메뉴 건너뛰기




Volumn 7, Issue 4, 2004, Pages 513-535

Recent advances in the design of matrix metalloprotease inhibitors

Author keywords

Inhibitor; Lead optimization; Matrix metalloprotease; Selectivity; Structure based design

Indexed keywords

MATRIX METALLOPROTEINASE; MATRIX METALLOPROTEINASE INHIBITOR;

EID: 4644248792     PISSN: 13676733     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (99)

References (118)
  • 1
    • 0035188727 scopus 로고    scopus 로고
    • How matrix metalloproteinases regulate cell behavior
    • Stemlicht M, Werb Z: How matrix metalloproteinases regulate cell behavior. Annu Rev Cell Dev Biol (2001) 17:463-516.
    • (2001) Annu Rev Cell Dev Biol , vol.17 , pp. 463-516
    • Stemlicht, M.1    Werb, Z.2
  • 2
    • 0025847582 scopus 로고
    • Matrix metalloproteinases and their inhibitors in connective tissue remodeling
    • Woessner JF Jr: Matrix metalloproteinases and their inhibitors in connective tissue remodeling. FASEB J (1991) 5(8)5145-2154.
    • (1991) FASEB J , vol.5 , Issue.8 , pp. 5145-12154
    • Woessner Jr., J.F.1
  • 3
    • 0003472468 scopus 로고    scopus 로고
    • Woessner JF, Nagase H (Eds). Oxford University Press, New York, NY, USA
    • Woessner JF, Nagase H (Eds): Matrix Metalloproteinases and TIMPs. Oxford University Press, New York, NY, USA (2000). A comprehensive overview of MMP structure and function and their inhibitors.
    • (2000) Matrix Metalloproteinases and TIMPs
  • 5
    • 0026903364 scopus 로고
    • The matrix metalloproteinases and their inhibitors
    • Murphy G, Docherty AJ: The matrix metalloproteinases and their inhibitors. Am J Respir Cell Mol Biol (1992) 7(2):120-125.
    • (1992) Am J Respir Cell Mol Biol , vol.7 , Issue.2 , pp. 120-125
    • Murphy, G.1    Docherty, A.J.2
  • 6
    • 0025230509 scopus 로고
    • Metalloproteinases and their inhibitors in matrix remodeling
    • Matrisian LM: Metalloproteinases and their inhibitors in matrix remodeling. Trends Genet (1990) 6(4):121-125.
    • (1990) Trends Genet , vol.6 , Issue.4 , pp. 121-125
    • Matrisian, L.M.1
  • 7
    • 0027450277 scopus 로고
    • Metalloproteinases, tissue inhibitor, and proteoglycan fragments in knee synovial fluid in human osteoarthritis
    • Lohmander LS, Hoermer LA, Lark MW: Metalloproteinases, tissue inhibitor, and proteoglycan fragments in knee synovial fluid in human osteoarthritis. Arthritis Rheum (1993) 36(2):181-189.
    • (1993) Arthritis Rheum , vol.36 , Issue.2 , pp. 181-189
    • Lohmander, L.S.1    Hoermer, L.A.2    Lark, M.W.3
  • 8
    • 0026577352 scopus 로고
    • Proteinases in rheumatoid arthritis
    • Murphy G, Hembry RM: Proteinases in rheumatoid arthritis. J Rheumatol Suppl (1992) 32:61-64.
    • (1992) J Rheumatol Suppl , vol.32 , pp. 61-64
    • Murphy, G.1    Hembry, R.M.2
  • 9
    • 0028895806 scopus 로고
    • Localization of tissue inhibitor of matrix metalloproteinases in Alzheimer's disease and normal brain
    • Peress N, Perillo E, Zucker S: Localization of tissue inhibitor of matrix metalloproteinases in Alzheimer's disease and normal brain. J Neuropathol Exp Neurol (1995) 54(1):16-22.
    • (1995) J Neuropathol Exp Neurol , vol.54 , Issue.1 , pp. 16-22
    • Peress, N.1    Perillo, E.2    Zucker, S.3
  • 10
    • 0035500490 scopus 로고    scopus 로고
    • The many faces of metalloproteases: Cell growth, invasion, angiogenesis and metastasis
    • Chang C. Werb Z: The many faces of metalloproteases: Cell growth, invasion, angiogenesis and metastasis. Trends Cell Biol (2001) 11(11):S37-S43.
    • (2001) Trends Cell Biol , vol.11 , Issue.11
    • Chang, C.1    Werb, Z.2
  • 11
    • 0036136731 scopus 로고    scopus 로고
    • Angioprevention: Angiogenesis is a common and key target for cancer chemopreventive agents
    • Tosetti F, Ferrari N, De Flora S, Albini A: Angioprevention: Angiogenesis is a common and key target for cancer chemopreventive agents. FASEB J (2002) 16(1):2-14.
    • (2002) FASEB J , vol.16 , Issue.1 , pp. 2-14
    • Tosetti, F.1    Ferrari, N.2    De Flora, S.3    Albini, A.4
  • 12
    • 0037192458 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibitors and cancer: Trials and tribulations
    • Coussens LM, Fingleton B, Matrisian LM: Matrix metalloproteinase inhibitors and cancer: Trials and tribulations. Science (2002) 295(5564):2387-2392. A key paper reviewing the results of clinical trials of MMP inhibitors for the treatment of cancer, and providing general lessons for future research into novel inhibitors in this field.
    • (2002) Science , vol.295 , Issue.5564 , pp. 2387-2392
    • Coussens, L.M.1    Fingleton, B.2    Matrisian, L.M.3
  • 13
    • 0001651169 scopus 로고    scopus 로고
    • Design and therapeutic application of matrix metalloproteinase inhibitors
    • Whittaker M, Floyd CD, Brown P, Gearing AJ: Design and therapeutic application of matrix metalloproteinase inhibitors. Chem Rev (1999) 99(9):2735-2776.
    • (1999) Chem Rev , vol.99 , Issue.9 , pp. 2735-2776
    • Whittaker, M.1    Floyd, C.D.2    Brown, P.3    Gearing, A.J.4
  • 14
    • 0032758392 scopus 로고    scopus 로고
    • Recent advances in matrix metalloproteinase inhibitors research
    • Michaelides MR, Curtin ML: Recent advances in matrix metalloproteinase inhibitors research. Curr Pharm Des (1999) 5(10):787-819.
    • (1999) Curr Pharm Des , vol.5 , Issue.10 , pp. 787-819
    • Michaelides, M.R.1    Curtin, M.L.2
  • 15
    • 0035030734 scopus 로고    scopus 로고
    • The design, structure and therapeutic application of matrix metalloproteinase inhibitors
    • Skiles JW, Gonella NC, Jeng AY: The design, structure and therapeutic application of matrix metalloproteinase inhibitors. Curr Med Chem (2001) 8(4):425-474. A comprehensive overview of the structural biology and medicinal chemistry of MMP inhibitors.
    • (2001) Curr Med Chem , vol.8 , Issue.4 , pp. 425-474
    • Skiles, J.W.1    Gonella, N.C.2    Jeng, A.Y.3
  • 16
    • 0142123136 scopus 로고    scopus 로고
    • Design strategies for the identification of MMP-13 and TACE inhibitors
    • Skotnicki JS, DiGrandi MJ, Levin JI: Design strategies for the identification of MMP-13 and TACE inhibitors. Curr Opin Drug Discovery Dev (2003) 6(5):742-759. A comprehensive review of the latest developments in medicinal chemistry for MMP-13 and TACE inhibition.
    • (2003) Curr Opin Drug Discovery Dev , vol.6 , Issue.5 , pp. 742-759
    • Skotnicki, J.S.1    DiGrandi, M.J.2    Levin, J.I.3
  • 17
    • 0000736684 scopus 로고    scopus 로고
    • Matrix metalloproteinases
    • Hooper NM (Ed), Tayor and Francis, London, UK
    • Nagase H: Matrix metalloproteinases. In: Zinc Metalloproteinases in Health and Disease. Hooper NM (Ed), Tayor and Francis, London, UK (1996):153-204.
    • (1996) Zinc Metalloproteinases in Health and Disease , pp. 153-204
    • Nagase, H.1
  • 18
    • 0031041647 scopus 로고    scopus 로고
    • Identification and characterization of a novel human matrix metalloproteinase with unique structural characteristics, chromosomal location, and tissue distribution
    • Pendas AM, Knauper V, Puente XS, Llano E, Mattel MG, Apte S, Murphy G, Lopez-Otin C: Identification and characterization of a novel human matrix metalloproteinase with unique structural characteristics, chromosomal location, and tissue distribution. J Biol Chem (1997) 272(7):4281-4286.
    • (1997) J Biol Chem , vol.272 , Issue.7 , pp. 4281-4286
    • Pendas, A.M.1    Knauper, V.2    Puente, X.S.3    Llano, E.4    Mattel, M.G.5    Apte, S.6    Murphy, G.7    Lopez-Otin, C.8
  • 19
    • 0031656460 scopus 로고    scopus 로고
    • Matrix metalloproteinases: Structures, evolution and diversification
    • Massova I, Kotra LP, Fridman R, Mobashery S: Matrix metalloproteinases: Structures, evolution and diversification. FASEB J(1998) 12(12):1075-1095.
    • (1998) FASEB J , vol.12 , Issue.12 , pp. 1075-1095
    • Massova, I.1    Kotra, L.P.2    Fridman, R.3    Mobashery, S.4
  • 20
    • 0035903506 scopus 로고    scopus 로고
    • Medicinal chemistry: Challenges and opportunities
    • Wess G, Urmann M, Sickenberger B: Medicinal chemistry: Challenges and opportunities. Angew Chem Int Ed (2001) 40(18):3341-3350.
    • (2001) Angew Chem Int Ed , vol.40 , Issue.18 , pp. 3341-3350
    • Wess, G.1    Urmann, M.2    Sickenberger, B.3
  • 22
    • 0036716282 scopus 로고    scopus 로고
    • Strategies for MMP inhibition in cancer: Innovations for the post-trial era
    • Overall CM, López-Otin C: Strategies for MMP inhibition in cancer: Innovations for the post-trial era. Nat Rev Cancer (2002) 2(9):657-672.
    • (2002) Nat Rev Cancer , vol.2 , Issue.9 , pp. 657-672
    • Overall, C.M.1    López-Otin, C.2
  • 24
    • 0038040768 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibitors for cancer therapy: The current situation and future prospects
    • Fingleton B: Matrix metalloproteinase inhibitors for cancer therapy: The current situation and future prospects. Exp Opin Ther Targets (2003) 7(3):385-397.
    • (2003) Exp Opin Ther Targets , vol.7 , Issue.3 , pp. 385-397
    • Fingleton, B.1
  • 25
    • 0000546937 scopus 로고    scopus 로고
    • Matrix metalloproteinases as emerging targets in anticancer therapy: Status and prospects
    • Stemlicht MD, Bergers G: Matrix metalloproteinases as emerging targets in anticancer therapy: Status and prospects. Emerging Ther Targets (2000) 4(5):609-633.
    • (2000) Emerging Ther Targets , vol.4 , Issue.5 , pp. 609-633
    • Stemlicht, M.D.1    Bergers, G.2
  • 26
    • 33748661959 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibitors as therapies for rheumatoid arthritis
    • Tsokos GC (Ed), Humana Press, Totowa, NJ, USA
    • Wollaston SJ, Kalunian KC: Matrix metalloproteinase inhibitors as therapies for rheumatoid arthritis. In: Modern Therapeutics in Rheumatic Diseases. Tsokos GC (Ed), Humana Press, Totowa, NJ, USA (2002):135-145.
    • (2002) Modern Therapeutics in Rheumatic Diseases , pp. 135-145
    • Wollaston, S.J.1    Kalunian, K.C.2
  • 27
    • 0036137433 scopus 로고    scopus 로고
    • The Inhibition of metalloproteinases to treat osteoarthritis: Reality and new perspectives
    • Henrotin Y, Sanchez C, Reginster JY: The Inhibition of metalloproteinases to treat osteoarthritis: Reality and new perspectives. Expert Opin Ther Pat (2002) 12(1):29-43. A significant contribution highlighting the impact of MMP inhibitors on the treatment of OA.
    • (2002) Expert Opin Ther Pat , vol.12 , Issue.1 , pp. 29-43
    • Henrotin, Y.1    Sanchez, C.2    Reginster, J.Y.3
  • 28
    • 1542541984 scopus 로고    scopus 로고
    • Rationale for the use of structure-modifying drugs and agents in the treatment of osteoarthritis
    • Pelletier JP: Rationale for the use of structure-modifying drugs and agents in the treatment of osteoarthritis. Osteoarthritis Cartilage (2003) 12(Suppl A):S63-S68.
    • (2003) Osteoarthritis Cartilage , vol.12
    • Pelletier, J.P.1
  • 29
    • 36148953600 scopus 로고    scopus 로고
    • TNF-α-converting enzyme (TACE) as a therapeutic target
    • Skotnicki JS, Levin JI: TNF-α-converting enzyme (TACE) as a therapeutic target. Ann Rep Med Chem (2003) 38:153-162.
    • (2003) Ann Rep Med Chem , vol.38 , pp. 153-162
    • Skotnicki, J.S.1    Levin, J.I.2
  • 31
    • 0036212773 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibitor development for the treatment of heart failure
    • Peterson JT, Li H: Matrix metalloproteinase inhibitor development for the treatment of heart failure. Drug Dev Res (2002) 55(1):29-44.
    • (2002) Drug Dev Res , vol.55 , Issue.1 , pp. 29-44
    • Peterson, J.T.1    Li, H.2
  • 32
    • 0037261987 scopus 로고    scopus 로고
    • Matrix metalloproteinases: A therapeutic target in cardiovascular disease
    • Sierevogel MJ, Pasterkamp G, de Kleijn DP, Strauss BH: Matrix metalloproteinases: A therapeutic target in cardiovascular disease. Curr Pharm Des (2003) 9(13):1033-1040.
    • (2003) Curr Pharm des , vol.9 , Issue.13 , pp. 1033-1040
    • Sierevogel, M.J.1    Pasterkamp, G.2    De Kleijn, D.P.3    Strauss, B.H.4
  • 34
    • 1042280329 scopus 로고    scopus 로고
    • MMP induction and inhibition in myocardial infarction
    • Lindsey ML: MMP induction and inhibition in myocardial infarction. Heart Failure Rev (2004) 9(1):7-19.
    • (2004) Heart Failure Rev , vol.9 , Issue.1 , pp. 7-19
    • Lindsey, M.L.1
  • 35
    • 0037361991 scopus 로고    scopus 로고
    • The role of matrix metalloproteinases (MMPs) in the pathophysiology of chronic obstructive pulmonary disease (COPD): A therapeutic role for inhibitors of MMPs?
    • Belvisi MG, Bottomley KM: The role of matrix metalloproteinases (MMPs) in the pathophysiology of chronic obstructive pulmonary disease (COPD): A therapeutic role for inhibitors of MMPs? Inflamm Res (2003) 52(3):95-100.
    • (2003) Inflamm Res , vol.52 , Issue.3 , pp. 95-100
    • Belvisi, M.G.1    Bottomley, K.M.2
  • 36
    • 0032951138 scopus 로고    scopus 로고
    • Structural properties of matrix metalloproteinases
    • Bode W, Fernandez-Catalan C, Tschesche H, Grams F, Nagase H, Maskos K: Structural properties of matrix metalloproteinases. Cell Mol Life Sci (1999) 55(4):639-652. A significant contribution highlighting many different aspects of MMP structures and complexes with their respective inhibitors.
    • (1999) Cell Mol Life Sci , vol.55 , Issue.4 , pp. 639-652
    • Bode, W.1    Fernandez-Catalan, C.2    Tschesche, H.3    Grams, F.4    Nagase, H.5    Maskos, K.6
  • 37
    • 0031671630 scopus 로고    scopus 로고
    • Matrix metalloproteases: Variations on the theme
    • Borkakoti N: Matrix metalloproteases: Variations on the theme. Prog Biophys Mol Biol (1998) 70(1):73-94. Highly interesting overview of structural biology aspects for MMP inhibition and comparison with other metalloproteases.
    • (1998) Prog Biophys Mol Biol , vol.70 , Issue.1 , pp. 73-94
    • Borkakoti, N.1
  • 38
    • 0033931053 scopus 로고    scopus 로고
    • Structural studies on matrix metalloproteinases
    • Borkakoti N: Structural studies on matrix metalloproteinases. J Mol Med (2000) 78(5):261-268.
    • (2000) J Mol Med , vol.78 , Issue.5 , pp. 261-268
    • Borkakoti, N.1
  • 39
    • 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(6):1263-1269.
    • (1994) EMBO J , vol.13 , Issue.6 , pp. 1263-1269
    • Bode, W.1    Reinemer, P.2    Huber, R.3    Kleine, T.4    Schnierer, S.5    Tschesche, H.6
  • 43
    • 0032492674 scopus 로고    scopus 로고
    • Structural insight into the binding motifs for the calcium ion and the non-catalytic zinc in matrix metalloproteinases
    • Massova I, Kotra LP, Mobashery S: Structural insight into the binding motifs for the calcium ion and the non-catalytic zinc in matrix metalloproteinases. Bioorg Med Chem Lett (1998) 8(7):853-858.
    • (1998) Bioorg Med Chem Lett , vol.8 , Issue.7 , pp. 853-858
    • Massova, I.1    Kotra, L.P.2    Mobashery, S.3
  • 44
    • 0028128235 scopus 로고
    • Crystal structures of recombinant 19-kDa human fibroblast collagenase complexed to itself
    • Lovejoy B, Hassell AM, Luther MA, Weigl D, Jordan SR: Crystal structures of recombinant 19-kDa human fibroblast collagenase complexed to itself. Biochemistry (1994) 33(27):8207-8217.
    • (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
  • 45
    • 0034646631 scopus 로고    scopus 로고
    • A rationalization of the acidic pH dependence for stromelysin-1 (matrix metalloproteinase-3) catalysis and inhibition
    • Johnson LL, Pavlovsky AG, Johnson AR, Janowicz JA, Man CF, Ortwine DF, Purchase CF 2nd, White AD, Hupe DJ: A rationalization of the acidic pH dependence for stromelysin-1 (matrix metalloproteinase-3) catalysis and inhibition. J Biol Chem (2000) 275(15):11026-11033. Important biochemical insights into the MMP-3 catalytic mechanism.
    • (2000) J Biol Chem , vol.275 , Issue.15 , pp. 11026-11033
    • Johnson, L.L.1    Pavlovsky, A.G.2    Johnson, A.R.3    Janowicz, J.A.4    Man, C.F.5    Ortwine, D.F.6    Purchase II, C.F.7    White, A.D.8    Hupe, D.J.9
  • 46
    • 0035937253 scopus 로고    scopus 로고
    • Crystal structure of the stromelysin-3 (MMP-11) catalytic domain complexed with a phosphinic inhibitor mimicking the transition-state
    • Gall AL, Ruff M, Kannan R, Cuniasse P, Yiotakis A, Dive V, Rio MC, Basset P, Moras D: Crystal structure of the stromelysin-3 (MMP-11) catalytic domain complexed with a phosphinic inhibitor mimicking the transition-state. J Mol Biol (2001) 307(2):577-586.
    • (2001) J Mol Biol , vol.307 , Issue.2 , pp. 577-586
    • Gall, A.L.1    Ruff, M.2    Kannan, R.3    Cuniasse, P.4    Yiotakis, A.5    Dive, V.6    Rio, M.C.7    Basset, P.8    Moras, D.9
  • 47
    • 4544229434 scopus 로고    scopus 로고
    • X-ray structures of binary and ternary enzyme-product-inhibitor complexes of matrix metalloproteinases
    • Bertini I, Calderone V, Fragai M, Luchinat C, Mangani S, Temi B: X-ray structures of binary and ternary enzyme-product-inhibitor complexes of matrix metalloproteinases. Angew Chem (2003) 115(23):2777-2780. The publication of 3D protein structures for mimicking MMP-substrate and product complexes which provides a greater understanding of the prerequisites for product binding.
    • (2003) Angew Chem , vol.115 , Issue.23 , pp. 2777-2780
    • Bertini, I.1    Calderone, V.2    Fragai, M.3    Luchinat, C.4    Mangani, S.5    Temi, B.6
  • 48
    • 0029758751 scopus 로고    scopus 로고
    • Human matrix metalloproteinase specificity studies using collagen sequence-based synthetic peptides
    • Nagase H, Fields GB: Human matrix metalloproteinase specificity studies using collagen sequence-based synthetic peptides. Biopolymers (1996) 40(4):399-416.
    • (1996) Biopolymers , vol.40 , Issue.4 , pp. 399-416
    • Nagase, H.1    Fields, G.B.2
  • 49
    • 0022419375 scopus 로고
    • Aromatic-aromatic interaction: A mechanism of protein structure stabilization
    • Burley SK, Petsko GA: Aromatic-aromatic interaction: A mechanism of protein structure stabilization. Science (1985) 229(4708):23-28.
    • (1985) Science , vol.229 , Issue.4708 , pp. 23-28
    • Burley, S.K.1    Petsko, G.A.2
  • 51
    • 0001731266 scopus 로고    scopus 로고
    • Use of Relibase for retrieving complex three-dimensional interaction patterns including crystallographic packing effects
    • Bergner A, Günther J, Hendlich M, Klebe G, Verdonk M: Use of Relibase for retrieving complex three-dimensional interaction patterns including crystallographic packing effects. Biopolymers (2002) 61(2):99-110.
    • (2002) Biopolymers , vol.61 , Issue.2 , pp. 99-110
    • Bergner, A.1    Günther, J.2    Hendlich, M.3    Klebe, G.4    Verdonk, M.5
  • 53
    • 0033048045 scopus 로고    scopus 로고
    • Crystal structures of MMP-1 and -13 reveal the crystal structural basis for selectivity of collagenase inhibitors
    • Lovejoy B, Welch AR, Carr S, Luong C, Broka C, Hendricks RT, Campbell JA, Walker KA, Martin R, Van Wart H, Browner MF: Crystal structures of MMP-1 and -13 reveal the crystal structural basis for selectivity of collagenase inhibitors. Nat Struct Biol (1999) 6(3):217-221. Important publication demonstrating the impact of X-ray crystal structure analysis on understanding selectivity differences in MMPs.
    • (1999) Nat Struct Biol , vol.6 , Issue.3 , pp. 217-221
    • Lovejoy, B.1    Welch, A.R.2    Carr, S.3    Luong, C.4    Broka, C.5    Hendricks, R.T.6    Campbell, J.A.7    Walker, K.A.8    Martin, R.9    Van Wart, H.10    Browner, M.F.11
  • 54
    • 0029030448 scopus 로고
    • Matrilysin-inhibitor complexes: Common themes among metalloproteases
    • Browner MF, Smith WW, Castelhano AL: Matrilysin-inhibitor complexes: Common themes among metalloproteases. Biochemistry (1995) 34(20):6602-6610.
    • (1995) Biochemistry , vol.34 , Issue.20 , pp. 6602-6610
    • Browner, M.F.1    Smith, W.W.2    Castelhano, A.L.3
  • 55
    • 0031174862 scopus 로고    scopus 로고
    • Assignments, secondary structure and dynamics of the inhibitor-free catalytic fragment of human fibroblast collagenase
    • Moy FJ, Pisano MR, Chanda PK, Urtano C, Killar LM, Sung ML, Powers R: Assignments, secondary structure and dynamics of the inhibitor-free catalytic fragment of human fibroblast collagenase. J Biomol NMR (1997) 10(1):9-19.
    • (1997) J Biomol NMR , vol.10 , Issue.1 , pp. 9-19
    • Moy, F.J.1    Pisano, M.R.2    Chanda, P.K.3    Urtano, C.4    Killar, L.M.5    Sung, M.L.6    Powers, R.7
  • 56
    • 0037202174 scopus 로고    scopus 로고
    • Impact of mobility on structure-based drug design for the MMPs
    • Moy FJ, Chanda PK, Chen J, Cosmi S, Edris W, Levin JI, Rush TS, Wilhelm J, Powers R: Impact of mobility on structure-based drug design for the MMPs. J Am Chem Soc (2002) 124(43):12658-12659. Important contribution to studies into the effect of protein binding site dynamics on inhibitor binding in the MMP family using NMR spectroscopy.
    • (2002) J Am Chem Soc , vol.124 , Issue.43 , pp. 12658-12659
    • Moy, F.J.1    Chanda, P.K.2    Chen, J.3    Cosmi, S.4    Edris, W.5    Levin, J.I.6    Rush, T.S.7    Wilhelm, J.8    Powers, R.9
  • 58
    • 2442706574 scopus 로고    scopus 로고
    • Receptor flexibility in the in silico screening of reagents in the S1' pocket of human collagenase
    • Källblad P, Todorov NP, Willems HM, Alberts IL: Receptor flexibility in the in silico screening of reagents in the S1' pocket of human collagenase. J Med Chem (2004) 47(11):2761-2767.
    • (2004) J Med Chem , vol.47 , Issue.11 , pp. 2761-2767
    • Källblad, P.1    Todorov, N.P.2    Willems, H.M.3    Alberts, I.L.4
  • 59
    • 0033519654 scopus 로고    scopus 로고
    • Quantitative structure-activity relationship of human neutrophil collagenase (MMP-8) inhibitors using comparative molecular field and X-ray structure analysis
    • Matter H, Schwab W, Barbier D, Billen G, Haase B, Neises B, Schudok M, Thorwart W, Brachvogel V, Lönze P, Weithmann KU: Quantitative structure-activity relationship of human neutrophil collagenase (MMP-8) inhibitors using comparative molecular field and X-ray structure analysis. J Med Chem (1999) 42(11):1908-1920. Study demonstrating that appropriate substituents in S1' can compensate for a loss of binding affinity resulting from changes to the zinc-binding group.
    • (1999) J Med Chem , vol.42 , Issue.11 , pp. 1908-1920
    • Matter, H.1    Schwab, W.2    Barbier, D.3    Billen, G.4    Haase, B.5    Neises, B.6    Schudok, M.7    Thorwart, W.8    Brachvogel, V.9    Lönze, P.10    Weithmann, K.U.11
  • 60
    • 0033524009 scopus 로고    scopus 로고
    • Affinity and selectivity of matrix metalloproteinase inhibitors: A chemometrical study from the perspective of ligands and proteins
    • 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(22):4506-4523.
    • (1999) J Med Chem , vol.42 , Issue.22 , pp. 4506-4523
    • Matter, H.1    Schwab, W.2
  • 61
    • 0021871375 scopus 로고
    • A computational procedure for determining energetically favorable binding sites on biologically important macromotecules
    • Goodford PJ: A computational procedure for determining energetically favorable binding sites on biologically important macromotecules. J Med Chem (1985) 28(7):849-857.
    • (1985) J Med Chem , vol.28 , Issue.7 , pp. 849-857
    • Goodford, P.J.1
  • 62
    • 0034645763 scopus 로고    scopus 로고
    • Knowledge-based scoring function to predict protein-ligand interactions
    • Gohlke H, Hendlich M, Klebe G: Knowledge-based scoring function to predict protein-ligand interactions. J Mol Biol (2000) 295(2):337-356.
    • (2000) J Mol Biol , vol.295 , Issue.2 , pp. 337-356
    • Gohlke, H.1    Hendlich, M.2    Klebe, G.3
  • 63
    • 0034632795 scopus 로고    scopus 로고
    • GRID/CPCA: A new computational tool to design selective ligands
    • Kastenholz MA, Pastor M, Cruciani G, Haaksma EE, Fox T: GRID/CPCA: A new computational tool to design selective ligands. J Med Chem (2000) 43(16):3033-3044.
    • (2000) J Med Chem , vol.43 , Issue.16 , pp. 3033-3044
    • Kastenholz, M.A.1    Pastor, M.2    Cruciani, G.3    Haaksma, E.E.4    Fox, T.5
  • 64
    • 0037142342 scopus 로고    scopus 로고
    • Structural differences of matrix metalloproteinases with potential implications for inhibitor selectivity examined by the GRID/CPCA approach
    • Terp GE, Cruciani G, Christensen IT, Jorgensen FS: Structural differences of matrix metalloproteinases with potential implications for inhibitor selectivity examined by the GRID/CPCA approach. J Med Chem (2002) 45(13)5675-2684. Description of a novel approach to finding selectivity differences in the MMP family using a combination of force field-based descriptors and statistical approaches. Several interesting differences within all major MMP subsites are highlighted.
    • (2002) J Med Chem , vol.45 , Issue.13 , pp. 5675-12684
    • Terp, G.E.1    Cruciani, G.2    Christensen, I.T.3    Jorgensen, F.S.4
  • 67
    • 33748639439 scopus 로고    scopus 로고
    • Target family landscapes to match ligand selectivity with binding site topology in chemical biology
    • Ford M, Livingstone D, Dearden J, Van de Waterbeemd H (Eds), Blackwell Publishing. Oxford, UK
    • Matter H, Naumann T, Pirard B: Target family landscapes to match ligand selectivity with binding site topology in chemical biology. In: EuroQSAR2002: Designing Drugs and Crop Protectants: Processes, Problems and Polutions. Ford M, Livingstone D, Dearden J, Van de Waterbeemd H (Eds), Blackwell Publishing. Oxford, UK (2003):183-185.
    • (2003) EuroQSAR2002: Designing Drugs and Crop Protectants: Processes, Problems and Polutions , pp. 183-185
    • Matter, H.1    Naumann, T.2    Pirard, B.3
  • 69
    • 0842289659 scopus 로고    scopus 로고
    • Crystal structure of the catalytic domain of human matrix metalloproteinase 10
    • Bertini I, Calderone V, Fragai M, Luchinat C, Mangani S, Terni B: Crystal structure of the catalytic domain of human matrix metalloproteinase 10. J Mol Biol (2004) 336(3)707-716.
    • (2004) J Mol Biol , vol.336 , Issue.3 , pp. 707-716
    • Bertini, I.1    Calderone, V.2    Fragai, M.3    Luchinat, C.4    Mangani, S.5    Terni, B.6
  • 70
  • 72
    • 0035965125 scopus 로고    scopus 로고
    • Substrate specificity determinants of human macrophage elastase (MMP-12) based on the 1.1 a crystal structure
    • Lang R, Kocourek A, Braun M, Tschesche H, Huber R, Bode W, Maskos K: Substrate specificity determinants of human macrophage elastase (MMP-12) based on the 1.1 A crystal structure. J Mol Biol (2001) 312(4):731-742. High-resolution X-ray structure of an MMP-inhibitor complex at atomic resolution provides unprecedented insights into protein-ligand interactions.
    • (2001) J Mol Biol , vol.312 , Issue.4 , pp. 731-742
    • Lang, R.1    Kocourek, A.2    Braun, M.3    Tschesche, H.4    Huber, R.5    Bode, W.6    Maskos, K.7
  • 73
    • 0035965133 scopus 로고    scopus 로고
    • Crystal structure of human macrophage elastase (MMP-12) in complex with a hydroxamic acid inhibitor
    • Nar H, Werte K, Bauer MM, Dollinger H, Jung B: Crystal structure of human macrophage elastase (MMP-12) In complex with a hydroxamic acid inhibitor. J Mol Biol (2001) 312(4):743-751.
    • (2001) J Mol Biol , vol.312 , Issue.4 , pp. 743-751
    • Nar, H.1    Werte, K.2    Bauer, M.M.3    Dollinger, H.4    Jung, B.5
  • 74
    • 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
    • Fernandez-Catalan C, Bode W, Huber R, Turk D, Calvete JJ, 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(17):5238-5248.
    • (1998) EMBO J , 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
  • 75
    • 0033550047 scopus 로고    scopus 로고
    • Analysis of the binding of hydroxamic acid and carboxylic acid inhibitors to the stromelysin-1 (matrix metalloproteinase-3) catalytic domain by isothermal titration calorimetry
    • Parker MH, Lunney EA, Ortwine DF, Pavlovsky AG, Humblet C, Brouillette CG: Analysis of the binding of hydroxamic acid and carboxylic acid inhibitors to the stromelysin-1 (matrix metalloproteinase-3) catalytic domain by isothermal titration calorimetry. Biochemistry (1999) 38(41):13592-13601. Important paper studying the protein-ligand binding event on a biophysical basis. It illustrates the value of thermodynamic profiles generated by ITC In discovering binding interactions that might be undetected, when relying on binding affinities alone, in structure-based design.
    • (1999) Biochemistry , vol.38 , Issue.41 , pp. 13592-13601
    • Parker, M.H.1    Lunney, E.A.2    Ortwine, D.F.3    Pavlovsky, A.G.4    Humblet, C.5    Brouillette, C.G.6
  • 79
    • 0642337794 scopus 로고    scopus 로고
    • Molecular diversity of hydroxamic acids: Part II. Potential therapeutic applications
    • Lou B, Yang K: Molecular diversity of hydroxamic acids: Part II. Potential therapeutic applications. Mini Rev Med Chem (2003) 3(6):609-620.
    • (2003) Mini Rev Med Chem , vol.3 , Issue.6 , pp. 609-620
    • Lou, B.1    Yang, K.2
  • 83
    • 12444273714 scopus 로고    scopus 로고
    • Synthesis and structure-activity relationship of N-substituted 4-arylsulfonylpiperidine-4-hydroxamic acids as novel, orally active matrix metalloproteinase inhibitors for the treatment of osteoarthritis
    • Aranapakam V, Davis JM, Grosu GT, Baker J, Ellingboe J, Zask A, Levin JI, Sandanayaka VP, Du M, Skotnicki JS, DiJoseph JF et al: Synthesis and structure-activity relationship of N-substituted 4-arylsulfonylpiperidine-4- hydroxamic acids as novel, orally active matrix metalloproteinase inhibitors for the treatment of osteoarthritis. J Med Chem (2003) 46(12):2376-2396. Detailed description of one specific series including all data from chemistry, SAP, X-ray crystallography, biology (from enzyme to cellular systems to animal models including ACL-model) and PK studies.
    • (2003) J Med Chem , vol.46 , Issue.12 , pp. 2376-2396
    • Aranapakam, V.1    Davis, J.M.2    Grosu, G.T.3    Baker, J.4    Ellingboe, J.5    Zask, A.6    Levin, J.I.7    Sandanayaka, V.P.8    Du, M.9    Skotnicki, J.S.10    Dijoseph, J.F.11
  • 84
    • 0037011911 scopus 로고    scopus 로고
    • Phenoxyphenyl sulfone N-formylhydroxylamines (retrohydroxamates) as potent, selective, orally bioavailable matrix metalloproteinase inhibitors
    • Wada CK, Holms JH, Curtin ML, Dai Y, Florjancic AS, Garland RB, Guo Y, Heyman HR, Stacey JR, Steinman DH, Albert DH et al: Phenoxyphenyl sulfone N-formylhydroxylamines (retrohydroxamates) as potent, selective, orally bioavailable matrix metalloproteinase inhibitors. J Med Chem (2002) 45(1):219-232. Detailed description of the chemical lead optimization process. This contribution includes many SAR and PK data.
    • (2002) J Med Chem , vol.45 , Issue.1 , pp. 219-232
    • Wada, C.K.1    Holms, J.H.2    Curtin, M.L.3    Dai, Y.4    Florjancic, A.S.5    Garland, R.B.6    Guo, Y.7    Heyman, H.R.8    Stacey, J.R.9    Steinman, D.H.10    Albert, D.H.11
  • 88
    • 12444272689 scopus 로고    scopus 로고
    • Discovery of N-hydroxy-2-(2-oxo-3-pyrrolidinyl)acetamides as potent and selective inhibitors of tumor necrosis factor-α converting enzyme (TACE)
    • Duan JJ, Lu Z, Xue C-B, He X, Seng JL, Roderick JJ, Wasserman ZR, Liu R-Q, Covington MB, Magolda RL, Newton RC et al: Discovery of N-hydroxy-2-(2-oxo-3-pyrrolidinyl)acetamides as potent and selective inhibitors of tumor necrosis factor-α converting enzyme (TACE). Bioorg Med Chem Lett (2003) 13(12):2035-2040. Description of an interesting MMP inhibitor scaffold and side chain which exhibits high specificity for TACE.
    • (2003) Bioorg Med Chem Lett , vol.13 , Issue.12 , pp. 2035-2040
    • Duan, J.J.1    Lu, Z.2    Xue, C.-B.3    He, X.4    Seng, J.L.5    Roderick, J.J.6    Wasserman, Z.R.7    Liu, R.-Q.8    Covington, M.B.9    Magolda, R.L.10    Newton, R.C.11
  • 89
    • 0037038311 scopus 로고    scopus 로고
    • Discovery of γ-lactam hydroxamic acids as selective inhibitors of tumor necrosis factor-α converting enzyme: Design, synthesis, and structure-activity relationships
    • Duan JJ, Chen L, Wasserman ZR, Lu Z, Liu R-Q, Covington MB, Qian M, Hardman KD, Magolda RL, Newton RC, Christ DD et al: Discovery of γ-lactam hydroxamic acids as selective inhibitors of tumor necrosis factor-α converting enzyme: Design, synthesis, and structure-activity relationships. J Med Chem (2002) 45(23):4954-4957. Review of an interesting series with high specificity for TACE.
    • (2002) J Med Chem , vol.45 , Issue.23 , pp. 4954-4957
    • Duan, J.J.1    Chen, L.2    Wasserman, Z.R.3    Lu, Z.4    Liu, R.-Q.5    Covington, M.B.6    Qian, M.7    Hardman, K.D.8    Magolda, R.L.9    Newton, R.C.10    Christ, D.D.11
  • 93
    • 33645396493 scopus 로고    scopus 로고
    • Phosphonamide-based metalloproteinase inhibitors: A new approach to the development of safer metalloproteinase inhibitors
    • Sawa M: Phosphonamide-based metalloproteinase inhibitors: A new approach to the development of safer metalloproteinase inhibitors. Curr Med Chem: Anti-Inflammatory Anti-Allergy Agents (2003) 2(4):367-378.
    • (2003) Curr Med Chem: Anti-Inflammatory Anti-Allergy Agents , vol.2 , Issue.4 , pp. 367-378
    • Sawa, M.1
  • 94
    • 0037075135 scopus 로고    scopus 로고
    • New type of metalloproteinase inhibitor: Design and synthesis of new phosphonamide-based hydroxamic acids
    • Sawa M, Kiyoi T, Kurokawa K, Kumihara H, Yamamoto M, Miyasaka T, Ito Y, Hirayama R, Inoue T, Kirii Y, Nishiwaki E et al: New type of metalloproteinase inhibitor: Design and synthesis of new phosphonamide-based hydroxamic acids. J Med Chem (2002) 45(4):919-929. Report providing a detailed description of a series of phosphonamides as analogs of sulfonamides, in terms of SAR, chemistry and properties such as biology and NMR data.
    • (2002) J Med Chem , vol.45 , Issue.4 , pp. 919-929
    • Sawa, M.1    Kiyoi, T.2    Kurokawa, K.3    Kumihara, H.4    Yamamoto, M.5    Miyasaka, T.6    Ito, Y.7    Hirayama, R.8    Inoue, T.9    Kirii, Y.10    Nishiwaki, E.11
  • 99
    • 0041842667 scopus 로고    scopus 로고
    • A potent, selective inhibitor of matrix metalloproteinase-3 for the topical treatment of chronic dermal ulcers
    • Fray MJ, Dickinson RP, Huggins JP, Occleston NL: A potent, selective inhibitor of matrix metalloproteinase-3 for the topical treatment of chronic dermal ulcers. J Med Chem (2003) 46(16):3514-3525.
    • (2003) J Med Chem , vol.46 , Issue.16 , pp. 3514-3525
    • Fray, M.J.1    Dickinson, R.P.2    Huggins, J.P.3    Occleston, N.L.4
  • 101
    • 0036082365 scopus 로고    scopus 로고
    • (E)-2(R)-[1(S)-(Hydroxycarbamoyl)-4-prienyl-3-butenyl] -2′-isobutyl-2′-(methanesurfonyl)-4-methylvaterohydrazide (Ro 32-7315), a selective and orally active inhibitor of tumor necrosis factor-α convertase
    • Beck G, Bottomley G, Bradshaw D, Brewster M, Broadhurst M, Devos R, Hill C, Johnson W, Kim H-J, Kirtland S, Kneer J et al: (E)-2(R)-[1(S)- (Hydroxycarbamoyl)-4-prienyl-3-butenyl]-2′-isobutyl-2′- (methanesurfonyl)-4-methylvaterohydrazide (Ro 32-7315), a selective and orally active inhibitor of tumor necrosis factor-α convertase. J Pharmacol Exp Ther (2002) 302(1):390-396.
    • (2002) J Pharmacol Exp Ther , vol.302 , Issue.1 , pp. 390-396
    • Beck, G.1    Bottomley, G.2    Bradshaw, D.3    Brewster, M.4    Broadhurst, M.5    Devos, R.6    Hill, C.7    Johnson, W.8    Kim, H.-J.9    Kirtland, S.10    Kneer, J.11
  • 102
    • 12444335919 scopus 로고    scopus 로고
    • Synthesis and structure-activity relationship of α- sulfonylhydroxamic acids as novel, orally active matrix metalloproteinase inhibitors for the treatment of osteoarthritis
    • Aranapakam V, Grosu GT, Davis JM, Hu B, Ellingboe J, Baker JL, Skotnicki JS, Zask A, DiJoseph JF, Sung A, Sharr MA et al: Synthesis and structure-activity relationship of α-sulfonylhydroxamic acids as novel, orally active matrix metalloproteinase inhibitors for the treatment of osteoarthritis. J Med Chem (2003) 46(12):2361-2375.
    • (2003) J Med Chem , vol.46 , Issue.12 , pp. 2361-2375
    • Aranapakam, V.1    Grosu, G.T.2    Davis, J.M.3    Hu, B.4    Ellingboe, J.5    Baker, J.L.6    Skotnicki, J.S.7    Zask, A.8    Dijoseph, J.F.9    Sung, A.10    Sharr, M.A.11
  • 104
    • 0037156343 scopus 로고    scopus 로고
    • Anthranilate sulfonamide hydroxamate TACE inhibitors. Part 1: Structure-based design of novel acetytenic P1' groups
    • Chen JM, Jin G, Sung A, Levin JI: Anthranilate sulfonamide hydroxamate TACE inhibitors. Part 1: Structure-based design of novel acetytenic P1' groups. Bioorg Med Chem Lett (2002) 12(8):1195-1198.
    • (2002) Bioorg Med Chem Lett , vol.12 , Issue.8 , pp. 1195-1198
    • Chen, J.M.1    Jin, G.2    Sung, A.3    Levin, J.I.4
  • 107
    • 12144287462 scopus 로고    scopus 로고
    • Identification and characterization of 4-[[4-(2-butynyloxy)-phenyl] sulfonyl]-N-hxdroxy-2,2-dimethyl-(3S)-thiomoroholinecarboxamide (TMI-1), a novel dual tumor necrosis factor-α-converting enzyme/matrix metalloprotease inhibitor for the treatment of rheumatoid arthritis
    • Zhang Y, Xu J, Levin J, Hegen M, Li G, Robertshaw H, Brennan F, Cummons T, Clarke D, Vansell N, Nickerson-Nutter C et al: Identification and characterization of 4-[[4-(2-butynyloxy)-phenyl]sulfonyl]-N-hxdroxy-2,2- dimethyl-(3S)-thiomoroholinecarboxamide (TMI-1), a novel dual tumor necrosis factor-α-converting enzyme/matrix metalloprotease inhibitor for the treatment of rheumatoid arthritis. J Pharmacol Exp Ther (2004) 309(1):348-355.
    • (2004) J Pharmacol Exp Ther , vol.309 , Issue.1 , pp. 348-355
    • Zhang, Y.1    Xu, J.2    Levin, J.3    Hegen, M.4    Li, G.5    Robertshaw, H.6    Brennan, F.7    Cummons, T.8    Clarke, D.9    Vansell, N.10    Nickerson-Nutter, C.11
  • 109
    • 0035907237 scopus 로고    scopus 로고
    • The 1.8-Å crystal structure of a matrix metalloproteinase 8-barbiturate inhibitor complex reveals a previously unobserved mechanism for collagenase substrate recognition
    • Brandstetter H, Grams F, Glitz D, Lang A, Huber R, Bode W, Krell HW1 Engh RA: The 1.8-Å crystal structure of a matrix metalloproteinase 8-barbiturate inhibitor complex reveals a previously unobserved mechanism for collagenase substrate recognition. J Biol Chem (2001) 276(20):17405-17412.
    • (2001) J Biol Chem , vol.276 , Issue.20 , pp. 17405-17412
    • Brandstetter, H.1    Grams, F.2    Glitz, D.3    Lang, A.4    Huber, R.5    Bode, W.6    Krell, H.W.7    Engh, R.A.8
  • 113
    • 0032809139 scopus 로고    scopus 로고
    • Isolation and identification of a major metabolite of PNU-107859, an MMP inhibitor from the biliary fluid of rats
    • Kuo MS, Yurek DA, Mizsak SA, Prairie MD, Mattern SJ, DeKoning TF: Isolation and identification of a major metabolite of PNU-107859, an MMP inhibitor from the biliary fluid of rats. J Pham Sci (1999) 88(7):705-708.
    • (1999) J Pham Sci , vol.88 , Issue.7 , pp. 705-708
    • Kuo, M.S.1    Yurek, D.A.2    Mizsak, S.A.3    Prairie, M.D.4    Mattern, S.J.5    DeKoning, T.F.6
  • 114
    • 2542586266 scopus 로고    scopus 로고
    • A molecular basis for the selectivity of thiadiazole urea inhibitors with stromelysin-1 and gelatinase-A from Generalized Born Molecular Dynamics simulations
    • Rizzo RC, Toba S, Kuntz ID: A molecular basis for the selectivity of thiadiazole urea inhibitors with stromelysin-1 and gelatinase-A from Generalized Born Molecular Dynamics simulations. J Med Chem (2004) 47(12):3065-3074.
    • (2004) J Med Chem , vol.47 , Issue.12 , pp. 3065-3074
    • Rizzo, R.C.1    Toba, S.2    Kuntz, I.D.3
  • 115
    • 0035959994 scopus 로고    scopus 로고
    • Structure-based design and synthesis of potent matrix metalloproteinase inhibitors derived from a 6H-1,3,4-thiadiazine scaffold
    • Schroeder J, Henke A, Wenzel H, Brandstetter H, Stammler HG, Stammler A, Pfeiffer WD, Tschesche H: Structure-based design and synthesis of potent matrix metalloproteinase inhibitors derived from a 6H-1,3,4-thiadiazine scaffold. J Med Chem (2001) 44(20):3231-3243.
    • (2001) J Med Chem , vol.44 , Issue.20 , pp. 3231-3243
    • Schroeder, J.1    Henke, A.2    Wenzel, H.3    Brandstetter, H.4    Stammler, H.G.5    Stammler, A.6    Pfeiffer, W.D.7    Tschesche, H.8
  • 116
    • 0037135993 scopus 로고    scopus 로고
    • Design and synthesis of novel inhibitors of gelatinase B
    • Wang X, Choe Y, Craik CS, Ellman JA: Design and synthesis of novel inhibitors of gelatinase B. Bioorg Med Chem Lett (2002) 12(16):2201-2204.
    • (2002) Bioorg Med Chem Lett , vol.12 , Issue.16 , pp. 2201-2204
    • Wang, X.1    Choe, Y.2    Craik, C.S.3    Ellman, J.A.4
  • 117
    • 0038779334 scopus 로고    scopus 로고
    • Examination of novel zinc-binding groups for use in matrix metalloproteinase inhibitors
    • Puerta DT, Cohen SM: Examination of novel zinc-binding groups for use in matrix metalloproteinase inhibitors. Inorg Chem (2003) 42(11):3423-3430.
    • (2003) Inorg Chem , vol.42 , Issue.11 , pp. 3423-3430
    • Puerta, D.T.1    Cohen, S.M.2
  • 118
    • 0042865983 scopus 로고    scopus 로고
    • From model complexes to metalloprotein Inhibition: A synergistic approach to structure-based drug discovery
    • Puerta DT, Schames JR, Henchman RH, McCammon JA, Cohen SM: From model complexes to metalloprotein Inhibition: A synergistic approach to structure-based drug discovery. Angew Chem Int Ed (2003) 42(32):3772-3774.
    • (2003) Angew Chem Int Ed , vol.42 , Issue.32 , pp. 3772-3774
    • Puerta, D.T.1    Schames, J.R.2    Henchman, R.H.3    McCammon, J.A.4    Cohen, S.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.