Matrix metalloproteinase inhibitors and cancer

Bibliography

• LIOTTA LA: Cancer cell invasion and metastasis. Sci. Am. (1992) 266(2):54–63.
   PubMed Web of Science ®Google Scholar
• STETLER-STEVENSON WG, HEWITT R, CORCORAN M: Matrix metalloproteinases and tumor invasion: from correlation and causality to the clinic. Cancer Biol. (1996) 7:147–154.
   PubMed Web of Science ®Google Scholar
• BASSET P, OKADA A, CHENARD MP et al.: Matrix metalloptoteinases as stromal effectors of human carcinoma progression: therapeutic implications. Matrix Biol. (1997) 15:535–541.
   PubMed Web of Science ®Google Scholar
• CHAMBERS AF, MATRISIAN LM: Changing views of the role of matrix metalloproteinases in metastasis. J. Nat. Cancer Inst. (1997) 89:1260–1270.
   PubMed Web of Science ®Google Scholar
• KLEINER DE, STETLER-STEVENSON WG: Matrix metallo-proteinases and metastasis. Cancer Chemother. Pharmacol. (1999) 43 (Suppl.):S42–S51.
   Google Scholar
• NELSON AR, FINGLETON B, ROTHENBERG ML, MATRISIAN LM: Matrix metalloproteinases: Biologic activity and clinical implications. J. Clin. Oncol. (2000) 18:1135–1149.
   PubMed Web of Science ®Google Scholar
• HODGSON J: Remodeling MMPIs. Bio/7'echnology (1995)13 :554–557.
   Google Scholar
• BECKETT RP, DAVIDSON AH, DRUMMOND AH, HUXLEYP, WHITTAKER M: Recent advances in matrix metallo-proteinase inhibitor research. Drug Des. Today (1996) 1:16–26.
   Google Scholar
• RASMUSSEN HS, MCCANN PP: Matrix metalloproteinaseinhibition as a novel anticancer strategy: a review with special focus on batimastat and marimastat. Pharmacol. Ther. (1997) 75:69–75.
   PubMed Web of Science ®Google Scholar
• BODE W, FERNANDEZ-CATALAN C, TSCHESCHE H, GRAMS F, NAGASE H, MASKOS K: Structural properties of matrix metalloproteinases. Cell. Mol Life ScL (1999) 55:639–652.
   PubMed Web of Science ®Google Scholar
• BECKETT RP: Recent advances in the field of matrix metalloproteinase inhibitors. Exp. Opin. Ther. Patents (1996) 6:1305–1315.
   Google Scholar
• BECKETT RP, WHITTAKER M: Matrix metalloproteinase inhibitors 1998. Exp. Opin. Ther. Patents (1998) 8:259–282.
   Web of Science ®Google Scholar
• NAGASE H: Matrix metalloproteinases. In: Zinc Metallo-proteases In Health and Disease. Hooper NM (Ed.), Taylor & Francis, London (1996):153–204.
   Google Scholar
• NAGASE H, WOESSNER JF, JR: Matrix metalloprote-inases. J. Biol. Chem. (1999) 274:21491–21494.
   PubMed Web of Science ®Google Scholar
• NAGASE H, FIELDS GB: Human matrix metalloprote-inase specificity studies using collagen sequence-based synthetic peptides. Biopolymers (1996) 40:399–416.
   PubMed Web of Science ®Google Scholar
• ELLERBROEK SM, STACK MS: Membrane associated matrix metalloproteinases in metastasis. BioEssays (1999) 21:940–949.
   PubMed Web of Science ®Google Scholar
• BORKAKOTI N, WINKLER FK, WILLIAMS DH et al: Structure of the catalytic domain of human fibroblast collagenase complexed with an inhibitor. Nature Struct. Biol. (1994) 1:106–110.
   PubMedGoogle Scholar
• SPURLINO JC, SMALLWOOD AM, CARLTON DD et al: 1.56 A Structure of mature truncated human fibroblast collagenase. Proteins (1994) 19:98–109.
   Google Scholar
• LI J, BRICK P, O'HARE MC et al: Structure of full-length porcine synovial collagenase reveals a C-terminal domain containing a calcium-linked, four-bladed 13-propeller. Structure (1995) 3:541–549.
   PubMed Web of Science ®Google Scholar
• VAN DOREN SR, KUROCHKIN AV, HU W et al: Solution structure of the catalytic domain of human strome-lysin complex ed with a hydrophobic inhibitor. Protein ScL (1995) 4:2487–2498.
   PubMed Web of Science ®Google Scholar
• PAVLOVSKY AG, WILLIAMS MG, YE Q-Z et al: X-ray structure of human stromelysin catalytic domain complexed with nonpeptide inhibitors: Implications for inhibitor selectivity. Protein ScL (1999) 8:1455–1462.
   PubMed Web of Science ®Google Scholar
• BODE W, REINEMER P, HUBER R, KLEINE T, SCHNIERER S, TSCHESCHE H: The X-ray crystal structure of the catalytic domain of human neutrophil collagenase inhibited by a substrate analogue reveals the essentials for catalysis and specificity. EMBO J. (1 9 9 4) 1 3:1263-1269.
   Google Scholar
• STAMS T, SPURLINO JC, SMITH DL et al: Structure of human neutrophil collagenase reveals large 51' specificity pocket. Structural Biol. (1994) 1:119–123.
   Google Scholar
• GRAMS F, CRIMMIN M, HINNES L et al.: Structure determination and analysis of human neutrophil collagenase complexed with a hydroxamate inhibitor. Biochemistry (1995) 34:14012–14020.
   PubMed Web of Science ®Google Scholar
• LOVEJOY B, CLEASBY A, HASSELL AM et al.: Structure of the catalytic domain of fibroblast collagenase complexed with an inhibitor. Science (1 9 9 4) 263:375–377.
   Google Scholar
• GOOLEY PR, O'CONNELL JF, MARCY Al et al.: Comparison of the structure of human recombinant short form stromelysin by multidimensional hetero-nuclear NMR and X-ray crystallography. J. Biomol NMR (1996) 7:8–28.
   Google Scholar
• MOY FJ, PISANO MR, CHANDA PK et al.: Assignments, secondary structure and dynamics of the inhibitor-free catalytic fragment of human fibroblast collage-nase. j Biomol. NMI? (1997) 10:9–19.
   PubMedGoogle Scholar
• BODE W, FERNANDEZ-CATALAN C, GRAMS F et al: Insights into MMP-TIMP interactions. Ann. NY Acad. ScL (1999) 878:73–91.
   PubMed Web of Science ®Google Scholar
• MORGUNOVA E, TUUTTILA A, BERGMANN U et al: Structure of human pro-matrix metalloproteinase-2: activation mechanism revealed. Science (19 9 9) 2 8 4:1667-1670.
   Google Scholar
• PERONA JJ, TSU CA, CRAIK CS, FLETTERICK RJ: Crystal structure of an ecotin-collagenase complex suggests a model for recognition and cleavage of the collagen triple helix. Biochemistry (1997) 36:5381–5392.
   PubMedGoogle Scholar
• BROUTIN-L'HERMITE I, RIES-KAUTT M, DUCRUIX A: 1.7 A X-ray structure of space-grown collagenase crystals. Acta Clyst. (2000) D56:376–378.
   Google Scholar
• FOX S: European roundup: no anticancer benefit in trials of marimastat. GeN. Engl. News (2000) 20 (4):30.
   Google Scholar
• FOX S. European roundup: Andre Pernet assumes the helm at Genset. GeN. Engl. News (2000) 20 (14) :38, 39, 84.
   Google Scholar
• MATTER H, SCHWAB W, BARBIER D et al: Quantitative structure-activity relationship of human neutrophil collagenase (MMP-8) inhibitors using comparative molecular field analysis and X-ray structure analysis.J. Med. Chem. (1999) 42:1908–1920.
   PubMed Web of Science ®Google Scholar
• VASSILIOU S, MUCHA A, CUNIASSE P et al: Phosphinic pseudo-tripeptides as potent inhibitors of matrix metalloproteinases: a structure-activity study. J Med. Chem. (1999) 42:2610–2620.
   PubMed Web of Science ®Google Scholar
• BROWN S, BERNARDO MM, LI Z-H et al.: Potent andselective mechanism-based inhibition of gelatinases. Am. Chem. Soc. (2000) 1 2 2:6799–6800.
   Google Scholar
• SZARDENINGS AK, ANTONENKO V, CAMPBELL DA et al.:Identification of highly selective inhibitors of collagenase-1 from combinatorial libraries of diketopiperazines. J Med. Chem. (1999) 42:1348–1357.
   PubMed Web of Science ®Google Scholar
• DEMEULE M, BROSSARD M, PAGE M, GINGRAS D, BELIVEAU R: Matrix metalloproteinase inhibition by green tea catchins. Biochim. Biophys. Acta (2000) 1478:51–60.
   PubMed Web of Science ®Google Scholar
• GOMIS-RUTH FX, MASKOS K, BETZ M et al: Mechanismof inhibition of the human matrix metalloproteinase stromelysin-1 by TIMP-1. Nature (1997) 389:77–81.
   PubMed Web of Science ®Google Scholar
• AHONEN M, BAKER AH, KAHARI V-M: Adenovirus-mediated gene delivery of tissue inhibitor of metalloproteinases-3 inhibits invasion and induces apoptosis in melanoma cells. Cancer Res. (1998) 5 8:2310–2315.
   Google Scholar
• MACKAY AR, CORBITT RH, HARTZLER JL, THORGEIRSSON UP: Basement membrane Type W collagen degradation: evidence for the involvement of proteolytic cascade independent of matrix metallo-proteinases. Cancer Res. (1990) 50:5997–6001.
   PubMed Web of Science ®Google Scholar
• OTTL J, BATTISTUTA R, PIEPER M et al.: Design and synthesis of heterotrimeric collagen peptides with a cystine-knot. FEBS Lett. (1996) 398:31–36.
   PubMed Web of Science ®Google Scholar
• OTTL J, MORODER L: Disulfide-bridged heterotrimeric collagen peptides containing the collagenase cleavage site of collagen Type I: synthesis and conformational properties. J. Am. Chem. Soc. (1999) 121:653–661.
   Web of Science ®Google Scholar
• OTTL J, GABRIEL D, MURPHY G et al.: Recognition and catabolism of synthetic heterotrimeric collagen peptides by matrix metalloproteinases. Chem. Biol. (2000) 7:119–132.
   PubMed Web of Science ®Google Scholar
• LAUER-FIELDS JL, TUZINSKI KA, SHIMOKAWA K-I, NAGASE H, FIELDS GB: Hydrolysis of triple-helical collagen peptide models by matrix metalloprote-inases. J. Biol. Chem. (2000) 275:13282–13290.
   PubMed Web of Science ®Google Scholar
• LAUER-FIELDS JL, NAGASE H, FIELDS GB: Use of Edman degradation sequence analysis and matrix-assisted laser desorption/ionization mass spectrometry in designing substrates for matrix metalloproteinases. Chromatogr. A. (2000) 890:117–125.
   PubMed Web of Science ®Google Scholar