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Volumn 10, Issue 9, 2010, Pages 794-805

Recent advances in the development of MMPIs and APNIs based on the pyrrolidine platforms

Author keywords

Anticancer; APNIs; Design; MMPIs; Pyrrolidine

Indexed keywords

ANTINEOPLASTIC AGENT; MATRIX METALLOPROTEINASE; MATRIX METALLOPROTEINASE INHIBITOR; MICROSOMAL AMINOPEPTIDASE; PROTEINASE INHIBITOR; PYRROLIDINE DERIVATIVE;

EID: 77956576575     PISSN: 13895575     EISSN: None     Source Type: Journal    
DOI: 10.2174/138955710791608334     Document Type: Article
Times cited : (38)

References (87)
  • 1
    • 33947216271 scopus 로고    scopus 로고
    • Can matrix metalloproteinase inhibitors provide a realistic therapy in cardiovascular medicine?
    • MacFadyen, R.J. Can matrix metalloproteinase inhibitors provide a realistic therapy in cardiovascular medicine? Curr. Opin. Pharmacol., 2007, 7, 171-178.
    • (2007) Curr. Opin. Pharmacol , vol.7 , pp. 171-178
    • Macfadyen, R.J.1
  • 2
    • 52949084668 scopus 로고    scopus 로고
    • Progress in matrix metalloproteinase research
    • Murphy, G.; Nagase, H. Progress in matrix metalloproteinase research. Mol. Aspects Med., 2008, 29, 290-308.
    • (2008) Mol. Aspects Med , vol.29 , pp. 290-308
    • Murphy, G.1    Nagase, H.2
  • 3
    • 0034472617 scopus 로고    scopus 로고
    • Matrix metalloproteinases in tumor invasion and metastasis
    • Stamenkovic, I. Matrix metalloproteinases in tumor invasion and metastasis. Semin. Cancer Biol., 2000, 10, 415-433.
    • (2000) Semin. Cancer Biol , vol.10 , pp. 415-433
    • Stamenkovic, I.1
  • 4
    • 2342637653 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibitors
    • Ramnath, N.; Creaven, P.J. Matrix metalloproteinase inhibitors. Curr. Oncol. Rep., 2004, 6, 96-102.
    • (2004) Curr. Oncol. Rep , vol.6 , pp. 96-102
    • Ramnath, N.1    Creaven, P.J.2
  • 5
    • 74949125629 scopus 로고    scopus 로고
    • Assessment of aprotinin influence on periodontal clinical status and matrix metalloproteinases 1, 2 and their tissue inhibitors saliva concentrations in patients with chronic periodontitis
    • Pietruska, M.; Pietruski, J.; Skurska, A.; Bernaczyk, A.; Zak, J.; Zelazowska, B.; Doli, E.; Paniczko-Drezek, A.; Wysocka, J. Assessment of aprotinin influence on periodontal clinical status and matrix metalloproteinases 1, 2 and their tissue inhibitors saliva concentrations in patients with chronic periodontitis. Adv. Med. Sci., 2009, 54, 239-246.
    • (2009) Adv. Med. Sci , vol.54 , pp. 239-246
    • Pietruska, M.1    Pietruski, J.2    Skurska, A.3    Bernaczyk, A.4    Zak, J.5    Zelazowska, B.6    Doli, E.7    Paniczko-Drezek, A.8    Wysocka, J.9
  • 7
    • 70449732763 scopus 로고    scopus 로고
    • Matrix metalloproteinase (MMP)-9, but not MMP-2, is involved in the development and progression of C protein-induced myocarditis and subsequent dilated cardiomyopathy
    • Matsumoto, Y.; Park, I.K.; Kohyama, K. Matrix metalloproteinase (MMP)-9, but not MMP-2, is involved in the development and progression of C protein-induced myocarditis and subsequent dilated cardiomyopathy. J. Immunol., 2009, 183, 4773-4781.
    • (2009) J. Immunol , vol.183 , pp. 4773-4781
    • Matsumoto, Y.1    Park, I.K.2    Kohyama, K.3
  • 8
    • 34447520043 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibitors as therapy for inflammatory and vascular diseases
    • Hu, J.; Van den Steen, P.E.; Sang, Q.X.; Opdenakker, G. Matrix metalloproteinase inhibitors as therapy for inflammatory and vascular diseases. Nat. Rev. Drug Discov., 2007, 6, 480-498.
    • (2007) Nat. Rev. Drug Discov , vol.6 , pp. 480-498
    • Hu, J.1    van den Steen, P.E.2    Sang, Q.X.3    Opdenakker, G.4
  • 9
    • 33646136687 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibitors as prospective agents for the prevention and treatment of cardiovascular and neoplastic diseases
    • Sang, Q.X.; Jin, Y.; Newcomer, R.G.; Monroe, S.C.; Fang, X.; Hurst, D.R.; Lee, S.; Cao, Q.; Schwartz, M.A. Matrix metalloproteinase inhibitors as prospective agents for the prevention and treatment of cardiovascular and neoplastic diseases. Curr. Top Med. Chem., 2006, 6, 289-316.
    • (2006) Curr. Top Med. Chem , vol.6 , pp. 289-316
    • Sang, Q.X.1    Jin, Y.2    Newcomer, R.G.3    Monroe, S.C.4    Fang, X.5    Hurst, D.R.6    Lee, S.7    Cao, Q.8    Schwartz, M.A.9
  • 11
    • 34547617698 scopus 로고    scopus 로고
    • Targeting matrix metalloproteinases and endothelial cells with a fusion peptide against tumor
    • Zou, Y.; Chen, Y.; Jiang, Y.; Gao, J.; Gu, J. Targeting matrix metalloproteinases and endothelial cells with a fusion peptide against tumor. Cancer Res., 2007, 67, 7295-7300.
    • (2007) Cancer Res , vol.67 , pp. 7295-7300
    • Zou, Y.1    Chen, Y.2    Jiang, Y.3    Gao, J.4    Gu, J.5
  • 12
    • 0001651169 scopus 로고    scopus 로고
    • Design and therapeutic application of matrix metalloproteinase inhibitors
    • Whittaker, M.; Floyd, C.D.; Brown, P.; Gearing, A.J. Design and therapeutic application of matrix metalloproteinase inhibitors. Chem. Rev., 1999, 99, 2735-2776.
    • (1999) Chem. Rev , vol.99 , pp. 2735-2776
    • Whittaker, M.1    Floyd, C.D.2    Brown, P.3    Gearing, A.J.4
  • 13
    • 34447269445 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibitors: New challenges in the era of post broad-spectrum inhibitors
    • Nuti, E.; Tuccinardi, T.; Rossello, A. Matrix metalloproteinase inhibitors: New challenges in the era of post broad-spectrum inhibitors. Curr. Pharm. Des., 2007, 13, 2087-2100.
    • (2007) Curr. Pharm. Des , vol.13 , pp. 2087-2100
    • Nuti, E.1    Tuccinardi, T.2    Rossello, A.3
  • 15
    • 33644545381 scopus 로고    scopus 로고
    • Tumour microenvironment-opinion: Validating matrix metalloproteinases as drug targets and antitargets for cancer therapy
    • Overall, C.M.; Kleifeld, O. Tumour microenvironment-opinion: Validating matrix metalloproteinases as drug targets and antitargets for cancer therapy. Nat. Rev. Cancer., 2006, 6, 227-239.
    • (2006) Nat. Rev. Cancer , vol.6 , pp. 227-239
    • Overall, C.M.1    Kleifeld, O.2
  • 16
    • 0032439091 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibitors
    • Brown, P.D. Matrix metalloproteinase inhibitors. Breast Cancer Res. Treat., 1998, 52, 125-136.
    • (1998) Breast Cancer Res. Treat , vol.52 , pp. 125-136
    • Brown, P.D.1
  • 18
    • 15244342010 scopus 로고    scopus 로고
    • Matrix metalloproteinases as therapeutic targets in cancer
    • Vihinen, P.; Ala-aho, R.; Kahari, V.M. Matrix metalloproteinases as therapeutic targets in cancer. Curr. Cancer Drug Targets, 2005, 5, 203-220.
    • (2005) Curr. Cancer Drug Targets , vol.5 , pp. 203-220
    • Vihinen, P.1    Ala-Aho, R.2    Kahari, V.M.3
  • 19
    • 33646584823 scopus 로고    scopus 로고
    • Recent advances in MMP inhibitor design
    • Fisher, J.F.; Mobashery, S. Recent advances in MMP inhibitor design. Cancer Metastasis. Rev., 2006, 25, 115-136.
    • (2006) Cancer Metastasis. Rev , vol.25 , pp. 115-136
    • Fisher, J.F.1    Mobashery, S.2
  • 21
    • 21344466344 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibitors as anticancer therapeutics
    • Mannello, F.; Tonti, G.; Papa, S. Matrix metalloproteinase inhibitors as anticancer therapeutics. Curr. Cancer Drug Targets, 2005, 5, 285-298.
    • (2005) Curr. Cancer Drug Targets , vol.5 , pp. 285-298
    • Mannello, F.1    Tonti, G.2    Papa, S.3
  • 22
    • 0037192458 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibitors and cancer: Trials and tribulations
    • Coussens, L.M.; Fingleton, B.; Matrisian, L.M. Matrix metalloproteinase inhibitors and cancer: trials and tribulations. Science, 2002, 295, 2387-2392.
    • (2002) Science , vol.295 , pp. 2387-2392
    • Coussens, L.M.1    Fingleton, B.2    Matrisian, L.M.3
  • 23
    • 0035030734 scopus 로고    scopus 로고
    • The design, structure, and therapeutic application of matrix metalloproteinase inhibitors
    • Skiles, J.W.; Gonnella, N.C.; Jeng, A.Y. The design, structure, and therapeutic application of matrix metalloproteinase inhibitors. Curr. Med. Chem., 2001, 8, 425-474.
    • (2001) Curr. Med. Chem , vol.8 , pp. 425-474
    • Skiles, J.W.1    Gonnella, N.C.2    Jeng, A.Y.3
  • 24
    • 5744249740 scopus 로고    scopus 로고
    • The design, structure, and clinical update of small molecular weight matrix metalloproteinase inhibitors
    • Skiles, J.W.; Gonnella, N.C.; Jeng, A.Y. The design, structure, and clinical update of small molecular weight matrix metalloproteinase inhibitors. Curr. Med. Chem., 2004, 11, 2911-2977.
    • (2004) Curr. Med. Chem , vol.11 , pp. 2911-2977
    • Skiles, J.W.1    Gonnella, N.C.2    Jeng, A.Y.3
  • 26
    • 0035064033 scopus 로고    scopus 로고
    • X-ray structure of a novel matrix metalloproteinase inhibitor complexed to stromelysin
    • Dunten, P.; Kammlott, U.; Crowther, R.; Levin, W.; Foley, L.H.; Wang, P.; Palermo, R. X-ray structure of a novel matrix metalloproteinase inhibitor complexed to stromelysin. Protein Sci., 2001, 10, 923-926.
    • (2001) Protein Sci , vol.10 , pp. 923-926
    • Dunten, P.1    Kammlott, U.2    Crowther, R.3    Levin, W.4    Foley, L.H.5    Wang, P.6    Palermo, R.7
  • 27
    • 0037142342 scopus 로고    scopus 로고
    • Structural differences of matrix metalloproteinases with potential implications for inhibitor selectivity examined by the GRID/CPCA approach
    • Terp, G.E.; Cruciani, G.; Christensen, I.T.; Jørgensen, F.S. Structural differences of matrix metalloproteinases with potential implications for inhibitor selectivity examined by the GRID/CPCA approach. J. Med. Chem., 2002, 45, 2675-2684.
    • (2002) J. Med. Chem , vol.45 , pp. 2675-2684
    • Terp, G.E.1    Cruciani, G.2    Christensen, I.T.3    Jørgensen, F.S.4
  • 28
    • 77149131528 scopus 로고    scopus 로고
    • To bind zinc or not to bind zinc: An examination of innovative approaches to improved metalloproteinase inhibition
    • Jacobsen, J.A.; Major Jourden, J.L.; Miller, M.T.; Cohen, S.M. To bind zinc or not to bind zinc: An examination of innovative approaches to improved metalloproteinase inhibition. Biochim. Biophys. Acta, 2010, 1803(1), 72-94.
    • (2010) Biochim. Biophys. Acta , vol.1803 , Issue.1 , pp. 72-94
    • Jacobsen, J.A.1    Major Jourden, J.L.2    Miller, M.T.3    Cohen, S.M.4
  • 29
    • 52949136266 scopus 로고    scopus 로고
    • Specific targeting of metzincin family members with small-molecule inhibitors: Progress toward a multifarious challenge
    • Georgiadis, D.; Yiotakis, A. Specific targeting of metzincin family members with small-molecule inhibitors: Progress toward a multifarious challenge. Bioorg. Med. Chem., 2008, 16, 8781-8794.
    • (2008) Bioorg. Med. Chem , vol.16 , pp. 8781-8794
    • Georgiadis, D.1    Yiotakis, A.2
  • 30
    • 0033082368 scopus 로고    scopus 로고
    • CD13--not just a marker in leukemia typing
    • Riemann, D.; Kehlen, A.; Langner, J. CD13--not just a marker in leukemia typing. Immunol. Today, 1999, 20, 83-88.
    • (1999) Immunol. Today , vol.20 , pp. 83-88
    • Riemann, D.1    Kehlen, A.2    Langner, J.3
  • 31
    • 0347626098 scopus 로고    scopus 로고
    • Biological significance of aminopeptidase N/CD13 in thyroid carcinomas
    • Kehlen, A.; Lendeckel, U.; Dralle, H.; Langner, J.; Hoang-Vu, C. Biological significance of aminopeptidase N/CD13 in thyroid carcinomas. Cancer Res., 2003, 63, 8500-8506.
    • (2003) Cancer Res , vol.63 , pp. 8500-8506
    • Kehlen, A.1    Lendeckel, U.2    Dralle, H.3    Langner, J.4    Hoang-Vu, C.5
  • 32
    • 38449084605 scopus 로고    scopus 로고
    • DP IV/CD26, APN/CD13 and related enzymes as regulators of T cell immunity: Implications for experimental encephalomyelitis and multiple sclerosis
    • Reinhold, D.; Bank, U.; Täger, M.; Ansorge, S.; Wrenger, S.; Thielitz, A.; Lendeckel, U.; Faust, J.; Neubert, K.; Brocke, S. DP IV/CD26, APN/CD13 and related enzymes as regulators of T cell immunity: implications for experimental encephalomyelitis and multiple sclerosis. Front. Biosci., 2008, 13, 2356-2363.
    • (2008) Front. Biosci , vol.13 , pp. 2356-2363
    • Reinhold, D.1    Bank, U.2    Täger, M.3    Ansorge, S.4    Wrenger, S.5    Thielitz, A.6    Lendeckel, U.7    Faust, J.8    Neubert, K.9    Brocke, S.10
  • 33
    • 37549035458 scopus 로고    scopus 로고
    • Aminopeptidase N (APN)/CD13-dependent CXCR4 downregulation is associated with diminished cell migration, proliferation and invasion
    • Wulfaenger, J.; Niedling, S.; Riemann, D.; Seliger, B. Aminopeptidase N (APN)/CD13-dependent CXCR4 downregulation is associated with diminished cell migration, proliferation and invasion. Mol. Membr. Biol., 2008, 25, 72-82.
    • (2008) Mol. Membr. Biol , vol.25 , pp. 72-82
    • Wulfaenger, J.1    Niedling, S.2    Riemann, D.3    Seliger, B.4
  • 34
    • 0029100416 scopus 로고
    • Human melanoma invasion and metastasis enhancement by high expression of aminopeptidase N/CD13
    • Fujii, H.; Nakajima, M.; Saiki, I.; Yoneda, J.; Azuma, I.; Tsuruo, T. Human melanoma invasion and metastasis enhancement by high expression of aminopeptidase N/CD13. Clin. Exp. Metastasis, 1995, 13, 337-344.
    • (1995) Clin. Exp. Metastasis , vol.13 , pp. 337-344
    • Fujii, H.1    Nakajima, M.2    Saiki, I.3    Yoneda, J.4    Azuma, I.5    Tsuruo, T.6
  • 36
    • 0034659306 scopus 로고    scopus 로고
    • Angiogenesis: New insights and therapeutic potential
    • Tomanek, R.J.; Schatteman, G.C. Angiogenesis: new insights and therapeutic potential. Anat. Rec., 2000, 261, 126-135.
    • (2000) Anat. Rec , vol.261 , pp. 126-135
    • Tomanek, R.J.1    Schatteman, G.C.2
  • 37
    • 33749449024 scopus 로고    scopus 로고
    • Aminopeptidase N (APN/CD13) is selectively expressed in vascular endothelial cells and plays multiple roles in angiogenesis
    • Fukasawa, K.; Fujii, H.; Saitoh, Y.; Koizumi, K.; Aozuka, Y.; Sekine, K.; Yamada, M.; Saiki, I.; Nishikawa, K. Aminopeptidase N (APN/CD13) is selectively expressed in vascular endothelial cells and plays multiple roles in angiogenesis. Cancer Lett., 2006, 243, 135-143.
    • (2006) Cancer Lett , vol.243 , pp. 135-143
    • Fukasawa, K.1    Fujii, H.2    Saitoh, Y.3    Koizumi, K.4    Aozuka, Y.5    Sekine, K.6    Yamada, M.7    Saiki, I.8    Nishikawa, K.9
  • 38
    • 0035254206 scopus 로고    scopus 로고
    • CD13/APN is activated by angiogenic signals and is essential for capillary tube formation
    • Bhagwat, S.V.; Lahdenranta, J.; Giordano, R.; Arap, W.; Pasqualini, R.; Shapiro, L.H. CD13/APN is activated by angiogenic signals and is essential for capillary tube formation. Blood, 2001, 97, 652-659.
    • (2001) Blood , vol.97 , pp. 652-659
    • Bhagwat, S.V.1    Lahdenranta, J.2    Giordano, R.3    Arap, W.4    Pasqualini, R.5    Shapiro, L.H.6
  • 39
    • 0036161112 scopus 로고    scopus 로고
    • Aminopeptidase N is involved in cell motility and angiogenesis: Its clinical significance in human colon cancer
    • Hashida, H.; Takabayashi, A.; Kanai, M.; Adachi, M.; Kondo, K.; Kohno, N.; Yamaoka, Y.; Miyake, M. Aminopeptidase N is involved in cell motility and angiogenesis: its clinical significance in human colon cancer. Gastroenterology, 2002, 122, 376-386.
    • (2002) Gastroenterology , vol.122 , pp. 376-386
    • Hashida, H.1    Takabayashi, A.2    Kanai, M.3    Adachi, M.4    Kondo, K.5    Kohno, N.6    Yamaoka, Y.7    Miyake, M.8
  • 40
    • 48149111676 scopus 로고    scopus 로고
    • The moonlighting enzyme CD13: Old and new functions to target
    • Mina-Osorio, P. The moonlighting enzyme CD13: old and new functions to target. Trends Mol. Med., 2008, 14, 361-371.
    • (2008) Trends Mol. Med , vol.14 , pp. 361-371
    • Mina-Osorio, P.1
  • 41
    • 33845954688 scopus 로고    scopus 로고
    • Crystal structure of aminopeptidase N (proteobacteria alanyl aminopeptidase) from Escherichia coli and conformational change of methionine 260 involved in substrate recognition
    • Ito, K.; Nakajima, Y.; Onohara, Y.; Takeo, M.; Nakashima, K.; Matsubara, F.; Ito, T.; Yoshimoto, T. Crystal structure of aminopeptidase N (proteobacteria alanyl aminopeptidase) from Escherichia coli and conformational change of methionine 260 involved in substrate recognition. J. Biol. Chem., 2006, 281, 33664-33676.
    • (2006) J. Biol. Chem , vol.281 , pp. 33664-33676
    • Ito, K.1    Nakajima, Y.2    Onohara, Y.3    Takeo, M.4    Nakashima, K.5    Matsubara, F.6    Ito, T.7    Yoshimoto, T.8
  • 43
    • 43249098656 scopus 로고    scopus 로고
    • Structural basis for the unusual specificity of Escherichia coli aminopeptidase N
    • Addlagatta, A.; Gay, L.; Matthews, B.W. Structural basis for the unusual specificity of Escherichia coli aminopeptidase N. Biochemistry, 2008, 47, 5303-5311.
    • (2008) Biochemistry , vol.47 , pp. 5303-5311
    • Addlagatta, A.1    Gay, L.2    Matthews, B.W.3
  • 44
    • 33748629692 scopus 로고    scopus 로고
    • Structure of aminopeptidase N from Escherichia coli suggests a compartmentalized, gated active site
    • Addlagatta, A.; Gay, L.; Matthews, B.W. Structure of aminopeptidase N from Escherichia coli suggests a compartmentalized, gated active site. Proc. Natl. Acad. Sci. U S A., 2006, 103, 13339-13344.
    • (2006) Proc. Natl. Acad. Sci. U S A , vol.103 , pp. 13339-13344
    • Addlagatta, A.1    Gay, L.2    Matthews, B.W.3
  • 45
    • 0034719482 scopus 로고    scopus 로고
    • Structure-activity relationships and pharmacokinetic analysis for a series of potent, systemically available biphenylsulfonamide matrix metalloproteinase inhibitors
    • O'Brien, P.M.; Ortwine, D.F.; Pavlovsky, A.G.; Picard, J.A.; Sliskovic, D.R.; Roth, B.D.; Dyer, R.D.; Johnson, L.L.; Man, C.F.; Hallak, H. Structure-activity relationships and pharmacokinetic analysis for a series of potent, systemically available biphenylsulfonamide matrix metalloproteinase inhibitors. J. Med. Chem., 2000, 43, 156-166.
    • (2000) J. Med. Chem , vol.43 , pp. 156-166
    • O'Brien, P.M.1    Ortwine, D.F.2    Pavlovsky, A.G.3    Picard, J.A.4    Sliskovic, D.R.5    Roth, B.D.6    Dyer, R.D.7    Johnson, L.L.8    Man, C.F.9    Hallak, H.10
  • 46
    • 1842828874 scopus 로고    scopus 로고
    • New radioiodinated carboxylic and hydroxamic matrix metalloproteinase inhibitor tracers as potential tumor imaging agents
    • Oltenfreiter, R.; Staelens, L.; Lejeune, A.; Dumont, F.; Frankenne, F.; Foidart, J.M.; Slegers, G. New radioiodinated carboxylic and hydroxamic matrix metalloproteinase inhibitor tracers as potential tumor imaging agents. Nucl. Med. Biol., 2004, 31, 459-468.
    • (2004) Nucl. Med. Biol , vol.31 , pp. 459-468
    • Oltenfreiter, R.1    Staelens, L.2    Lejeune, A.3    Dumont, F.4    Frankenne, F.5    Foidart, J.M.6    Slegers, G.7
  • 48
    • 5444231462 scopus 로고    scopus 로고
    • A ligand-based molecular modeling study on some matrix metalloproteinase-1 inhibitors using several 3D QSAR techniques
    • Tsai, K.C.; Lin, T.H. A ligand-based molecular modeling study on some matrix metalloproteinase-1 inhibitors using several 3D QSAR techniques. J. Chem. Inf. Comput. Sci., 2004, 44, 1857-1871.
    • (2004) J. Chem. Inf. Comput. Sci , vol.44 , pp. 1857-1871
    • Tsai, K.C.1    Lin, T.H.2
  • 50
    • 0037401628 scopus 로고    scopus 로고
    • A quantitative structureactivity relationship study of hydroxamate matrix metalloproteinase inhibitors derived from functionalized 4-aminoprolines
    • Gupta, S.P.; Kumar, D.; Kumaran, S. A quantitative structureactivity relationship study of hydroxamate matrix metalloproteinase inhibitors derived from functionalized 4-aminoprolines. Bioorg. Med. Chem., 2003, 11, 1975-1981.
    • (2003) Bioorg. Med. Chem , vol.11 , pp. 1975-1981
    • Gupta, S.P.1    Kumar, D.2    Kumaran, S.3
  • 52
    • 0038351836 scopus 로고    scopus 로고
    • Protease inhibitors: Synthesis of bacterial collagenase and matrix metalloproteinase inhibitors incorporating succinyl hydroxamate and iminodiacetic acid hydroxamate moieties
    • Santos, M.A.; Marques, S.; Gil, M.; Tegoni, M.; Scozzafava, A.; Supuran, C.T. Protease inhibitors: synthesis of bacterial collagenase and matrix metalloproteinase inhibitors incorporating succinyl hydroxamate and iminodiacetic acid hydroxamate moieties J. Enzyme Inhib. Med. Chem., 2003, 18, 233-242.
    • (2003) J. Enzyme Inhib. Med. Chem , vol.18 , pp. 233-242
    • Santos, M.A.1    Marques, S.2    Gil, M.3    Tegoni, M.4    Scozzafava, A.5    Supuran, C.T.6
  • 54
    • 0035030734 scopus 로고    scopus 로고
    • The design, structure, and therapeutic application of matrix metalloproteinase inhibitors
    • Skiles, J.W.; Gonnella, N.C.; Jeng, A.Y. The design, structure, and therapeutic application of matrix metalloproteinase inhibitors. Curr. Med. Chem., 2001, 8, 425-474.
    • (2001) Curr. Med. Chem , vol.8 , pp. 425-474
    • Skiles, J.W.1    Gonnella, N.C.2    Jeng, A.Y.3
  • 55
    • 33645738383 scopus 로고    scopus 로고
    • Towards third generation matrix metalloproteinase inhibitors for cancer therapy
    • Overall, C.M.; Kleifeld, O. Towards third generation matrix metalloproteinase inhibitors for cancer therapy. Br. J. Cancer, 2006, 94, 941-946.
    • (2006) Br. J. Cancer , vol.94 , pp. 941-946
    • Overall, C.M.1    Kleifeld, O.2
  • 57
    • 33846906016 scopus 로고    scopus 로고
    • Matrix metalloproteinases (MMPs): Chemical-biological functions and (Q)SARs
    • Verma, R.P.; Hansch, C. Matrix metalloproteinases (MMPs): chemical-biological functions and (Q)SARs. Bioorg. Med. Chem., 2007, 15, 2223-2268.
    • (2007) Bioorg. Med. Chem , vol.15 , pp. 2223-2268
    • Verma, R.P.1    Hansch, C.2
  • 58
    • 64349106309 scopus 로고    scopus 로고
    • Extra binding region induced by non-zinc chelating inhibitors into the S1' subsite of matrix metalloproteinase 8 (MMP8)
    • Pochetti, G.; Montanari, R.; Gege, C.; Chevrier, C.; Taveras, A.G.; Mazza, F. Extra binding region induced by non-zinc chelating inhibitors into the S1' subsite of matrix metalloproteinase 8 (MMP8). J. Med. Chem., 2009, 52, 1040-1049.
    • (2009) J. Med. Chem , vol.52 , pp. 1040-1049
    • Pochetti, G.1    Montanari, R.2    Gege, C.3    Chevrier, C.4    Taveras, A.G.5    Mazza, F.6
  • 59
    • 52949113083 scopus 로고    scopus 로고
    • Synthetic active site-directed inhibitors of metzincins: Achievement and perspectives
    • Yiotakis, A.; Dive, V. Synthetic active site-directed inhibitors of metzincins: achievement and perspectives. Mol. Aspects Med., 2008, 29, 329-338.
    • (2008) Mol. Aspects Med , vol.29 , pp. 329-338
    • Yiotakis, A.1    Dive, V.2
  • 63
    • 0035855834 scopus 로고    scopus 로고
    • Design and synthesis of matrix metalloproteinase inhibitors guided by molecular modeling. Picking the S(1) pocket using conformationally constrained inhibitors
    • Hanessian, S.; MacKay, D.B.; Moitessier, N. Design and synthesis of matrix metalloproteinase inhibitors guided by molecular modeling. Picking the S(1) pocket using conformationally constrained inhibitors. J. Med. Chem., 2001, 44, 3074-3082.
    • (2001) J. Med. Chem , vol.44 , pp. 3074-3082
    • Hanessian, S.1    Mackay, D.B.2    Moitessier, N.3
  • 64
    • 33646186011 scopus 로고    scopus 로고
    • Linear and nonlinear QSAR study of N-hydroxy-2-[(phenylsulfonyl)amino] acetamide derivatives as matrix metalloproteinase inhibitors
    • Fernández, M.; Caballero, J.; Tundidor-Camba, A. Linear and nonlinear QSAR study of N-hydroxy-2-[(phenylsulfonyl)amino] acetamide derivatives as matrix metalloproteinase inhibitors. Bioorg. Med. Chem., 2006, 14, 4137-4150.
    • (2006) Bioorg. Med. Chem , vol.14 , pp. 4137-4150
    • Fernández, M.1    Caballero, J.2    Tundidor-Camba, A.3
  • 66
    • 19344366798 scopus 로고    scopus 로고
    • Gelatinase-mediated migration and invasion of cancer cells
    • Björklund, M.; Koivunen, E. Gelatinase-mediated migration and invasion of cancer cells. Biochim. Biophys. Acta, 2005, 1755, 37-69.
    • (2005) Biochim. Biophys. Acta , vol.1755 , pp. 37-69
    • Björklund, M.1    Koivunen, E.2
  • 67
    • 47349084576 scopus 로고    scopus 로고
    • Progress in the development of matrix metalloproteinase inhibitors
    • Tu, G.; Xu, W.; Huang, H.; Li, S. Progress in the development of matrix metalloproteinase inhibitors. Curr. Med. Chem., 2008, 15, 1388-1395.
    • (2008) Curr. Med. Chem , vol.15 , pp. 1388-1395
    • Tu, G.1    Xu, W.2    Huang, H.3    Li, S.4
  • 68
    • 4444264198 scopus 로고    scopus 로고
    • In discussion of the inhibition of angiogenesis and its mechanism in
    • Science Publishing Company. Beijing
    • Feng, X.; Danqing, S.; Yongsu, Z. In discussion of the inhibition of angiogenesis and its mechanism in Progress of Anti-neoplasmdrugs and Chemotherapy. Science Publishing Company. Beijing, 2001; Vol. 10, p. 243.
    • (2001) Progress of Anti-neoplasmdrugs and Chemotherapy , vol.10 , pp. 243
    • Feng, X.1    Danqing, S.2    Yongsu, Z.3
  • 69
    • 4444250592 scopus 로고    scopus 로고
    • Design, synthesis, and activity of caffeoyl pyrrolidine derivatives as potential gelatinase inhibitors
    • Li, Y.L.; Xu, W.F. Design, synthesis, and activity of caffeoyl pyrrolidine derivatives as potential gelatinase inhibitors. Bioorg. Med. Chem., 2004, 12, 5171-5180.
    • (2004) Bioorg. Med. Chem , vol.12 , pp. 5171-5180
    • Li, Y.L.1    Xu, W.F.2
  • 70
    • 33645008011 scopus 로고    scopus 로고
    • Inhibitory effect of caffeic acid phenethyl ester on the growth of C6 glioma cells in vitro and in vivo
    • Kuo, H.C.; Kuo, W.H.; Lee, Y.J.; Lin, W.L.; Chou, F.P.; Tseng, T.H. Inhibitory effect of caffeic acid phenethyl ester on the growth of C6 glioma cells in vitro and in vivo. Cancer Lett., 2006, 234, 199-208.
    • (2006) Cancer Lett , vol.234 , pp. 199-208
    • Kuo, H.C.1    Kuo, W.H.2    Lee, Y.J.3    Lin, W.L.4    Chou, F.P.5    Tseng, T.H.6
  • 71
    • 11844260060 scopus 로고    scopus 로고
    • Chemistry and biological activities of caffeic acid derivatives from Salvia miltiorrhiza
    • Jiang, R.W.; Lau, K.M.; Hon, P.M.; Mak, T.C.; Woo, K.S.; Fung, K.P. Chemistry and biological activities of caffeic acid derivatives from Salvia miltiorrhiza. Curr. Med. Chem., 2005, 12, 237-246.
    • (2005) Curr. Med. Chem , vol.12 , pp. 237-246
    • Jiang, R.W.1    Lau, K.M.2    Hon, P.M.3    Mak, T.C.4    Woo, K.S.5    Fung, K.P.6
  • 72
    • 33750689843 scopus 로고    scopus 로고
    • Caffeoyl pyrrolidine derivative LY52 inhibits tumor invasion and metastasis via suppression of matrix metalloproteinase activity
    • Qu, X.; Yuan, Y.; Xu, W.; Chen, M.; Cui, S.; Meng, H.; Li, Y.; Makuuchi, M.; Nakata, M.; Tang, W. Caffeoyl pyrrolidine derivative LY52 inhibits tumor invasion and metastasis via suppression of matrix metalloproteinase activity. Anticancer Res., 2006, 26, 3573-3578.
    • (2006) Anticancer Res , vol.26 , pp. 3573-3578
    • Qu, X.1    Yuan, Y.2    Xu, W.3    Chen, M.4    Cui, S.5    Meng, H.6    Li, Y.7    Makuuchi, M.8    Nakata, M.9    Tang, W.10
  • 73
    • 34547734676 scopus 로고    scopus 로고
    • Using caffeoyl pyrrolidine derivative LY52, a potential inhibitor of matrix metalloproteinase-2, to suppress tumor invasion and metastasis
    • Qu, X.J.; Yuan, Y.X.; Tian, Z.G.; Xu, W.F.; Chen, M.H.; Cui, S.X.; Guo, Q.; Gai, R.; Makuuchi, M.; Nakata, M.; Tang, W. Using caffeoyl pyrrolidine derivative LY52, a potential inhibitor of matrix metalloproteinase-2, to suppress tumor invasion and metastasis. Int. J. Mol. Med., 2006, 18, 609-614.
    • (2006) Int. J. Mol. Med , vol.18 , pp. 609-614
    • Qu, X.J.1    Yuan, Y.X.2    Tian, Z.G.3    Xu, W.F.4    Chen, M.H.5    Cui, S.X.6    Guo, Q.7    Gai, R.8    Makuuchi, M.9    Nakata, M.10    Tang, W.11
  • 74
    • 39449129390 scopus 로고    scopus 로고
    • Inhibitory effects of matrix metalloproteinase (MMP) inhibitor LY52 on expression of MMP-2 and MMP-9 and invasive ability of human ovarian carcinoma cell line SKOV3
    • Yuan, Y.X.; Xu, W.F.; Liu, J.; Chen, M.H.; Meng, H.; Qu, X.J. Inhibitory effects of matrix metalloproteinase (MMP) inhibitor LY52 on expression of MMP-2 and MMP-9 and invasive ability of human ovarian carcinoma cell line SKOV3. Ai Zheng, 2006, 25, 663-670.
    • (2006) Ai Zheng , vol.25 , pp. 663-670
    • Yuan, Y.X.1    Xu, W.F.2    Liu, J.3    Chen, M.H.4    Meng, H.5    Qu, X.J.6
  • 75
    • 31044453202 scopus 로고    scopus 로고
    • Design, synthesis, and evaluation of novel galloyl pyrrolidine derivatives as potential anti-tumor agents
    • Li, X.; Li, Y.; Xu, W. Design, synthesis, and evaluation of novel galloyl pyrrolidine derivatives as potential anti-tumor agents. Bioorg. Med. Chem., 2006, 14, 1287-1293.
    • (2006) Bioorg. Med. Chem , vol.14 , pp. 1287-1293
    • Li, X.1    Li, Y.2    Xu, W.3
  • 76
    • 33750506919 scopus 로고    scopus 로고
    • Design, synthesis and preliminary evaluation of new cinnamoyl pyrrolidine derivatives as potent gelatinase inhibitors
    • Zhang, L.; Zhang, J.; Fang, H.; Wang, Q.; Xu, W. Design, synthesis and preliminary evaluation of new cinnamoyl pyrrolidine derivatives as potent gelatinase inhibitors. Bioorg. Med. Chem., 2006, 14, 8286-8294.
    • (2006) Bioorg. Med. Chem , vol.14 , pp. 8286-8294
    • Zhang, L.1    Zhang, J.2    Fang, H.3    Wang, Q.4    Xu, W.5
  • 77
    • 50349090567 scopus 로고    scopus 로고
    • Synthesis of new sulfonyl pyrrolidine derivatives as matrix metalloproteinase inhibitors
    • Cheng, X.C.; Wang, Q.; Fang, H.; Tang, W.; Xu, W.F. Synthesis of new sulfonyl pyrrolidine derivatives as matrix metalloproteinase inhibitors. Bioorg. Med. Chem., 2008, 16, 7932-7938.
    • (2008) Bioorg. Med. Chem , vol.16 , pp. 7932-7938
    • Cheng, X.C.1    Wang, Q.2    Fang, H.3    Tang, W.4    Xu, W.F.5
  • 78
    • 43749091066 scopus 로고    scopus 로고
    • Design, synthesis and evaluation of novel sulfonyl pyrrolidine derivatives as matrix metalloproteinase inhibitors
    • Cheng, X.C.; Wang, Q.; Fang, H.; Tang, W.; Xu, W.F. Design, synthesis and evaluation of novel sulfonyl pyrrolidine derivatives as matrix metalloproteinase inhibitors. Bioorg. Med. Chem., 2008, 16, 5398-5404.
    • (2008) Bioorg. Med. Chem , vol.16 , pp. 5398-5404
    • Cheng, X.C.1    Wang, Q.2    Fang, H.3    Tang, W.4    Xu, W.F.5
  • 79
    • 53149148170 scopus 로고    scopus 로고
    • Design, synthesis and preliminary evaluation of novel pyrrolidine derivatives as matrix metalloproteinase inhibitors
    • Cheng, X.C.; Wang, Q.; Fang, H.; Tang, W.; Xu, W.F. Design, synthesis and preliminary evaluation of novel pyrrolidine derivatives as matrix metalloproteinase inhibitors. Eur. J. Med. Chem., 2008, 43, 2130-2139.
    • (2008) Eur. J. Med. Chem , vol.43 , pp. 2130-2139
    • Cheng, X.C.1    Wang, Q.2    Fang, H.3    Tang, W.4    Xu, W.F.5
  • 80
    • 39449127018 scopus 로고    scopus 로고
    • Role of sulfonamide group in matrix metalloproteinase inhibitors
    • Cheng, X.C.; Wang, Q.; Fang, H.; Xu, W.F. Role of sulfonamide group in matrix metalloproteinase inhibitors. Curr. Med. Chem., 2008, 15, 368-373.
    • (2008) Curr. Med. Chem , vol.15 , pp. 368-373
    • Cheng, X.C.1    Wang, Q.2    Fang, H.3    Xu, W.F.4
  • 82
    • 28144451811 scopus 로고    scopus 로고
    • Combining in Silico tools and NMR data to validate protein-ligand structural models: Application to matrix metalloproteinases
    • Bertini, I.; Fragai, M.; Giachetti, A.; Luchinat, C.; Maletta, M.; Parigi, G.; Yeo, K.J. Combining in Silico tools and NMR data to validate protein-ligand structural models: application to matrix metalloproteinases. J. Med. Chem., 2005, 48, 7544-7559.
    • (2005) J. Med. Chem , vol.48 , pp. 7544-7559
    • Bertini, I.1    Fragai, M.2    Giachetti, A.3    Luchinat, C.4    Maletta, M.5    Parigi, G.6    Yeo, K.J.7
  • 83
    • 0025190250 scopus 로고
    • Probestin, a new inhibitor of aminopeptidase N, produced by Streptomyces azureus MH663-2F6. I. Taxonomy, production, isolation, physico-chemical properties, and biological activities
    • Aoyagi, T.; Yoshida, S.; Nakamura, Y.; Shigihara, Y.; Hamada, M.; Takeuchi, T. Probestin, a new inhibitor of aminopeptidase N, produced by Streptomyces azureus MH663-2F6. I. Taxonomy, production, isolation, physico-chemical properties, and biological activities. J. Antibiot. (Tokyo), 1990, 43, 143-148.
    • (1990) J. Antibiot. (Tokyo) , vol.43 , pp. 143-148
    • Aoyagi, T.1    Yoshida, S.2    Nakamura, Y.3    Shigihara, Y.4    Hamada, M.5    Takeuchi, T.6
  • 84
    • 0030070283 scopus 로고    scopus 로고
    • MR-387A and B, new aminopeptidase N inhibitors, produced by Streptomyces neyagawaensis SL-387
    • Chung, M.C.; Chun, H.K.; Han, K.H.; Lee, H.J.; Lee, C.H.; Kho, Y.H. MR-387A and B, new aminopeptidase N inhibitors, produced by Streptomyces neyagawaensis SL-387. J. Antibiot. (Tokyo), 1996, 49, 99-102.
    • (1996) J. Antibiot. (Tokyo) , vol.49 , pp. 99-102
    • Chung, M.C.1    Chun, H.K.2    Han, K.H.3    Lee, H.J.4    Lee, C.H.5    Kho, Y.H.6
  • 85
    • 0035072854 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibitors: How can we optimize their development?
    • Hidalgo, M.; Eckhardt, S.G. Matrix metalloproteinase inhibitors: how can we optimize their development? Ann. Oncol., 2001, 12, 285-287.
    • (2001) Ann. Oncol , vol.12 , pp. 285-287
    • Hidalgo, M.1    Eckhardt, S.G.2
  • 87
    • 58149384690 scopus 로고    scopus 로고
    • Aminopeptidase N (APN/CD13) as a target for anti-cancer agent design
    • Zhang, X.; Xu, W. Aminopeptidase N (APN/CD13) as a target for anti-cancer agent design. Curr. Med. Chem., 2008, 15, 2850-2865.
    • (2008) Curr. Med. Chem , vol.15 , pp. 2850-2865
    • Zhang, X.1    Xu, W.2    Aminopeptidase, N.3


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