메뉴 건너뛰기




Volumn 19, Issue 7, 2012, Pages 1036-1064

MMP-2 selectivity in hydroxamate-type inhibitors

Author keywords

Hydroxamate; Molecular modelling; Selective matrix metalloproteinase 2 inhibitors; Synthesis

Indexed keywords

A 070; A 071; A 072; A 076; A 077; A 078; A 079; A 080; A 081; A 083; A 084; A 085; A 086; A 087; A 088; A 089; A 090; ABT 518; ANTINEOPLASTIC AGENT; BATIMASTAT; CGS 27023A; DOXYCYCLINE; GELATINASE A; GELATINASE A INHIBITOR; HYDROXAMIC ACID DERIVATIVE; INCYCLINIDE; MATRIX METALLOPROTEINASE INHIBITOR; RO 323555; SC 44463; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 84858242083     PISSN: 09298673     EISSN: 1875533X     Source Type: Journal    
DOI: 10.2174/092986712799320628     Document Type: Review
Times cited : (29)

References (138)
  • 1
    • 0029766216 scopus 로고    scopus 로고
    • Metalloproteinase inhibitors and the prevention of connective tissue breakdown
    • DOI 10.1016/0163-7258(96)00015-0
    • Cawston, T. E., Metalloproteinase inhibitors and the prevention of connective tissue breakdown. Pharmacol. Ther. 1996, 70, 163-182. (Pubitemid 26259574)
    • (1996) Pharmacology and Therapeutics , vol.70 , Issue.3 , pp. 163-182
    • Cawston, T.E.1
  • 3
    • 0031656460 scopus 로고    scopus 로고
    • Matrix metalloproteinases: Structures, evolution, and diversification
    • Massova, I.; Kotra, L. P.; Fridman, R.; Mobashery, S., Matrix metalloproteinases: structures, evolution, and diversification. FASEB J. 1998, 12, 1075-1095. (Pubitemid 28418938)
    • (1998) FASEB Journal , vol.12 , Issue.12 , pp. 1075-1095
    • Massova, I.1    Kotra, L.P.2    Fridman, R.3    Mobashery, S.4
  • 4
    • 0034075487 scopus 로고    scopus 로고
    • Protease inhibitors: Synthesis of potent bacterial collagenase and matrix metalloproteinase inhibitors incorporating N-4- nitrobenzylsulfonylglycine hydroxamate moieties
    • DOI 10.1021/jm990594k
    • Scozzafava, A.; Supuran, C. T., Protease inhibitors: Synthesis of potent bacterial collagenase and matrix metalloproteinase inhibitors incorporating N-4-nitrobenzylsulfonylglycine hydroxamate moieties. J. Med. Chem. 2000, 43, 1858-1865. (Pubitemid 30305018)
    • (2000) Journal of Medicinal Chemistry , vol.43 , Issue.9 , pp. 1858-1865
    • Scozzafava, A.1    Supuran, C.T.2
  • 5
    • 0001330615 scopus 로고
    • The organization of ground substance and basement membrane and its significance in tissue injury disease and growth
    • incl 457 pl.
    • Gersh, I.; Catchpole, H. R., The organization of ground substance and basement membrane and its significance in tissue injury disease and growth. Am. J. Anat. 1949, 85, 457-521, incl 457 pl.
    • (1949) Am. J. Anat. , vol.85 , pp. 457-521
    • Gersh, I.1    Catchpole, H.R.2
  • 6
    • 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
  • 7
    • 77956756060 scopus 로고    scopus 로고
    • Robertson, D.; Plattner, J., Eds. Academic Press: San Diego
    • Summers, J. B., In Annual Reports in Medicinal Chemistry, Robertson, D.; Plattner, J., Eds. Academic Press: San Diego, 1998; Vol. 33, pp 131-149.
    • (1998) Annual Reports in Medicinal Chemistry , vol.33 , pp. 131-149
    • Summers, J.B.1
  • 8
    • 77950931419 scopus 로고    scopus 로고
    • Matrix metalloproteinases: Regulators of the tumor microenvironment
    • Kessenbrock, K.; Plaks, V.; Werb, Z., Matrix metalloproteinases: regulators of the tumor microenvironment. Cell 2010, 141, 52-67.
    • (2010) Cell , vol.141 , pp. 52-67
    • Kessenbrock, K.1    Plaks, V.2    Werb, Z.3
  • 9
    • 33646175469 scopus 로고    scopus 로고
    • Amber force field implementation, molecular modelling study, synthesis and MMP-1/MMP-2 inhibition profile of (R)and (S)-N-hydroxy-2-(N- isopropoxybiphenyl-4-ylsulfonamido)-3-methylbutanamides
    • Tuccinardi, T.; Martinelli, A.; Nuti, E.; Carelli, P.; Balzano, F.; Uccello- Barretta, G.; Murphy, G.; Rossello, A., Amber force field implementation, molecular modelling study, synthesis and MMP-1/MMP-2 inhibition profile of (R)and (S)-N-hydroxy-2-(N-isopropoxybiphenyl-4-ylsulfonamido)-3- methylbutanamides. Bioorg. Med. Chem. 2006, 14, 4260-4276.
    • (2006) Bioorg. Med. Chem. , vol.14 , pp. 4260-4276
    • Tuccinardi, T.1    Martinelli, A.2    Nuti, E.3    Carelli, P.4    Balzano, F.5    Uccello-Barretta, G.6    Murphy, G.7    Rossello, A.8
  • 10
    • 33846120591 scopus 로고    scopus 로고
    • Matrix metalloproteinases as valid clinical targets
    • DOI 10.2174/138161207779313551
    • Fingleton, B., Matrix Metalloproteinases as Valid Clinical Targets. Curr. Pharm. Des. 2007, 13, 333-346. (Pubitemid 46085282)
    • (2007) Current Pharmaceutical Design , vol.13 , Issue.3 , pp. 333-346
    • Fingleton, B.1
  • 11
    • 15244342010 scopus 로고    scopus 로고
    • Matrix metalloproteinases as therapeutic targets in cancer
    • DOI 10.2174/1568009053765799
    • Vihinen, P.; Ala-aho, R.; Kahari, V.-M., Matrix Metalloproteinases as Therapeutic Targets in Cancer. Curr. Cancer Drug Targets 2005, 5, 203-220. (Pubitemid 40694861)
    • (2005) Current Cancer Drug Targets , vol.5 , Issue.3 , pp. 203-220
    • Vihinen, P.1    Ala-Aho, R.2    Kahari, V.-M.3
  • 12
    • 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
  • 13
    • 77952647070 scopus 로고    scopus 로고
    • Matrix Metalloproteinase Inhibitors: A Critical Appraisal of Design Principles and Proposed Therapeutic Utility
    • Dorman, G.; Cseh, S.; Hajdu, I.; Barna, L.; Konya, D.; Kupai, K.; Kovacs, L.; Ferdinandy, P., Matrix Metalloproteinase Inhibitors: A Critical Appraisal of Design Principles and Proposed Therapeutic Utility. Drugs 2010, 70, 949-964.
    • (2010) Drugs , vol.70 , pp. 949-964
    • Dorman, G.1    Cseh, S.2    Hajdu, I.3    Barna, L.4    Konya, D.5    Kupai, K.6    Kovacs, L.7    Ferdinandy, P.8
  • 14
    • 78650424066 scopus 로고    scopus 로고
    • Roles of matrix metalloproteinases in cancer progression and their pharmacological targeting
    • Gialeli, C.; Theocharis, A. D.; Karamanos, N. K., Roles of matrix metalloproteinases in cancer progression and their pharmacological targeting. FEBS J. 2011, 278, 16-27.
    • (2011) FEBS J. , vol.278 , pp. 16-27
    • Gialeli, C.1    Theocharis, A.D.2    Karamanos, N.K.3
  • 16
    • 33746274099 scopus 로고    scopus 로고
    • A high-affinity carbohydrate-containing inhibitor of matrix metalloproteinases
    • DOI 10.1002/cmdc.200600020
    • Calderone, V.; Fragai, M.; Luchinat, C.; Nativi, C.; Richichi, B.; Roelens, S., A High-Affinity Carbohydrate-Containing Inhibitor of Matrix Metalloproteinases. ChemMedChem 2006, 1, 598-601. (Pubitemid 44105785)
    • (2006) ChemMedChem , vol.1 , Issue.6 , pp. 598-601
    • Calderone, V.1    Fragai, M.2    Luchinat, C.3    Nativi, C.4    Richichi, B.5    Roelens, S.6
  • 17
    • 0032612133 scopus 로고    scopus 로고
    • Latest FDA approvals for dentistry
    • Wynn, R. L., Latest FDA approvals for dentistry. Gen. Dent. 1999, 47, 19-22.
    • (1999) Gen. Dent. , vol.47 , pp. 19-22
    • Wynn, R.L.1
  • 18
    • 34447520043 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibitors as therapy for inflammatory and vascular diseases
    • DOI 10.1038/nrd2308, PII NRD2308
    • 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. (Pubitemid 47064570)
    • (2007) Nature Reviews Drug Discovery , vol.6 , Issue.6 , pp. 480-498
    • Hu, J.1    Van Den, S.P.E.2    Sang, Q.-X.A.3    Opdenakker, G.4
  • 19
    • 0036716282 scopus 로고    scopus 로고
    • Strategies for MMP inhibition in cancer: Innovations for the post-trial era
    • DOI 10.1038/nrc884
    • Overall, C. M.; Lopez-Otin, C., Strategies for MMP inhibition in cancer: Innovations for the post-trial era. Nat. Rev. Cancer 2002, 2, 657-672. (Pubitemid 37328917)
    • (2002) Nature Reviews Cancer , vol.2 , Issue.9 , pp. 657-672
    • Overall, C.M.1    Lopez-Otin, C.2
  • 24
    • 0019873814 scopus 로고
    • Partial purification and characterization of a neutral protease which cleaves type IV collagen
    • Liotta, L. A.; Tryggvason, K.; Garbisa, S.; Robey, P. G.; Abe, S., Partial purification and characterization of a neutral protease which cleaves type IV collagen. Biochemistry 1981, 20, 100-104.
    • (1981) Biochemistry , vol.20 , pp. 100-104
    • Liotta, L.A.1    Tryggvason, K.2    Garbisa, S.3    Robey, P.G.4    Abe, S.5
  • 26
    • 0028947020 scopus 로고
    • Matrix Metalloproteinase-2 Is an Interstitial Collagenase
    • Aimes, R. T.; Quigley, J. P., Matrix Metalloproteinase-2 Is an Interstitial Collagenase. J. Biol. Chem. 1995, 270, 5872-5876.
    • (1995) J. Biol. Chem. , vol.270 , pp. 5872-5876
    • Aimes, R.T.1    Quigley, J.P.2
  • 27
    • 34147150065 scopus 로고    scopus 로고
    • Characterization of the Mechanisms by which Gelatinase A, Neutrophil Collagenase, and Membrane-Type Metalloproteinase MMP-14 Recognize Collagen I and Enzymatically Process the Two α-Chains
    • DOI 10.1016/j.jmb.2007.02.076, PII S0022283607002689
    • Gioia, M.; Monaco, S.; Fasciglione, G. F.; Coletti, A.; Modesti, A.; Marini, S.; Coletta, M., Characterization of the Mechanisms by which Gelatinase A, Neutrophil Collagenase, and Membrane-Type Metalloproteinase MMP-14 Recognize Collagen I and Enzymatically Process the Two α-Chains. J. Mol. Biol. 2007, 368, 1101-1113. (Pubitemid 46574666)
    • (2007) Journal of Molecular Biology , vol.368 , Issue.4 , pp. 1101-1113
    • Gioia, M.1    Monaco, S.2    Fasciglione, G.F.3    Coletti, A.4    Modesti, A.5    Marini, S.6    Coletta, M.7
  • 31
    • 0028116127 scopus 로고
    • Hydrolytic inactivation of a breast carcinoma cell-derived serpin by human stromelysin-3
    • Pei, D.; Majmudar, G.; Weiss, S. J., Hydrolytic inactivation of a breast carcinoma cell-derived serpin by human stromelysin-3. J. Biol. Chem. 1994, 269, 25849-25855. (Pubitemid 24336285)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.41 , pp. 25849-25855
    • Pei, D.1    Majmudar, G.2    Weiss, S.J.3
  • 32
    • 2942536116 scopus 로고    scopus 로고
    • Membrane-bound matrix metalloproteinase-8 on activated polymorphonuclear cells is a potent, tissue inhibitor of metalloproteinase-resistant collagenase and serpinase
    • Owen, C. A.; Hu, Z.; Lopez-Otin, C.; Shapiro, S. D., Membrane-bound matrix metalloproteinase-8 on activated polymorphonuclear cells is a potent, tissue inhibitor of metalloproteinase-resistant collagenase and serpinase. J. Immunol. 2004, 172, 7791-7803. (Pubitemid 38747647)
    • (2004) Journal of Immunology , vol.172 , Issue.12 , pp. 7791-7803
    • Owen, C.A.1    Hu, Z.2    Lopez-Otin, C.3    Shapiro, S.D.4
  • 34
    • 0024318368 scopus 로고
    • Pump-1 cDNA codes for a protein with characteristics similar to those of classical collagenase family members
    • Quantin, B.; Murphy, G.; Breathnach, R., Pump-1 cDNA codes for a protein with characteristics similar to those of classical collagenase family members. Biochemistry 1989, 28, 5327-5334. (Pubitemid 19175740)
    • (1989) Biochemistry , vol.28 , Issue.13 , pp. 5327-5334
    • Quantin, B.1    Murphy, G.2    Breathnach, R.3
  • 35
    • 0034617262 scopus 로고    scopus 로고
    • Identification and characterization of human endometase (Matrix metalloproteinase-26) from endometrial tumor
    • Park, H. I.; Ni, J.; Gerkema, F. E.; Liu, D.; Belozerov, V. E.; Sang, Q. X., Identification and characterization of human endometase (Matrix metalloproteinase-26) from endometrial tumor. J. Biol. Chem. 2000, 275, 20540-20544.
    • (2000) J. Biol. Chem. , vol.275 , pp. 20540-20544
    • Park, H.I.1    Ni, J.2    Gerkema, F.E.3    Liu, D.4    Belozerov, V.E.5    Sang, Q.X.6
  • 36
    • 0027515289 scopus 로고
    • Cloning and characterization of a unique elastolytic metalloproteinase produced by human alveolar macrophages
    • Shapiro, S. D.; Kobayashi, D. K.; Ley, T. J., Cloning and characterization of a unique elastolytic metalloproteinase produced by human alveolar macrophages. J. Biol. Chem. 1993, 268, 23824-23829. (Pubitemid 23335353)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.32 , pp. 23824-23829
    • Shapiro, S.D.1    Kobayashi, D.K.2    Ley, T.J.3
  • 37
    • 0030581634 scopus 로고    scopus 로고
    • Macrophage metalloelastase degrades matrix and myelin proteins and processes a tumour necrosis factor-alpha fusion protein
    • DOI 10.1006/bbrc.1996.1677
    • Chandler, S.; Cossins, J.; Lury, J.; Wells, G., Macrophage metalloelastase degrades matrix and myelin proteins and processes a tumour necrosis factor-alpha fusion protein. Biochem. Biophys. Res. Commun. 1996, 228, 421-429. (Pubitemid 26396090)
    • (1996) Biochemical and Biophysical Research Communications , vol.228 , Issue.2 , pp. 421-429
    • Chandler, S.1    Cossins, J.2    Lury, J.3    Wells, G.4
  • 38
    • 0028291737 scopus 로고
    • A matrix metalloproteinase expressed on the surface of invasive tumour cells
    • DOI 10.1038/370061a0
    • Sato, H.; Takino, T.; Okada, Y.; Cao, J.; Shinagawa, A.; Yamamoto, E.; Seiki, M., A matrix metalloproteinase expressed on the surface of invasive tumour cells. Nature 1994, 370, 61-65. (Pubitemid 24216953)
    • (1994) Nature , vol.370 , Issue.6484 , pp. 61-65
    • Sato, H.1    Takino, T.2    Okada, Y.3    Cao, J.4    Shinagawa, A.5    Yamamoto, E.6    Seiki, M.7
  • 39
    • 0029133344 scopus 로고
    • cDNA sequence and mRNA tissue distribution of a novel human matrix metalloproteinase with a potential transmembrane segment
    • Will, H.; Hinzmann, B., cDNA sequence and mRNA tissue distribution of a novel human matrix metalloproteinase with a potential transmembrane segment. Eur. J. Biochem. 1995, 231, 602-608.
    • (1995) Eur. J. Biochem. , vol.231 , pp. 602-608
    • Will, H.1    Hinzmann, B.2
  • 40
    • 0029118269 scopus 로고
    • Identification of the second membrane-type matrix metalloproteinase (MT-MMP-2) gene from a human placenta cDNA library. MT-MMPs form a unique membrane-type subclass in the MMP family
    • Takino, T.; Sato, H.; Shinagawa, A.; Seiki, M., Identification of the second membrane-type matrix metalloproteinase (MT-MMP-2) gene from a human placenta cDNA library. MT-MMPs form a unique membrane-type subclass in the MMP family. J. Biol. Chem. 1995, 270, 23013-23020.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23013-23020
    • Takino, T.1    Sato, H.2    Shinagawa, A.3    Seiki, M.4
  • 41
    • 0030022539 scopus 로고    scopus 로고
    • Molecular cloning of a novel membrane-type matrix metalloproteinase from a human breast carcinoma
    • Puente, X. S.; Pendas, A. M.; Llano, E.; Velasco, G.; Lopez-Otin, C., Molecular cloning of a novel membrane-type matrix metalloproteinase from a human breast carcinoma. Cancer Res. 1996, 56, 944-949. (Pubitemid 26065382)
    • (1996) Cancer Research , vol.56 , Issue.5 , pp. 944-949
    • Puente, X.S.1    Pendas, A.M.2    Llano, E.3    Velasco, G.4    Lopez-Otin, C.5
  • 42
    • 0033152980 scopus 로고    scopus 로고
    • Identification and characterization of human MT5-MMP, a new membrane- bound activator of progelatinase A overexpressed in brain tumors
    • Llano, E.; Pendas, A. M.; Freije, J. P.; Nakano, A.; Knauper, V.; Murphy, G.; Lopez-Otin, C., Identification and characterization of human MT5-MMP, a new membrane-bound activator of progelatinase a overexpressed in brain tumors. Cancer Res. 1999, 59, 2570-2576. (Pubitemid 29269100)
    • (1999) Cancer Research , vol.59 , Issue.11 , pp. 2570-2576
    • Llano, E.1    Pendas, A.M.2    Freije, J.P.3    Nakano, A.4    Knauper, V.5    Murphy, G.6    Lopez-Otin, C.7
  • 43
    • 0034652623 scopus 로고    scopus 로고
    • Human MT6-matrix metalloproteinase: Identification, progelatinase A activation, and expression in brain tumors
    • Velasco, G.; Cal, S.; Merlos-Suarez, A.; Ferrando, A. A.; Alvarez, S.; Nakano, A.; Arribas, J.; Lopez-Otin, C., Human MT6-matrix metalloproteinase: identification, progelatinase A activation, and expression in brain tumors. Cancer Res. 2000, 60, 877-882. (Pubitemid 30129519)
    • (2000) Cancer Research , vol.60 , Issue.4 , pp. 877-882
    • Velasco, G.1    Cal, S.2    Merlos-Suarez, A.3    Ferrando, A.A.4    Alvarez, S.5    Nakano, A.6    Arribas, J.7    Lopez-Otin, C.8
  • 44
    • 0028907318 scopus 로고
    • Mechanism of cell surface activation of 72-kDa type IV collagenase. Isolation of the activated form of the membrane metalloprotease
    • Strongin, A. Y.; Collier, I.; Bannikov, G.; Marmer, B. L.; Grant, G. A.; Goldberg, G. I., Mechanism of cell surface activation of 72-kDa type IV collagenase. Isolation of the activated form of the membrane metalloprotease. J. Biol. Chem. 1995, 270, 5331-5338.
    • (1995) J. Biol. Chem. , vol.270 , pp. 5331-5338
    • Strongin, A.Y.1    Collier, I.2    Bannikov, G.3    Marmer, B.L.4    Grant, G.A.5    Goldberg, G.I.6
  • 45
    • 0031025218 scopus 로고    scopus 로고
    • Membrane type 1 matrix metalloproteinase digests interstitial collagens and other extracellular matrix macromolecules
    • DOI 10.1074/jbc.272.4.2446
    • Ohuchi, E.; Imai, K.; Fujii, Y.; Sato, H.; Seiki, M.; Okada, Y., Membrane type 1 matrix metalloproteinase digests interstitial collagens and other extracellular matrix macromolecules. J. Biol. Chem. 1997, 272, 2446-2451. (Pubitemid 27058534)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.4 , pp. 2446-2451
    • Ohuchi, E.1    Imai, K.2    Fujii, Y.3    Sato, H.4    Seiki, M.5    Okada, Y.6
  • 46
    • 0042090268 scopus 로고    scopus 로고
    • Cleavage of metastasis suppressor gene product KiSS-1 protein/metastin by matrix metalloproteinases
    • DOI 10.1038/sj.onc.1206542
    • Takino, T.; Koshikawa, N.; Miyamori, H.; Tanaka, M.; Sasaki, T.; Okada, Y.; Seiki, M.; Sato, H., Cleavage of metastasis suppressor gene product KiSS-1 protein/metastin by matrix metalloproteinases. Oncogene 2003, 22, 4617-4626. (Pubitemid 36976435)
    • (2003) Oncogene , vol.22 , Issue.30 , pp. 4617-4626
    • Takino, T.1    Koshikawa, N.2    Miyamori, H.3    Tanaka, M.4    Sasaki, T.5    Okada, Y.6    Seiki, M.7    Sato, H.8
  • 47
    • 0034686076 scopus 로고    scopus 로고
    • Biochemical characterization of the catalytic domain of human matrix metalloproteinase 19. Evidence for a role as a potent basement membrane degrading enzyme
    • Stracke, J. O.; Hutton, M.; Stewart, M.; Pendas, A. M.; Smith, B.; Lopez- Otin, C.; Murphy, G.; Knauper, V., Biochemical characterization of the catalytic domain of human matrix metalloproteinase 19. Evidence for a role as a potent basement membrane degrading enzyme. J. Biol. Chem. 2000, 275, 14809-14816.
    • (2000) J. Biol. Chem. , vol.275 , pp. 14809-14816
    • Stracke, J.O.1    Hutton, M.2    Stewart, M.3    Pendas, A.M.4    Smith, B.5    Lopez-Otin, C.6    Murphy, G.7    Knauper, V.8
  • 48
    • 0038676949 scopus 로고    scopus 로고
    • The structure and regulation of the human and mouse matrix metalloproteinase-21 gene and protein
    • DOI 10.1042/BJ20030174
    • Marchenko, G. N.; Marchenko, N. D.; Strongin, A. Y., The structure and regulation of the human and mouse matrix metalloproteinase-21 gene and protein. Biochem. J. 2003, 372, 503-515. (Pubitemid 36723896)
    • (2003) Biochemical Journal , vol.372 , Issue.2 , pp. 503-515
    • Marchenko, G.N.1    Marchenko, N.D.2    Strongin, A.Y.3
  • 49
    • 17744381545 scopus 로고    scopus 로고
    • Cloning and characterization of a rat ortholog of MMP-23 (matrix metalloproteinase-23), a unique type of membrane-anchored matrix metalloproteinase and conditioned switching of its expression during the ovarian follicular development
    • DOI 10.1210/me.15.5.747
    • Ohnishi, J.; Ohnishi, E.; Jin, M.; Hirano, W.; Nakane, D.; Matsui, H.; Kimura, A.; Sawa, H.; Nakayama, K.; Shibuya, H.; Nagashima, K.;Takahashi, T., Cloning and characterization of a rat ortholog of MMP-23 (matrix metalloproteinase-23), a unique type of membrane-anchored matrix metalloproteinase and conditioned switching of its expression during the ovarian follicular development. Mol. Endocrinol. 2001, 15, 747-764. (Pubitemid 32411314)
    • (2001) Molecular Endocrinology , vol.15 , Issue.5 , pp. 747-764
    • Ohnishi, J.1    Ohnishi, E.2    Jin, M.3    Hirano, W.4    Nakane, D.5    Matsui, H.6    Kimura, A.7    Sawa, H.8    Nakayama, K.9    Shibuya, H.10    Nagashima, K.11    Takahashi, T.12
  • 50
    • 0035971090 scopus 로고    scopus 로고
    • Epilysin, a novel human matrix metalloproteinase (MMP-28) expressed in testis and keratinocytes and in response to injury
    • Lohi, J.; Wilson, C. L.; Roby, J. D.; Parks, W. C., Epilysin, a novel human matrix metalloproteinase (MMP-28) expressed in testis and keratinocytes and in response to injury. J. Biol. Chem. 2001, 276, 10134-10144.
    • (2001) J. Biol. Chem. , vol.276 , pp. 10134-10144
    • Lohi, J.1    Wilson, C.L.2    Roby, J.D.3    Parks, W.C.4
  • 55
    • 0028128235 scopus 로고
    • Crystal structures of recombinant 19-kDa human fibroblast collagenase complexed to itself
    • DOI 10.1021/bi00193a006
    • Lovejoy, B.; Hassell, A. M.; Luther, M. A.; Weigl, D.; Jordan, S. R., Crystal structures of recombinant 19-kDa human fibroblast collagenase complexed to itself. Biochemistry 1994, 33, 8207-8217. (Pubitemid 24241053)
    • (1994) Biochemistry , vol.33 , Issue.27 , pp. 8207-8217
    • Lovejoy, B.1    Hassell, A.M.2    Luther, M.A.3    Weigl, D.4    Jordan, S.R.5
  • 57
    • 0028324076 scopus 로고
    • 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
    • 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. 1994, 13, 1263-1269. (Pubitemid 24090206)
    • (1994) EMBO Journal , vol.13 , Issue.6 , pp. 1263-1269
    • Bode, W.1    Reinemer, P.2    Huber, R.3    Kleine, T.4    Schmierer, S.5    Tschesche, H.6
  • 59
    • 0028838862 scopus 로고
    • Structure determination and analysis of human neutrophil collagenase complexed with a hydroxamate inhibitor
    • Grams, F.; Crimmin, M.; Hinnes, L.; Huxley, P.; Pieper, M.; Tschesche, H.; Bode, W., Structure determination and analysis of human neutrophil collagenase complexed with a hydroxamate inhibitor. Biochemistry 1995, 34, 14012-14020.
    • (1995) Biochemistry , vol.34 , pp. 14012-14020
    • Grams, F.1    Crimmin, M.2    Hinnes, L.3    Huxley, P.4    Pieper, M.5    Tschesche, H.6    Bode, W.7
  • 60
    • 0028915695 scopus 로고
    • X-ray structures of human neutrophil collagenase complexed with peptide hydroxamate and peptide thiol inhibitors. Implications for substrate binding and rational drug design
    • Grams, F.; Reinemer, P.; Powers, J. C.; Kleine, T.; Pieper, M.; Tschesche, H.; Huber, R.; Bode, W., X-ray structures of human neutrophil collagenase complexed with peptide hydroxamate and peptide thiol inhibitors. Implications for substrate binding and rational drug design. Eur. J. Biochem. 1995, 228, 830-841.
    • (1995) Eur. J. Biochem. , vol.228 , pp. 830-841
    • Grams, F.1    Reinemer, P.2    Powers, J.C.3    Kleine, T.4    Pieper, M.5    Tschesche, H.6    Huber, R.7    Bode, W.8
  • 62
    • 0028841016 scopus 로고
    • Solution structure of the catalytic domain of human stromelysin complexed with a hydrophobic inhibitor
    • Van Doren, S. R.; Kurochkin, A. V.; Hu, W.; Ye, Q. Z.; Johnson, L. L.; Hupe, D. J.; Zuiderweg, E. R., Solution structure of the catalytic domain of human stromelysin complexed with a hydrophobic inhibitor. Protein Sci. 1995, 4, 2487-2498.
    • (1995) Protein Sci. , vol.4 , pp. 2487-2498
    • Van Doren, S.R.1    Kurochkin, A.V.2    Hu, W.3    Ye, Q.Z.4    Johnson, L.L.5    Hupe, D.J.6    Zuiderweg, E.R.7
  • 64
    • 0029030448 scopus 로고
    • Matrilysin-inhibitor complexes: Common themes among metalloproteases
    • Browner, M. F.; Smith, W. W.; Castelhano, A. L., Matrilysin-inhibitor complexes: common themes among metalloproteases. Biochemistry 1995, 34, 6602-6610.
    • (1995) Biochemistry , vol.34 , pp. 6602-6610
    • Browner, M.F.1    Smith, W.W.2    Castelhano, A.L.3
  • 66
    • 0032492674 scopus 로고    scopus 로고
    • Structural insight into the binding motifs for the calcium ion and the non-catalytic zinc in matrix metalloproteases
    • DOI 10.1016/S0960-894X(98)00128-0, PII S0960894X98001280
    • Massova, I.; Kotra, L. P.; Mobashery, S., Structural insight into the binding motifs for the calcium ion and the non-catalytic zinc in matrix metalloproteases. Bioorg. Med. Chem. Lett. 1998, 8, 853-858. (Pubitemid 28160053)
    • (1998) Bioorganic and Medicinal Chemistry Letters , vol.8 , Issue.7 , pp. 853-858
    • Massova, I.1    Kotra, L.P.2    Mobashery, S.3
  • 67
    • 0028840254 scopus 로고
    • Interaction of peptide substrates of fibroblast collagenase with divalent cations: Ca2+ binding by substrate as a suggested recognition signal for collagenase action
    • Upadhye, S.; Ananthanarayanan, V. S., Interaction of peptide substrates of fibroblast collagenase with divalent cations: Ca2+ binding by substrate as a suggested recognition signal for collagenase action. Biochem. Biophys. Res. Commun. 1995, 215, 474-482.
    • (1995) Biochem. Biophys. Res. Commun. , vol.215 , pp. 474-482
    • Upadhye, S.1    Ananthanarayanan, V.S.2
  • 68
    • 0033523040 scopus 로고    scopus 로고
    • Structure of human pro-matrix metalloproteinase-2: Activation mechanism revealed
    • DOI 10.1126/science.284.5420.1667
    • Morgunova, E.; Tuuttila, A.; Bergmann, U.; Isupov, M.; Lindqvist, Y.; Schneider, G.; Tryggvason, K., Structure of human pro-matrix metalloproteinase-2: Activation mechanism revealed. Science 1999, 284, 1667-1670. (Pubitemid 29291376)
    • (1999) Science , vol.284 , Issue.5420 , pp. 1667-1670
    • Morgunova, E.1    Tuuttila, A.2    Bergmann, U.3    Isupov, M.4    Lindqvist, Y.5    Schneider, G.6    Tryggvason, K.7
  • 69
    • 0032167522 scopus 로고    scopus 로고
    • Crystal structure of the complex formed by the membrane type 1-matrix metalloproteinase with the tissue inhibitor of metalloproteinases-2, the soluble progelatinase A receptor
    • DOI 10.1093/emboj/17.17.5238
    • Fernandez-Catalan, C.; Bode, W.; Huber, R.; Turk, D.; Calvete, J. J.; Lichte, A.; Tschesche, H.; Maskos, K., Crystal structure of the complex formed by the membrane type 1-matrix metalloproteinase with the tissue inhibitor of metalloproteinases-2, the soluble progelatinase A receptor. EMBO J. 1998, 17, 5238-5248. (Pubitemid 28408489)
    • (1998) EMBO Journal , vol.17 , Issue.17 , pp. 5238-5248
    • Fernandez-Catalan, C.1    Bode, W.2    Huber, R.3    Turk, D.4    Calvete, J.J.5    Lichte, A.6    Tschesche, H.7    Maskos, K.8
  • 70
    • 0026455197 scopus 로고
    • Mechanistic studies on the human matrix metalloproteinase stromelysin
    • Harrison, R. K.; Chang, B.; Niedzwiecki, L.; Stein, R. L., Mechanistic studies on the human matrix metalloproteinase stromelysin. Biochemistry 1992, 31, 10757-10762.
    • (1992) Biochemistry , vol.31 , pp. 10757-10762
    • Harrison, R.K.1    Chang, B.2    Niedzwiecki, L.3    Stein, R.L.4
  • 71
    • 50249107450 scopus 로고    scopus 로고
    • Peptide Hydrolysis Catalyzed by Matrix Metalloproteinase 2: A Computational Study
    • Díaz, N.; Suárez, D., Peptide Hydrolysis Catalyzed by Matrix Metalloproteinase 2: A Computational Study. J. Phys. Chem. 2008, 112, 8412-8424.
    • (2008) J. Phys. Chem. , vol.112 , pp. 8412-8424
    • Díaz, N.1    Suárez, D.2
  • 72
    • 0031189711 scopus 로고    scopus 로고
    • Molecular recognition of protein-ligand complexes: Applications to drug design
    • Babine, R. E.; Bender, S. L., Molecular Recognition of Protein-Ligand Complexes: Applications to Drug Design. Chem. Rev. 1997, 97, 1359-1472. (Pubitemid 127659602)
    • (1997) Chemical Reviews , vol.97 , Issue.5 , pp. 1359-1472
    • Babine, R.E.1    Bender, S.L.2
  • 73
    • 77149154385 scopus 로고    scopus 로고
    • Matrix metalloproteinases: Fold and function of their catalytic domains
    • Tallant, C.; Marrero, A.; Gomis-Ruth, F. X., Matrix metalloproteinases: Fold and function of their catalytic domains. Biochim. Biophys. Acta 2010, 1803, 20-28.
    • (2010) Biochim. Biophys. Acta , vol.1803 , pp. 20-28
    • Tallant, C.1    Marrero, A.2    Gomis-Ruth, F.X.3
  • 75
    • 0025738332 scopus 로고
    • Sequence Specificities of Human Fibroblast and Neutrophil Collagenases
    • Netzel-Arnett, S.; Fields, G.; Birkedal-Hansen, H.; E, V. W., Sequence Specificities of Human Fibroblast and Neutrophil Collagenases. J. Biol. Chem. 1991, 266, 6747-6755.
    • (1991) J. Biol. Chem. , vol.266 , pp. 6747-6755
    • Netzel-Arnett, S.1    Fields, G.2    Birkedal-Hansen, H.3    E, V.W.4
  • 76
    • 0033927682 scopus 로고    scopus 로고
    • Structural differences of matrix metalloproteinases. Homology modeling and energy minimization of enzyme-substrate complexes
    • Terp, G. E.; Christensen, I. T.; Jorgensen, F. S., Structural differences of matrix metalloproteinases. Homology modeling and energy minimization of enzyme-substrate complexes. J. Biomol. Struct. Dyn. 2000, 17, 933-946. (Pubitemid 30480359)
    • (2000) Journal of Biomolecular Structure and Dynamics , vol.17 , Issue.6 , pp. 933-946
    • Terp, G.E.1    Christensen, I.T.2    Jorgensen, F.S.3
  • 81
    • 0035855835 scopus 로고    scopus 로고
    • 2' pockets
    • DOI 10.1021/jm010097f
    • Hanessian, S.; Moitessier, N.; Gauchet, C.; Viau, M., N-Aryl sulfonyl homocysteine hydroxamate inhibitors of matrix metalloproteinases: further probing of the S(1), S(1)', and S(2)' pockets. J. Med. Chem. 2001, 44, 3066-3073. (Pubitemid 32862337)
    • (2001) Journal of Medicinal Chemistry , vol.44 , Issue.19 , pp. 3066-3073
    • Hanessian, S.1    Moitessier, N.2    Gauchet, C.3    Viau, M.4
  • 83
    • 0029666453 scopus 로고    scopus 로고
    • 1' pocket mutations in matrilysin and stromelysin-1
    • DOI 10.1021/bi9601969
    • Welch, A. R.; Holman, C. M.; Huber, M.; Brenner, M. C.; Browner, M. F.; Van Wart, H. E., Understanding the P1' specificity of the matrix metalloproteinases: effect of S1' pocket mutations in matrilysin and stromelysin-1. Biochemistry 1996, 35, 10103-10109. (Pubitemid 26269926)
    • (1996) Biochemistry , vol.35 , Issue.31 , pp. 10103-10109
    • Welch, A.R.1    Holman, C.M.2    Huber, M.3    Brenner, M.C.4    Browner, M.F.5    Van Wart, H.E.6
  • 84
    • 0033524009 scopus 로고    scopus 로고
    • Affinity and selectivity of matrix metalloproteinase inhibitors: A chemometrical study from the perspective of ligands and proteins
    • DOI 10.1021/jm990250u
    • Matter, H.; Schwab, W., Affinity and selectivity of matrix metalloproteinase inhibitors: a chemometrical study from the perspective of ligands and proteins. J. Med. Chem. 1999, 42, 4506-4523. (Pubitemid 29530006)
    • (1999) Journal of Medicinal Chemistry , vol.42 , Issue.22 , pp. 4506-4523
    • Matter, H.1    Schwab, W.2
  • 85
    • 0037142342 scopus 로고    scopus 로고
    • Structural differences of matrix metalloproteinases with potential implications for inhibitor selectivity examined by the GRID/CPCA approach
    • DOI 10.1021/jm0109053
    • Terp, G. E.; Cruciani, G.; Christensen, I. T.; Jorgensen, 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. (Pubitemid 34627640)
    • (2002) Journal of Medicinal Chemistry , vol.45 , Issue.13 , pp. 2675-2684
    • Terp, G.E.1    Cruciani, G.2    Christensen, I.T.3    Jorgensen, F.S.4
  • 86
    • 30444435765 scopus 로고    scopus 로고
    • Matrix metalloproteinase target family landscape: A chemometrical approach to ligand selectivity based on protein binding site analysis
    • DOI 10.1021/jm050363f
    • Pirard, B.; Matter, H., Matrix metalloproteinase target family landscape: a chemometrical approach to ligand selectivity based on protein binding site analysis. J. Med. Chem. 2006, 49, 51-69. (Pubitemid 43077322)
    • (2006) Journal of Medicinal Chemistry , vol.49 , Issue.1 , pp. 51-69
    • Pirard, B.1    Matter, H.2
  • 88
    • 0029855561 scopus 로고    scopus 로고
    • Complementarity of combinatorial chemistry and structure-based ligand design: Application to the discovery of novel inhibitors of matrix metalloproteinases
    • DOI 10.1021/ja960897t, PII S0002786396008979
    • Rockwell, A.; Melden, M.; Copeland, R. A.; Hardman, K.; Decicco, C. P.; DeGrado, W. F., Complementarity of Combinatorial Chemistry and Structure-Based Ligand Design: Application to the Discovery of Novel Inhibitors of Matrix Metalloproteinases. J. Am. Chem. Soc. 1996, 118, 10337-10338. (Pubitemid 26375234)
    • (1996) Journal of the American Chemical Society , vol.118 , Issue.42 , pp. 10337-10338
    • Rockwell, A.1    Melden, M.2    Copeland, R.A.3    Hardman, K.4    Decicco, C.P.5    DeGrado, W.F.6
  • 91
    • 37249073324 scopus 로고    scopus 로고
    • Screening of matrix metalloproteinases available from the protein data bank: Insights into biological functions, domain organization, and zinc binding groups
    • Nicolotti, O.; Miscioscia, T. F.; Leonetti, F.; Muncipinto, G.; Carotti, A., Screening of matrix metalloproteinases available from the protein data bank: Insights into biological functions, domain organization, and zinc binding groups. J. Chem. Inf. Model. 2007, 47, 2439-2448.
    • (2007) J. Chem. Inf. Model. , vol.47 , pp. 2439-2448
    • Nicolotti, O.1    Miscioscia, T.F.2    Leonetti, F.3    Muncipinto, G.4    Carotti, A.5
  • 92
    • 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
  • 95
    • 79955698736 scopus 로고    scopus 로고
    • Recent advances in studies on hydroxamates as matrix metalloproteinase inhibitors: A review
    • Yadav, R. K.; Gupta, S. P.; Sharma, P. K.; Patil, V. M., Recent advances in studies on hydroxamates as matrix metalloproteinase inhibitors: a review. Curr. Med. Chem. 2011, 18, 1704-1722.
    • (2011) Curr. Med. Chem. , vol.18 , pp. 1704-1722
    • Yadav, R.K.1    Gupta, S.P.2    Sharma, P.K.3    Patil, V.M.4
  • 96
    • 0023619941 scopus 로고
    • Collagenase inhibitors: Their design and potential therapeutic use
    • Johnson, W. H.; Roberts, N. A.; Borkakoti, N., Collagenase inhibitors: their design and potential therapeutic use. J. Enzym. Inhib. 1987, 2, 1-22. (Pubitemid 17157138)
    • (1987) Journal of Enzyme Inhibition , vol.2 , Issue.1 , pp. 1-22
    • Johnson, W.H.1    Roberts, N.A.2    Borkakoti, N.3
  • 102
    • 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. (Pubitemid 32409788)
    • (2001) Current Medicinal Chemistry , vol.8 , Issue.4 , pp. 425-474
    • Skilest, J.W.1    Gonnella, N.C.2    Jeng, A.Y.3
  • 103
    • 0034719482 scopus 로고    scopus 로고
    • Structure-activity relationships and pharmacokinetic analysis for a series of potent, systemically available biphenylsulfonamide matrix metalloproteinase inhibitors
    • DOI 10.1021/jm9903141
    • 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.; 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. (Pubitemid 30078147)
    • (2000) Journal of Medicinal Chemistry , vol.43 , Issue.2 , 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
  • 104
    • 14044274265 scopus 로고    scopus 로고
    • Recent developments in the design of specific matrix metalloproteinase inhibitors aided by structural and computational studies
    • DOI 10.2174/1381612053382115
    • Rao, B. G., Recent developments in the design of specific Matrix Metalloproteinase inhibitors aided by structural and computational studies. Curr. Pharm. Des. 2005, 11, 295-322. (Pubitemid 40277859)
    • (2005) Current Pharmaceutical Design , vol.11 , Issue.3 , pp. 295-322
    • Rao, B.G.1
  • 106
    • 33845935060 scopus 로고    scopus 로고
    • Molecular modeling of binding between amidinobenzisothiazoles, with antidegenerative activity on cartilage, and matrix metalloproteinase-3
    • DOI 10.1016/j.bmc.2006.11.001, PII S096808960600914X
    • Amadasi, A.; Cozzini, P.; Incerti, M.; Duce, E.; Fisicaro, E.; Vicini, P., Molecular modeling of binding between amidinobenzisothiazoles, with antidegenerative activity on cartilage, and matrix metalloproteinase-3. Bioorg. Med. Chem. 2007, 15, 1420-1429. (Pubitemid 46038127)
    • (2007) Bioorganic and Medicinal Chemistry , vol.15 , Issue.3 , pp. 1420-1429
    • Amadasi, A.1    Cozzini, P.2    Incerti, M.3    Duce, E.4    Fisicaro, E.5    Vicini, P.6
  • 109
    • 0036499078 scopus 로고    scopus 로고
    • Phase II trial of temozolomide plus the matrix metalloproteinase inhibitor, marimastat, in recurrent and progressive glioblastoma multiforme
    • DOI 10.1200/JCO.20.5.1383
    • Groves, M. D.; Puduvalli, V. K.; Hess, K. R.; Jaeckle, K. A.; Peterson, P.; Yung, W. K. A.; Levin, V. A., Phase II trial of temozolomide plus the matrix metalloproteinase inhibitor, marimastat, in recurrent and progressive glioblastoma multiforme. J. Clin. Oncol. 2002, 20, 1383-1388. (Pubitemid 34177446)
    • (2002) Journal of Clinical Oncology , vol.20 , Issue.5 , pp. 1383-1388
    • Groves, M.D.1    Puduvalli, V.K.2    Hess, K.R.3    Jaeckle, K.A.4    Peterson, P.5    Yung, W.K.A.6    Levin, V.A.7
  • 116
    • 0041919643 scopus 로고    scopus 로고
    • Protease inhibitors of the sulfonamide type: Anticancer, antiinflammatory, and antiviral agents
    • DOI 10.1002/med.10047
    • Supuran, C. T.; Casini, A.; Scozzafava, A., Protease inhibitors of the sulfonamide type: anticancer, antiinflammatory, and antiviral agents. Med. Res. Rev. 2003, 23, 535-558. (Pubitemid 37034144)
    • (2003) Medicinal Research Reviews , vol.23 , Issue.5 , pp. 535-558
    • Supuran, C.T.1    Casini, A.2    Scozzafava, A.3
  • 117
    • 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
  • 118
    • 0033587024 scopus 로고    scopus 로고
    • Homology modeling of gelatinase catalytic domains and docking simulations of novel sulfonamide inhibitors
    • DOI 10.1021/jm980514x
    • Kiyama, R.; Tamura, Y.; Watanabe, F.; Tsuzuki, H.; Ohtani, M.; Yodo, M., Homology modeling of gelatinase catalytic domains and docking simulations of novel sulfonamide inhibitors. J. Med. Chem. 1999, 42, 1723-1738. (Pubitemid 29244966)
    • (1999) Journal of Medicinal Chemistry , vol.42 , Issue.10 , pp. 1723-1738
    • Kiyama, R.1    Tamura, Y.2    Watanabe, F.3    Tsuzuki, H.4    Ohtani, M.5    Yodo, M.6
  • 119
    • 0034609778 scopus 로고    scopus 로고
    • Carbonic anhydrase and matrix metalloproteinase inhibitors: Sulfonylated amino acid hydroxamates with MMP inhibitory properties act as efficient inhibitors of CA isozymes I, II, and IV, and N-hydroxysulfonamides inhibit both these zinc enzymes
    • Scozzafava, A.; Supuran, C. T., Carbonic anhydrase and matrix metalloproteinase inhibitors: sulfonylated amino acid hydroxamates with MMP inhibitory properties act as efficient inhibitors of CA isozymes I, II, and IV, and N-hydroxysulfonamides inhibit both these zinc enzymes. J. Med. Chem. 2000, 43, 3677-3687.
    • (2000) J. Med. Chem. , vol.43 , pp. 3677-3687
    • Scozzafava, A.1    Supuran, C.T.2
  • 120
    • 33847003058 scopus 로고    scopus 로고
    • Carbonic anhydrase and matrix metalloproteinase inhibitors. Inhibition of human tumor-associated isozymes IX and cytosolic isozyme I and II with sulfonylated hydroxamates
    • DOI 10.1016/j.bmc.2007.01.023, PII S0968089607000417
    • Nuti, E.; Orlandini, E.; Nencetti, S.; Rossello, A.; Innocenti, A.; Scozzafava, A.; Supuran, C. T., Carbonic anhydrase and matrix metalloproteinase inhibitors. Inhibition of human tumor-associated isozymes IX and cytosolic isozyme I and II with sulfonylated hydroxamates. Bioorg. Med. Chem. 2007, 15, 2298-2311. (Pubitemid 46242198)
    • (2007) Bioorganic and Medicinal Chemistry , vol.15 , Issue.6 , pp. 2298-2311
    • Nuti, E.1    Orlandini, E.2    Nencetti, S.3    Rossello, A.4    Innocenti, A.5    Scozzafava, A.6    Supuran, C.T.7
  • 121
    • 36148960822 scopus 로고    scopus 로고
    • Novel fluorinated derivatives of the broad-spectrum MMP inhibitors N-hydroxy-2(R)-[[(4-methoxyphenyl)sulfonyl](benzyl)- and (3-picolyl)-amino]-3- methyl-butanamide as potential tools for the molecular imaging of activated MMPs with PET
    • DOI 10.1021/jm0708533
    • Wagner, S.; Breyholz, H. J.; Law, M. P.; Faust, A.; Holtke, C.; Schroer, S.; Haufe, G.; Levkau, B.; Schober, O.; Schafers, M.; Kopka, K., Novel fluorinated derivatives of the broad-spectrum MMP inhibitors N-Hydroxy- 2(R)-[[(4-methoxyphenyl)sulfonyl](benzyl)- and (3-picolyl)-amino]-3-methyl- butanamide as potential tools for the molecular Imaging of activated MMPs with PET. J. Med. Chem. 2007, 50, 5752-5764. (Pubitemid 350106030)
    • (2007) Journal of Medicinal Chemistry , vol.50 , Issue.23 , pp. 5752-5764
    • Wagner, S.1    Breyholz, H.-J.2    Law, M.P.3    Faust, A.4    Holtke, C.5    Schroer, S.6    Haufe, G.7    Levkau, B.8    Schober, O.9    Schafers, M.10    Kopka, K.11
  • 129
    • 33749265325 scopus 로고    scopus 로고
    • Design, synthesis and molecular modeling study of iminodiacetyl monohydroxamic acid derivatives as MMP inhibitors
    • DOI 10.1016/j.bmc.2006.07.011, PII S0968089606005669
    • Santos, M. A.; Marques, S. M.; Tuccinardi, T.; Carelli, P.; Panelli, L.; Rossello, A., Design, synthesis and molecular modeling study of iminodiacetyl monohydroxamic acid derivatives as MMP inhibitors. Bioorg. Med. Chem. 2006, 14, 7539-7550. (Pubitemid 44486794)
    • (2006) Bioorganic and Medicinal Chemistry , vol.14 , Issue.22 , pp. 7539-7550
    • Amelia, S.M.1    Marques, S.M.2    Tuccinardi, T.3    Carelli, P.4    Panelli, L.5    Rossello, A.6
  • 130
    • 58149086406 scopus 로고    scopus 로고
    • Dual Inhibitors of Matrix Metalloproteinases and Carbonic Anhydrases: Iminodiacetyl-Based Hydroxamate- Benzenesulfonamide Conjugates
    • Marques, S. M.; Nuti, E.; Rossello, A.; Supura, C. T.; Tuccinardi, T.; Martinelli, A.; Santos, M. A., Dual Inhibitors of Matrix Metalloproteinases and Carbonic Anhydrases: Iminodiacetyl-Based Hydroxamate- Benzenesulfonamide Conjugates. J. Med. Chem. 2008, 51, 7968-7979.
    • (2008) J. Med. Chem. , vol.51 , pp. 7968-7979
    • Marques, S.M.1    Nuti, E.2    Rossello, A.3    Supura, C.T.4    Tuccinardi, T.5    Martinelli, A.6    Santos, M.A.7
  • 132
    • 72449157094 scopus 로고    scopus 로고
    • A combined molecular modeling study on gelatinases and their potent inhibitors
    • Xi, L.; Du, J.; Li, S.; Li, J.; Liu, H.; Yao, X., A combined molecular modeling study on gelatinases and their potent inhibitors. J. Comp. Chem. 2009, 31, 24-42.
    • (2009) J. Comp. Chem. , vol.31 , pp. 24-42
    • Xi, L.1    Du, J.2    Li, S.3    Li, J.4    Liu, H.5    Yao, X.6
  • 133
    • 64349111295 scopus 로고    scopus 로고
    • Does a fast nuclear magnetic resonance spectroscopy- and X-ray crystallography hybrid approach provide reliable structural information of ligand-protein complexes? A case study of metalloproteinases
    • Isaksson, J.; Nystrom, S.; Derbyshire, D.; Wallberg, H.; Agback, T.; Kovacs, H.; Bertini, I.; Giachetti, A.; Luchinat, C., Does a fast nuclear magnetic resonance spectroscopy- and X-ray crystallography hybrid approach provide reliable structural information of ligand-protein complexes? A case study of metalloproteinases. J. Med. Chem. 2009, 52, 1712-1722.
    • (2009) J. Med. Chem. , vol.52 , pp. 1712-1722
    • Isaksson, J.1    Nystrom, S.2    Derbyshire, D.3    Wallberg, H.4    Agback, T.5    Kovacs, H.6    Bertini, I.7    Giachetti, A.8    Luchinat, C.9
  • 134
    • 77949416782 scopus 로고    scopus 로고
    • Kinetic and binding effects in peptide substrate selectivity of matrix metalloproteinase-2: Molecular dynamics and QM/MM calculations
    • Díaz, N.; Suárez, D.; Suárez, E., Kinetic and binding effects in peptide substrate selectivity of matrix metalloproteinase-2: Molecular dynamics and QM/MM calculations. Proteins 2010, 78, 1-11.
    • (2010) Proteins , vol.78 , pp. 1-11
    • Díaz, N.1    Suárez, D.2    Suárez, E.3
  • 135
    • 34547787057 scopus 로고    scopus 로고
    • Molecular dynamics simulations of matrix metalloproteinase 2: Role of the structural metal ions
    • DOI 10.1021/bi700541p
    • Díaz, N.; Suárez, D., Molecular Dynamics Simulations of Matrix Metalloproteinase 2: Role of the Structural Metal Ions. Biochemistry 2007, 46, 8943-8952. (Pubitemid 47237369)
    • (2007) Biochemistry , vol.46 , Issue.31 , pp. 8943-8952
    • Diaz, N.1    Suarez, D.2
  • 136
    • 44949110147 scopus 로고    scopus 로고
    • Molecular dynamics simulations of the active matrix metalloproteinase-2: Positioning of the N-terminal fragment and binding of a small peptide substrate
    • DOI 10.1002/prot.21894
    • Díaz, N.; Suárez, D., Molecular dynamics simulations of the active matrix metalloproteinase-2: Positioning of the N-terminal fragment and binding of a small peptide substrate. Proteins: Structure, Function, and Bioinformatics 2008, 72, 50-61. (Pubitemid 351809147)
    • (2008) Proteins: Structure, Function and Genetics , vol.72 , Issue.1 , pp. 50-61
    • Diaz, N.1    Suarez, D.2
  • 137
    • 33846092077 scopus 로고    scopus 로고
    • Quantum chemical study on the coordination environment of the catalytic zinc ion in matrix metalloproteinases
    • DOI 10.1021/jp0656882
    • Díaz, N.; Suárez, D.; Sordo, T. L., Quantum Chemical Study on the Coordination Environment of the Catalytic Zinc ion in Matrix Metalloproteinases. J. Phys. Chem. B 2006, 110, 24222-24230. (Pubitemid 46065863)
    • (2006) Journal of Physical Chemistry B , vol.110 , Issue.47 , pp. 24222-24230
    • Diaz, N.1    Suarez, D.2    Sordo, T.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.