol. Chem. (1997) 272(30):19059-19066.
    • (1997) J. Biol. Chem. , vol.272 , Issue.30 , pp. 19059-19066
    • Lee, S.1    Solow-Cordero, D.E.2    Kessler, E.3    Takahara, K.4    Greenspan, D.S.5
  • 19
    • 0038043187 scopus 로고    scopus 로고
    • Paired basic/furin-like proprotein convertase cleavage of pro-BMP-1 in the trans-Golgi Network
    • LEIGHTON M, KADLER KE: Paired basic/furin-like proprotein convertase cleavage of pro-BMP-1 in the trans-Golgi Network. J. Biol. Chem. (2003) 278(20):18478-18484.
    • (2003) J. Biol. Chem. , vol.278 , Issue.20 , pp. 18478-18484
    • Leighton, M.1    Kadler, K.E.2
  • 20
    • 0037044775 scopus 로고    scopus 로고
    • Post-translational modification of bone morphogenetic protein-1 is required for secretion and stability of the protein
    • GARRIGUE-ANTAR L, HARTIGAN N, KADLER KE: Post-translational modification of bone morphogenetic protein-1 is required for secretion and stability of the protein. J. Biol. Chem. (2002) 277(45):43327-43334.
    • (2002) J. Biol. Chem. , vol.277 , Issue.45 , pp. 43327-43334
    • Garrigue-Antar, L.1    Hartigan, N.2    Kadler, K.E.3
  • 21
    • 0347298758 scopus 로고    scopus 로고
    • PCOLCE2 encodes a functional procollagen c-proteinase enhancer (PCPE2) that is a collagen-binding protein differing in distribution of expression and post-translational modification from the previously described PCPE1
    • STEIGLITZ BM, KEENE DR, GREENSPAN DS: PCOLCE2 encodes a functional procollagen c-proteinase enhancer (PCPE2) that is a collagen-binding protein differing in distribution of expression and post-translational modification from the previously described PCPE1. J. Biol. Chem. (2002) 277(51):49820-49830.
    • (2002) J. Biol. Chem. , vol.277 , Issue.51 , pp. 49820-49830
    • Steiglitz, B.M.1    Keene, D.R.2    Greenspan, D.S.3
  • 22
    • 18544364796 scopus 로고    scopus 로고
    • Interaction properties of the procollagen c-proteinase enhancer protein shed light on the mechanism of stimulation of VMP-1
    • RICARD-BLUM S, BERNOCCO S, FONT B et al.: Interaction properties of the procollagen c-proteinase enhancer protein shed light on the mechanism of stimulation of VMP-1. J. Biol. Chem. (2002) 277(37):33864-33869.
    • (2002) J. Biol. Chem. , vol.277 , Issue.37 , pp. 33864-33869
    • Ricard-Blum, S.1    Bernocco, S.2    Font, B.3
  • 23
    • 0035933765 scopus 로고    scopus 로고
    • Multiple bone morphogenetic protein-1 related mammalian metalloproteinases process pro-lysyl oxidase at the correct physiological site and control lysyl oxidase activation in mouse embryo fibroblast cultures
    • UZEL MI, SCOTT IC, BABAKHANLOU-CHASE H et al.: Multiple bone morphogenetic protein-1 related mammalian metalloproteinases process pro-lysyl oxidase at the correct physiological site and control lysyl oxidase activation in mouse embryo fibroblast cultures. J. Biol. Chem. (2001) 276(25):22537-22543.
    • (2001) J. Biol. Chem. , vol.276 , Issue.25 , pp. 22537-22543
    • Uzel, M.I.1    Scott, I.C.2    Babakhanlou-Chase, H.3
  • 24
    • 0347723963 scopus 로고    scopus 로고
    • Bone Morphogenetic protein-1/tolloid-like proteinases process dentin matrix protein
    • STEIGLITZ BM, AYALA M, NARAYANAN K, GEORGE A, GREENSPAN DS: Bone Morphogenetic protein-1/tolloid-like proteinases process dentin matrix protein. J. Biol. Chem. (2004) 279(2):980-986.
    • (2004) J. Biol. Chem. , vol.279 , Issue.2 , pp. 980-986
    • Steiglitz, B.M.1    Ayala, M.2    Narayanan, K.3    George, A.4    Greenspan, D.S.5
  • 25
    • 0038044731 scopus 로고    scopus 로고
    • Use of Bmp 1/tll1 doubly homozygous null mice and proteomics to identify an validate in vivo substrates of bone morphogenetic protein 1/tolloid-like metalloproteinases
    • PAPPANO WN, STEIGLITZ BM, SCOTT IC, KEENE DR, GREENSPAN DS: Use of Bmp 1/tll1 doubly homozygous null mice and proteomics to identify an validate in vivo substrates of bone morphogenetic protein 1/tolloid-like metalloproteinases. Mol. Cell. Bio. (2003) 23(13):4428-4438.
    • (2003) Mol. Cell. Bio. , vol.23 , Issue.13 , pp. 4428-4438
    • Pappano, W.N.1    Steiglitz, B.M.2    Scott, I.C.3    Keene, D.R.4    Greenspan, D.S.5
  • 26
    • 0037135569 scopus 로고    scopus 로고
    • Proteinases of the bone morphogenetic protein-1 family convert procollagen VII to mature anchoring fibril collagen
    • RATTENHOLL A, PAPPANO WN, KOCH M et al.: Proteinases of the bone morphogenetic protein-1 family convert procollagen VII to mature anchoring fibril collagen. J. Biol. Chem. (2002) 277(29):26372-26378.
    • (2002) J. Biol. Chem. , vol.277 , Issue.29 , pp. 26372-26378
    • Rattenholl, A.1    Pappano, W.N.2    Koch, M.3
  • 27
    • 0348147583 scopus 로고    scopus 로고
    • BMP-1 mediated proteolytic processing of alternatively spliced isoforms of collagen type XI
    • MEDECK RJ, SOSA S, MORRIS N, OXFORD JT. BMP-1 mediated proteolytic processing of alternatively spliced isoforms of collagen type XI. Biochem J. (2003) 376:361-368.
    • (2003) Biochem J. , vol.376 , pp. 361-368
    • Medeck, R.J.1    Sosa, S.2    Morris, N.3    Oxford, J.T.4
  • 28
    • 0034724260 scopus 로고    scopus 로고
    • Structure and function of Procollagen C-proteinase (m Tolloid) domains determined by protease digestion, circular dichroism, binding to procollagen Type I, and computer modeling
    • SIERON AL, TRETIAKOVA A, JAMESON BA et al.: Structure and function of Procollagen C-proteinase (m Tolloid) domains determined by protease digestion, circular dichroism, binding to procollagen Type I, and computer modeling. Biochemistry (2000) 39:3231-3239.
    • (2000) Biochemistry , vol.39 , pp. 3231-3239
    • Sieron, A.L.1    Tretiakova, A.2    Jameson, B.A.3
  • 29
    • 0035920213 scopus 로고    scopus 로고
    • Bone morphogenetic protein-1 (BMP-1) mediates C-terminal processing of procollagen V homotrimer
    • KESSLER E, FICHARD A, CHANUT-DELALANDE H, BRUSEL M, RUGGIERO F: Bone morphogenetic protein-1 (BMP-1) mediates C-terminal processing of procollagen V homotrimer. J. Biol Chem. (2001) 276(29):27051-27057.
    • (2001) J. Biol Chem. , vol.276 , Issue.29 , pp. 27051-27057
    • Kessler, E.1    Fichard, A.2    Chanut-Delalande, H.3    Brusel, M.4    Ruggiero, F.5
  • 31
    • 0034730627 scopus 로고    scopus 로고
    • Bone morphogenetic protein-1 processes probiglycan
    • SCOTT IC, IMAMURA Y, PAPPANO WN et al.: Bone morphogenetic protein-1 processes probiglycan. J. Biol. Chem. (2000) 275(39):30504-30511.
    • (2000) J. Biol. Chem. , vol.275 , Issue.39 , pp. 30504-30511
    • Scott, I.C.1    Imamura, Y.2    Pappano, W.N.3
  • 33
    • 0029098129 scopus 로고
    • Decorin-binding sites for collagen Type I are mainly located in leucine-rich repeats 4-5
    • SVENSSON L, HEINEGARD D, OLDBERG A: Decorin-binding sites for collagen Type I are mainly located in leucine-rich repeats 4-5. J. Biol. Chem. (1995) 270(35): 20712-20716.
    • (1995) J. Biol. Chem. , vol.270 , Issue.35 , pp. 20712-20716
    • Svensson, L.1    Heinegard, D.2    Oldberg, A.3
  • 34
    • 0034725611 scopus 로고    scopus 로고
    • Bone morphogenetic protein 1 is an extracellular processing enzyme of the laminin 5γ2 chain
    • AMANO S, SCOTT IC, TAKAHARA K et al.: Bone morphogenetic protein 1 is an extracellular processing enzyme of the laminin 5γ2 chain. J. Biol. Chem. (2000) 275(30):22728-22735.
    • (2000) J. Biol. Chem. , vol.275 , Issue.30 , pp. 22728-22735
    • Amano, S.1    Scott, I.C.2    Takahara, K.3
  • 35
    • 0141668890 scopus 로고    scopus 로고
    • Evidence for the proteolytic processing of dentin matrix protein 1
    • QIN C, BRUNN JC, COOK RG et al.: Evidence for the proteolytic processing of dentin matrix protein 1. J. Biol. Chem. (2003) 278(36):34700-34708.
    • (2003) J. Biol. Chem. , vol.278 , Issue.36 , pp. 34700-34708
    • Qin, C.1    Brunn, J.C.2    Cook, R.G.3
  • 36
    • 0031465734 scopus 로고    scopus 로고
    • Cleavage of the BMP4 antagonist chordin by zebrafish tolloid
    • BLADER P, RASTEGAR S, FISCHER N, STRAHLE U: Cleavage of the BMP4 antagonist chordin by zebrafish tolloid. Science (1997) 278:1937-1940.
    • (1997) Science , vol.278 , pp. 1937-1940
    • Blader, P.1    Rastegar, S.2    Fischer, N.3    Strahle, U.4
  • 37
    • 4344717210 scopus 로고    scopus 로고
    • New targets for the treatment of pathological fibrosis, an unmet clinical need
    • ZAVOICO GB: New targets for the treatment of pathological fibrosis, an unmet clinical need. Drug Market Dev. (1999) 10(1):2-10.
    • (1999) Drug Market Dev. , vol.10 , Issue.1 , pp. 2-10
    • Zavoico, G.B.1
  • 38
    • 0025972679 scopus 로고
    • Fibroproliferative disorders
    • BITTERMAN PB, HENKE CA: Fibroproliferative disorders. Chest (1991) 99(3):81S-84S.
    • (1991) Chest , vol.99 , Issue.3
    • Bitterman, P.B.1    Henke, C.A.2
  • 39
    • 0026799246 scopus 로고
    • Continuum model of fibroblast-driven wound contraction: Inflammation-mediation
    • TRANSQUILLO RT, MURRAY JD: Continuum model of fibroblast-driven wound contraction: inflammation-mediation. J. Ther. Biol. (1992) 158:135-172.
    • (1992) J. Ther. Biol. , vol.158 , pp. 135-172
    • Transquillo, R.T.1    Murray, J.D.2
  • 41
    • 0038521319 scopus 로고    scopus 로고
    • Mammalian tolloid metalloproteinase, and not matrix metalloprotease 2 or membrane Type 1 metalloprotease, process laminin-5 in keratinocytes and skin
    • VEITCH DP, NOKELAINEN P, MCGOWAN KA et al.: Mammalian tolloid metalloproteinase, and not matrix metalloprotease 2 or membrane Type 1 metalloprotease, process laminin-5 in keratinocytes and skin. J. Biol. Chem. (2003) 278(18):15661-15668.
    • (2003) J. Biol. Chem. , vol.278 , Issue.18 , pp. 15661-15668
    • Veitch, D.P.1    Nokelainen, P.2    McGowan, K.A.3
  • 42
    • 0035892362 scopus 로고    scopus 로고
    • Laminin-5 in the progression of carcinomas
    • LOHI J: Laminin-5 in the progression of carcinomas. Int. J Cancer. (2001) 94:763-767.
    • (2001) Int. J. Cancer , vol.94 , pp. 763-767
    • Lohi, J.1
  • 43
    • 0034858098 scopus 로고    scopus 로고
    • Biological and clinical relevance of laminin-5 in cancer
    • GIANNELLI G, ANTONACI S: Biological and clinical relevance of laminin-5 in cancer. Clin. Exp. Metastasis (2000) 18(6):439-443.
    • (2000) Clin. Exp. Metastasis , vol.18 , Issue.6 , pp. 439-443
    • Giannelli, G.1    Antonaci, S.2
  • 44
    • 0035858887 scopus 로고    scopus 로고
    • The short arm of the laminin γ2 chain plays a pivotal role in the incorporation of laminin-5 into the extracellular matrix and in cell adhesion
    • GAGNOUX-PALACIOS L, ALLEGRA M, SPIRITO F et al.: The short arm of the laminin γ2 chain plays a pivotal role in the incorporation of laminin-5 into the extracellular matrix and in cell adhesion. J. Cell Biol. (2001) 153(4):835-849.
    • (2001) J. Cell Biol. , vol.153 , Issue.4 , pp. 835-849
    • Gagnoux-Palacios, L.1    Allegra, M.2    Spirito, F.3
  • 46
    • 0035205898 scopus 로고    scopus 로고
    • Tumor deposition of laminin-5 and the relationship with perineural invasion
    • ANDERSON TD, FELDMAN M, WEBER RS, ZIOBER AF, ZIOBER BL: Tumor deposition of laminin-5 and the relationship with perineural invasion. Laryngoscope (2001) 111:2140-2143.
    • (2001) Laryngoscope , vol.111 , pp. 2140-2143
    • Anderson, T.D.1    Feldman, M.2    Weber, R.S.3    Ziober, A.F.4    Ziober, B.L.5
  • 47
    • 0037168957 scopus 로고    scopus 로고
    • Epidermal growth factor receptor gene amplification is correlated with laminin-5 γ2 chain expression in oral squamous cell carcinoma cell lines
    • ONO Y, NAKANISHI Y, GOTOH M, SAKAMOTO M, HIROHASHI S: Epidermal growth factor receptor gene amplification is correlated with laminin-5 γ2 chain expression in oral squamous cell carcinoma cell lines. Cancer Lett. (2002) 175:197-204.
    • (2002) Cancer Lett. , vol.175 , pp. 197-204
    • Ono, Y.1    Nakanishi, Y.2    Gotoh, M.3    Sakamoto, M.4    Hirohashi, S.5
  • 48
    • 0033520765 scopus 로고    scopus 로고
    • Laminin-5 as a marker of invasiveness in cervical lesions
    • SKYLDBERG B, SALO S, ERIKSSON E et al.: Laminin-5 as a marker of invasiveness in cervical lesions. J. Natl. Cancer Inst. (1999) 91(21):1882-1887.
    • (1999) J. Natl. Cancer Inst. , vol.91 , Issue.21 , pp. 1882-1887
    • Skyldberg, B.1    Salo, S.2    Eriksson, E.3
  • 49
    • 0034800325 scopus 로고    scopus 로고
    • Laminin-5 gamma2 chain expression correlates with unfavorable prognosis in colon carcinomas
    • LENANDER C, HABERMANN JK, OST A et al.: Laminin-5 gamma2 chain expression correlates with unfavorable prognosis in colon carcinomas. Anal. Cell. Pathol. (2001) 22(4):201-209.
    • (2001) Anal. Cell. Pathol. , vol.22 , Issue.4 , pp. 201-209
    • Lenander, C.1    Habermann, J.K.2    Ost, A.3
  • 50
    • 0141679409 scopus 로고    scopus 로고
    • Laminin-5 chains are expressed differentially in metastatic and nonmetastatic hepatocellular carcinoma
    • GIANNELLI G, FRANSVEA E, BERGAMINI C, MARINOSCI F, ANTONACI S: Laminin-5 chains are expressed differentially in metastatic and nonmetastatic hepatocellular carcinoma. Clin. Cancer Res. (2003) 9(10):3684-3691.
    • (2003) Clin. Cancer Res. , vol.9 , Issue.10 , pp. 3684-3691
    • Giannelli, G.1    Fransvea, E.2    Bergamini, C.3    Marinosci, F.4    Antonaci, S.5
  • 51
    • 33746372370 scopus 로고    scopus 로고
    • BMP-1 processing of laminin-5 controls migration of human epithelial cells
    • Chicago, USA
    • MCGOWAN K, VEITCH D, FINDELL P et al.: BMP-1 processing of laminin-5 controls migration of human epithelial cells. Ann. Meeting Soc. Invest. Dermatol. Chicago, USA (2000).
    • (2000) Ann. Meeting Soc. Invest. Dermatol
    • Mcgowan, K.1    Veitch, D.2    Findell, P.3
  • 52
    • 0025144326 scopus 로고
    • Thio containing compounds and amino acid hydroxamates as reversible synthetic inhibitors of astacus proteinase
    • WOLZ RL, ZEGGAF C, STOCKER W, ZWILLING R: Thio containing compounds and amino acid hydroxamates as reversible synthetic inhibitors of astacus proteinase. Arch. Biochem. Biophys. (1990) 281(2):275-281.
    • (1990) Arch. Biochem. Biophys. , vol.281 , Issue.2 , pp. 275-281
    • Wolz, R.L.1    Zeggaf, C.2    Stocker, W.3    Zwilling, R.4
  • 53
    • 0032522565 scopus 로고    scopus 로고
    • Phosphinic acids, the first potent inhibitors of astacin, behave as extremely slow-binding inhibitors
    • YIALLOUROS I, VASSILIOU S, YIOTAKIS A, ZWILLING R, STOCKER W, DIVE V: Phosphinic acids, the first potent inhibitors of astacin, behave as extremely slow-binding inhibitors. Biochem. J. (1998) 331:375-379.
    • (1998) Biochem. J. , vol.331 , pp. 375-379
    • Yiallouros, I.1    Vassiliou, S.2    Yiotakis, A.3    Zwilling, R.4    Stocker, W.5    Dive, V.6
  • 55
    • 0033832622 scopus 로고    scopus 로고
    • Design and synthesis of acidic dipeptide hydroxamate inhibitors of procollagen C-proteinase
    • OVENS A, JOULE JA, KADLER KE: Design and synthesis of acidic dipeptide hydroxamate inhibitors of procollagen C-proteinase. J. Peptide Sci. (2000) 6:489-495.
    • (2000) J. Peptide Sci. , vol.6 , pp. 489-495
    • Ovens, A.1    Joule, J.A.2    Kadler, K.E.3
  • 57
    • 0037156344 scopus 로고    scopus 로고
    • Amino acid derived sulfonamide hydroxamates as inhibitors of procollagen C-proteinase. Part 2: Solid-phase optimization of side chains
    • DANKWARDT SM, ABBOT SC, BROKA CA, MARTIN RL, CHAN CS, SPRINGMAN EB et al.: Amino acid derived sulfonamide hydroxamates as inhibitors of procollagen C-proteinase. Part 2: Solid-phase optimization of side chains. Bioorg. Med. Chem. Lett. (2002) 12:1233-1235.
    • (2002) Bioorg. Med. Chem. Lett. , vol.12 , pp. 1233-1235
    • Dankwardt, S.M.1    Abbot, S.C.2    Broka, C.A.3    Martin, R.L.4    Chan, C.S.5    Springman, E.B.6
  • 58
    • 4344583537 scopus 로고    scopus 로고
    • Discovery of UK-383,367, a potent and selective non-peptidic inhibitor of procollagen C-proteinase for the treatment of dermal scarring
    • Anaheim, USA MEDI 13
    • BAILEY S, FISH PV, JAMES K, MCELROY A: Discovery of UK-383,367, a potent and selective non-peptidic inhibitor of procollagen C-proteinase for the treatment of dermal scarring. 227th American Chem. Soc. National Meeting. Anaheim, USA (2004) MEDI 13.
    • (2004) 227th American Chem. Soc. National Meeting
    • Bailey, S.1    Fish, P.V.2    James, K.3    McElroy, A.4
  • 59
    • 0035966867 scopus 로고    scopus 로고
    • Development of new carboxylic acid-based MMP inhibitors derived from functionalized propargylglycines
    • NATCHUS MG, BOOKLAND RG, LAUTERSWEILER MJ et al.: Development of new carboxylic acid-based MMP inhibitors derived from functionalized propargylglycines. J. Med. Chem. (2001) 44:1060-1071.
    • (2001) J. Med. Chem. , vol.44 , pp. 1060-1071
    • Natchus, M.G.1    Bookland, R.G.2    Lautersweiler, M.J.3
  • 60
    • 10544240364 scopus 로고    scopus 로고
    • Failure of ventral body wall closure in mouse embryos lacking a procollagen C-proteinase encoded by BMP1, a mammalian gene related to Drosophila tolloid
    • SUZUKI N, LABOSKY PA, FURUTA Y et al.: Failure of ventral body wall closure in mouse embryos lacking a procollagen C-proteinase encoded by BMP1, a mammalian gene related to Drosophila tolloid. Development (1996) 122:3587-3595.
    • (1996) Development , vol.122 , pp. 3587-3595
    • Suzuki, N.1    Labosky, P.A.2    Furuta, Y.3
  • 61
    • 0037137618 scopus 로고    scopus 로고
    • NMR-based modification of matrix metalloproteinase inhibitors with improved bioavailibility
    • HAJDUK PJ, SHUKER SB, NETTESHEIM DG et al.: NMR-based modification of matrix metalloproteinase inhibitors with improved bioavailibility. J. Med. Chem. (2002) 45:5628-5639.
    • (2002) J. Med. Chem. , vol.45 , pp. 5628-5639
    • Hajduk, P.J.1    Shuker, S.B.2    Nettesheim, D.G.3
  • 62
    • 15644374838 scopus 로고    scopus 로고
    • Discovery of CGS-27023A, a non-peptidic, potent, and orally active stromelysin inhibitor that blocks cartilage degradation in rabbits
    • MACPHERSON LJ, BAYBURT EK, CAPPARELLI MP et al.: Discovery of CGS-27023A, a non-peptidic, potent, and orally active stromelysin inhibitor that blocks cartilage degradation in rabbits. J. Med. Chem. (1997) 40:2525-2532.
    • (1997) J. Med. Chem. , vol.40 , pp. 2525-2532
    • Macpherson, L.J.1    Bayburt, E.K.2    Capparelli, M.P.3
  • 63
    • 0028891669 scopus 로고
    • Relationship between structure and bioavailability in a series of hydroxamate based metalloprotease inhibitors
    • SINGH J, CONZENTINO P, CUNDY K et al.: Relationship between structure and bioavailability in a series of hydroxamate based metalloprotease inhibitors. Bioorg. Med. Chem. Lett. (1995) 5:337-342.
    • (1995) Bioorg. Med. Chem. Lett. , vol.5 , pp. 337-342
    • Singh, J.1    Conzentino, P.2    Cundy, K.3


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