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Volumn 1, Issue 4, 2010, Pages 145-149

Identification of novel urease inhibitors by high-throughput virtual and in vitro screening

Author keywords

binding free energy calculations; computational docking; high throughput screening; in vitro screening; Urease inhibitors

Indexed keywords

UREASE INHIBITOR;

EID: 77955865448     PISSN: None     EISSN: 19485875     Source Type: Journal    
DOI: 10.1021/ml100068u     Document Type: Article
Times cited : (78)

References (23)
  • 1
    • 0016846997 scopus 로고
    • Letter: Jack bean urease (EC 3.5.1.5). A metalloenzyme. A simple biological role for nickel?
    • Dixon, N. E.; Gazzola, T. C. Letter: Jack bean urease (EC 3.5.1.5). A metalloenzyme. A simple biological role for nickel? J. Am. Chem. Soc. 1975, 97, 4131-4133
    • (1975) J. Am. Chem. Soc. , vol.97 , pp. 4131-4133
    • Dixon, N.E.1    Gazzola, T.C.2
  • 2
    • 0020715539 scopus 로고
    • Jack bean urease: The first nickel enzyme
    • Blakeley, R. L.; Zerner, B. Jack bean urease: The first nickel enzyme J. Mol. Catal. 1984, 23, 263-292
    • (1984) J. Mol. Catal. , vol.23 , pp. 263-292
    • Blakeley, R.L.1    Zerner, B.2
  • 3
    • 0024514293 scopus 로고
    • Microbial ureases: Significance, regulation, and molecular characterization
    • Mobley, H. L.; Hausinger, R. P. Microbial ureases: Significance, regulation, and molecular characterization Microbiol. Mol. Biol. Rev. 1989, 53, 85-108
    • (1989) Microbiol. Mol. Biol. Rev. , vol.53 , pp. 85-108
    • Mobley, H.L.1    Hausinger, R.P.2
  • 4
    • 0028888729 scopus 로고
    • Allium sativum and Allium ursinum part 2: Pharmacology and medicinal application
    • Reuter, H. D.; Reuter, H. D. Allium sativum and Allium ursinum part 2: Pharmacology and medicinal application Phytomedicine 1995, 2, 73-91
    • (1995) Phytomedicine , vol.2 , pp. 73-91
    • Reuter, H.D.1    Reuter, H.D.2
  • 5
    • 0034039960 scopus 로고    scopus 로고
    • Bacterial ureases in infectious diseases
    • Burne, R. A.; Chen, Y. Y. M. Bacterial ureases in infectious diseases Microb. Infect. 2000, 2, 533-542
    • (2000) Microb. Infect. , vol.2 , pp. 533-542
    • Burne, R.A.1    Chen, Y.Y.M.2
  • 7
    • 0033759922 scopus 로고    scopus 로고
    • Production of urease from Helicobacter pylori in transgenic tobacco plants
    • Brodzik, R.; Koprowski, H.; Yusibov, V.; Sirko, A. Production of urease from Helicobacter pylori in transgenic tobacco plants Cell Mol. Biol. Lett. 2000, 5, 357-366
    • (2000) Cell Mol. Biol. Lett. , vol.5 , pp. 357-366
    • Brodzik, R.1    Koprowski, H.2    Yusibov, V.3    Sirko, A.4
  • 8
    • 33747235366 scopus 로고    scopus 로고
    • Quantum mechanical and molecular dynamics simulations of ureases and Zn β-lactamases
    • Estiu, G.; Su'rez, D.; Merz, K. M. Quantum mechanical and molecular dynamics simulations of ureases and Zn β-lactamases J. Comput. Chem. 2006, 27, 1240
    • (2006) J. Comput. Chem. , vol.27 , pp. 1240
    • Estiu, G.1    Su'rez, D.2    Merz, K.M.3
  • 9
    • 0033303297 scopus 로고    scopus 로고
    • Structural properties of the nickel ions in urease: Novel insights into the catalytic and inhibition mechanisms
    • Ciurli, S.; Benini, S.; Rypniewski, W. R.; Wilson, K. S.; Miletti, S.; Mangani, S. Structural properties of the nickel ions in urease: Novel insights into the catalytic and inhibition mechanisms Coord. Chem. Rev. 1999, 190, 331-355
    • (1999) Coord. Chem. Rev. , vol.190 , pp. 331-355
    • Ciurli, S.1    Benini, S.2    Rypniewski, W.R.3    Wilson, K.S.4    Miletti, S.5    Mangani, S.6
  • 10
    • 0019021563 scopus 로고
    • Jack bean urease (EC 3.5.1.5). I. A simple dry ashing procedure for the microdetermination of trace metals in proteins. The nickel content of urease
    • Dixon, N. E.; Blakeley, R. L.; Zerner, B. Jack bean urease (EC 3.5.1.5). I. A simple dry ashing procedure for the microdetermination of trace metals in proteins. The nickel content of urease Can. J. Biochem. 1980, 58, 469-473
    • (1980) Can. J. Biochem. , vol.58 , pp. 469-473
    • Dixon, N.E.1    Blakeley, R.L.2    Zerner, B.3
  • 11
    • 0034000386 scopus 로고    scopus 로고
    • The complex of Bacillus pasteurii urease with acetohydroxamate anion from X-ray data at 1.55 - resolution
    • Benini, S.; Rypniewski, W. R.; Wilson, K. S.; Miletti, S.; Ciurli, S.; Mangani, S. The complex of Bacillus pasteurii urease with acetohydroxamate anion from X-ray data at 1.55 - resolution J. Biol. Inorg. Chem. 2000, 5, 110-118
    • (2000) J. Biol. Inorg. Chem. , vol.5 , pp. 110-118
    • Benini, S.1    Rypniewski, W.R.2    Wilson, K.S.3    Miletti, S.4    Ciurli, S.5    Mangani, S.6
  • 13
    • 77955889304 scopus 로고    scopus 로고
    • version 6.9; Triops Associates Inc.: St. Louis, MO.
    • SYBYL Software Package, version 6.9; Triops Associates Inc.: St. Louis, MO, 2006.
    • (2006) SYBYL Software Package
  • 14
    • 77955880095 scopus 로고    scopus 로고
    • Version 4.0; Astex Technology: Cambridge, United Kingdom.
    • GOLD, Version 4.0; Astex Technology: Cambridge, United Kingdom, 2001.
    • (2001) GOLD
  • 15
    • 0034846165 scopus 로고    scopus 로고
    • Structure-based computational study of the catalytic and inhibition mechanisms of urease
    • Musiani, F.; Arnofi, E.; Casadio, R.; Ciurli, S. Structure-based computational study of the catalytic and inhibition mechanisms of urease J. Biol. Inorg. Chem. 2001, 6, 300-314
    • (2001) J. Biol. Inorg. Chem. , vol.6 , pp. 300-314
    • Musiani, F.1    Arnofi, E.2    Casadio, R.3    Ciurli, S.4
  • 17
    • 0346690153 scopus 로고    scopus 로고
    • Alpha-hydroxyketones as inhibitors of urease
    • Tanaka, T.; Kawase, M.; Tani, S. Alpha-hydroxyketones as inhibitors of urease Bioorg. Med. Chem. 2004, 12, 501-505
    • (2004) Bioorg. Med. Chem. , vol.12 , pp. 501-505
    • Tanaka, T.1    Kawase, M.2    Tani, S.3
  • 18
    • 33947332625 scopus 로고
    • Enzymic method for urea in urine
    • Weatherburn, M. W. Enzymic method for urea in urine Anal. Chem. 1967, 39, 971-974
    • (1967) Anal. Chem. , vol.39 , pp. 971-974
    • Weatherburn, M.W.1
  • 19
    • 77955905164 scopus 로고    scopus 로고
    • Catalog No. 102049, Lot No. 3478E; M. B., LLC: Aurora, OH.
    • Catalog No. 102049, Lot No. 3478E; M. B., LLC: Aurora, OH.
  • 20
    • 77955859118 scopus 로고    scopus 로고
    • Lot and Filling Code 1108805; Fluka Chemie GmbH: Buchs, Germany.
    • Lot and Filling Code 1108805; Fluka Chemie GmbH: Buchs, Germany.
  • 21
    • 77955890257 scopus 로고    scopus 로고
    • K. S. U., 742012, 24-microaion, 5-1, Nukus City, Uzbekistan.
    • Tlegenoy, R. T. K. S. U., 742012, 24-microaion, 5-1, Nukus City, Uzbekistan.
    • Tlegenoy, R.T.1
  • 22
    • 2942530702 scopus 로고    scopus 로고
    • Kinetics of novel competitive inhibitors of urease enzymes by a focused library of oxadiazoles/thiadiazoles and triazoles
    • Amtul, Z.; Rasheed, M.; Choudhary, M. I.; Rosanna, S.; Khan, K. M. Kinetics of novel competitive inhibitors of urease enzymes by a focused library of oxadiazoles/thiadiazoles and triazoles Biochem. Biophys. Res. Commun. 2004, 319, 1053-1063
    • (2004) Biochem. Biophys. Res. Commun. , vol.319 , pp. 1053-1063
    • Amtul, Z.1    Rasheed, M.2    Choudhary, M.I.3    Rosanna, S.4    Khan, K.M.5
  • 23
    • 67649846462 scopus 로고    scopus 로고
    • Synthesis, urease inhibition and antimicrobial activities of some chiral 5-aryl-4-(1-phenylpropyl)-2 H -1,2,4-triazole-3(4 H)-thiones
    • Serwar, M.; Akhtar, T.; Hameed, S.; Khan, K. M. Synthesis, urease inhibition and antimicrobial activities of some chiral 5-aryl-4-(1-phenylpropyl) -2 H -1,2,4-triazole-3(4 H)-thiones ARKIVOC 2009, 7, 210-221
    • (2009) ARKIVOC , vol.7 , pp. 210-221
    • Serwar, M.1    Akhtar, T.2    Hameed, S.3    Khan, K.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.