메뉴 건너뛰기




Volumn 41, Issue 16, 1998, Pages 3041-3047

Bis-substituted malonic acid hydroxamate derivatives as inhibitors of human neutrophil collagenase (MMP8)

Author keywords

[No Author keywords available]

Indexed keywords

COLLAGENASE INHIBITOR; HYDROXAMIC ACID DERIVATIVE; MALONIC ACID DERIVATIVE; NEUTROPHIL COLLAGENASE;

EID: 0342699963     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm980112p     Document Type: Article
Times cited : (13)

References (30)
  • 4
    • 0028040070 scopus 로고
    • Structural Implications for the Role of the N-terminus in the "Superactivation" of Collagenases - A Crystallographic Study
    • Reinemer, P.; Grams, F.; Huber, R.; Kleine, T.; Schnierer, S.; Pieper, K.; Tschesche, H.; Bode, W. Structural Implications for the Role of the N-terminus in the "Superactivation" of Collagenases - A Crystallographic Study. FEBS Lett 1994, 338, 227-233.
    • (1994) FEBS Lett. , vol.338 , pp. 227-233
    • Reinemer, P.1    Grams, F.2    Huber, R.3    Kleine, T.4    Schnierer, S.5    Pieper, K.6    Tschesche, H.7    Bode, W.8
  • 5
    • 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
    • (1994) EMBO J. , vol.13 , pp. 1263-1269
    • Bode, W.1    Reinemer, P.2    Huber, R.3    Kleine, T.4    Schnierer, S.5    Tschesche, H.6
  • 8
    • 0028128235 scopus 로고
    • Crystal-Structures of Recombinant 19-kDa Human Fibroblast Collagenase Complexed to Itself
    • Lovejoy, B.; Hassell, A. M.; Luther, A. M.; Weigl, D.; Jordan, S. R. Crystal-Structures of Recombinant 19-kDa Human Fibroblast Collagenase Complexed to Itself. Biochemistry 1994, 33, 8207-8217.
    • (1994) Biochemistry , vol.33 , pp. 8207-8217
    • Lovejoy, B.1    Hassell, A.M.2    Luther, A.M.3    Weigl, D.4    Jordan, S.R.5
  • 9
    • 0028838862 scopus 로고
    • Structure Determination and Analysis of Human Neutrophil Collagenase Complexed with a Hydroxamate Inhibitor
    • Grams, F.; Crimmin, M.; Hinnes, P.; 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, P.3    Huxley, P.4    Pieper, M.5    Tschesche, H.6    Bode, W.7
  • 10
    • 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. D.; Ye, Q. Z.; Johnson, L. L.; Hupe, D. J.; Zuiderweg, E. R. P. 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.D.3    Ye, Q.Z.4    Johnson, L.L.5    Hupe, D.J.6    Zuiderweg, E.R.P.7
  • 11
    • 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
  • 14
    • 0030609810 scopus 로고    scopus 로고
    • 1.8-Å Crystal Structure of the Catalytic Domain of Human Neutrophil Collagenase (Matrix-Metalloproteinase-8) Complexed with a Peptidomimetic Hydroxamate Primed-Side Inhibitor with a Distinct Selectivity Profile
    • Betz, M.; Huxley, P.; Davies, S. J.; Mushtaq, Y.; Pieper, M.; Tschesche, H.; Bode, W.; Gomis-Rüth, F. X. 1.8-Å Crystal Structure of the Catalytic Domain of Human Neutrophil Collagenase (Matrix-Metalloproteinase-8) Complexed with a Peptidomimetic Hydroxamate Primed-Side Inhibitor with a Distinct Selectivity Profile. Eur. J. Biochem 1997, 247, 356-363.
    • (1997) Eur. J. Biochem. , vol.247 , pp. 356-363
    • Betz, M.1    Huxley, P.2    Davies, S.J.3    Mushtaq, Y.4    Pieper, M.5    Tschesche, H.6    Bode, W.7    Gomis-Rüth, F.X.8
  • 15
    • 0028915695 scopus 로고
    • X-ray Structures of Human Neutrophil Collagenase Complexed with Peptide Hydroxamate and Peptide Thiol Inhibitors
    • Grams, F.; Reinemer, P.; Powers, F. 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. Eur. J. Biochem 1995, 228, 830-841.
    • (1995) Eur. J. Biochem. , vol.228 , pp. 830-841
    • Grams, F.1    Reinemer, P.2    Powers, F.C.3    Kleine, T.4    Pieper, M.5    Tschesche, H.6    Huber, R.7    Bode, W.8
  • 16
    • 0017810151 scopus 로고
    • Peptide Hydroxamic Acids as Inhibitors of Thermolysin
    • Nishino, N.; Powers, J. C. Peptide Hydroxamic Acids as Inhibitors of Thermolysin. Biochemistry 1978, 17, 2846-2850.
    • (1978) Biochemistry , vol.17 , pp. 2846-2850
    • Nishino, N.1    Powers, J.C.2
  • 17
    • 0018780188 scopus 로고
    • Design of Potent Reversible Inhibitors for Thermolysin. Peptides Containing Zinc Coordinating Ligands and their Use in Affinity Chromatography
    • Nishino, N.; Powers, J. C. Design of Potent Reversible Inhibitors for Thermolysin. Peptides Containing Zinc Coordinating Ligands and their Use in Affinity Chromatography. Biochemistry 1979, 18, 4340-4347.
    • (1979) Biochemistry , vol.18 , pp. 4340-4347
    • Nishino, N.1    Powers, J.C.2
  • 18
    • 0030475119 scopus 로고    scopus 로고
    • Recent Advances in the Field of Matrix Metalloproteinase Inhibitors
    • Beckett, R. P. Recent Advances in the Field of Matrix Metalloproteinase Inhibitors. Exp. Opin. Ther. Pat 1996, 6, 1305-1315.
    • (1996) Exp. Opin. Ther. Pat. , vol.6 , pp. 1305-1315
    • Beckett, R.P.1
  • 19
    • 0032576767 scopus 로고    scopus 로고
    • Synthesis of Malonic Acid-Based Inhibitors of Human Neutrophil Collagenase (MMP8)
    • Graf von Roedern, E.; Grams, F.; Brandstetter, H.; Moroder, L. Synthesis of Malonic Acid-Based Inhibitors of Human Neutrophil Collagenase (MMP8). J. Med. Chem 1998, 41, 339-345.
    • (1998) J. Med. Chem. , vol.41 , pp. 339-345
    • Graf Von Roedern, E.1    Grams, F.2    Brandstetter, H.3    Moroder, L.4
  • 21
    • 84982456997 scopus 로고
    • Conformational equilibrium in 5,5-disubstituted 1,3-dioxanes
    • Coene, E.; Anteunis, M. Conformational equilibrium in 5,5-disubstituted 1,3-dioxanes. Bull. Soc. Chim. Belg 1970, 79, 25-35.
    • (1970) Bull. Soc. Chim. Belg. , vol.79 , pp. 25-35
    • Coene, E.1    Anteunis, M.2
  • 22
    • 84977697749 scopus 로고
    • Ueber die Benzylmethylmalonsäure
    • Conrad, M.; Bischoff, C. A. Ueber die Benzylmethylmalonsäure. Liebigs Ann. Chem 1880, 204, 177-189.
    • (1880) Liebigs Ann. Chem. , vol.204 , pp. 177-189
    • Conrad, M.1    Bischoff, C.A.2
  • 23
    • 0041159141 scopus 로고
    • The Use of Ethyl Acetamidomalonate in the Synthesis of Amino Acids. The Preparation of dl-Histidine, dl-Phenylalanine and dl-Leucine
    • Albertson, N. F.; Archer, S. The Use of Ethyl Acetamidomalonate in the Synthesis of Amino Acids. The Preparation of dl-Histidine, dl-Phenylalanine and dl-Leucine. J. Am. Chem. Soc 1945, 67, 308-310.
    • (1945) J. Am. Chem. Soc. , vol.67 , pp. 308-310
    • Albertson, N.F.1    Archer, S.2
  • 24
    • 0342347049 scopus 로고
    • The Probable Cause of the Elimination of a Carbethoxyl Group as Ethyl Carbonate by the Action of Sodium Ethoxide
    • Thole, F. B.; Thorpe, J. F. The Probable Cause of the Elimination of a Carbethoxyl Group as Ethyl Carbonate by the Action of Sodium Ethoxide. J. Chem. Soc 1911, 99, 2182-2187.
    • (1911) J. Chem. Soc. , vol.99 , pp. 2182-2187
    • Thole, F.B.1    Thorpe, J.F.2
  • 25
    • 37049154100 scopus 로고
    • The Formation of Cylic Compounds from Derivatives of 2:2′-Ditolyl
    • Kenner, J. The Formation of Cylic Compounds from Derivatives of 2:2′-Ditolyl. J. Chem. Soc 1913, 103, 613-627.
    • (1913) J. Chem. Soc. , vol.103 , pp. 613-627
    • Kenner, J.1
  • 26
    • 0024564708 scopus 로고
    • Comparison of Vertebrate Collagenase and Gelatinase Using a New Fluorogenic Substrate Peptide
    • Stack, M. S.; Gray, R. D. Comparison of Vertebrate Collagenase and Gelatinase Using a New Fluorogenic Substrate Peptide. J. Biol. Chem 1989, 264, 4277-4281.
    • (1989) J. Biol. Chem. , vol.264 , pp. 4277-4281
    • Stack, M.S.1    Gray, R.D.2
  • 28
    • 0027027467 scopus 로고
    • LUDI: Rule-Based Automatic Design of New Substituents for Enzyme Inhibitor Leads
    • Böhm, H. J. LUDI: Rule-Based Automatic Design of New Substituents for Enzyme Inhibitor Leads. J. Comput.-Aided Mol. Des 1992, 6, 593-606.
    • (1992) J. Comput.-Aided Mol. Des. , vol.6 , pp. 593-606
    • Böhm, H.J.1
  • 29
    • 0043143224 scopus 로고
    • A new general synthesis of 2-amino alcohols
    • Berlinguet, L. A new general synthesis of 2-amino alcohols. Can. J. Chem 1954, 32, 31-39.
    • (1954) Can. J. Chem. , vol.32 , pp. 31-39
    • Berlinguet, L.1
  • 30
    • 0002097072 scopus 로고
    • 3:5-Dioxo-1:2-diphenylpyrazolidines. the 4-Hydroxy- And Certain 4-Alkoxy- and 4-Alkylamino-Analogues
    • Hammond, K. M.; Fisher, N.; Morgan, E. N.; Tanner, E. M.; Franklin, C. S. 3:5-Dioxo-1:2-diphenylpyrazolidines. The 4-Hydroxy-and Certain 4-Alkoxy-and 4-Alkylamino-Analogues. J. Chem. Soc 1957, 1062-1067.
    • (1957) J. Chem. Soc. , pp. 1062-1067
    • Hammond, K.M.1    Fisher, N.2    Morgan, E.N.3    Tanner, E.M.4    Franklin, C.S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.