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Volumn 4, Issue 11, 2009, Pages 928-938

Discovery of specific flavodoxin inhibitors as potential therapeutic agents against Helicobacter pylori infection

Author keywords

[No Author keywords available]

Indexed keywords

ANTIINFECTIVE AGENT; FLAVODOXIN; FLAVODOXIN INHIBITOR; PROTEIN INHIBITOR; UNCLASSIFIED DRUG;

EID: 73449083030     PISSN: 15548929     EISSN: None     Source Type: Journal    
DOI: 10.1021/cb900166q     Document Type: Article
Times cited : (50)

References (44)
  • 1
    • 0021259505 scopus 로고
    • Unidentified curved bacilli in the stomach of patients with gastritis and peptic ulceration
    • Marshall, B. J., and Warren, J. R. (1984) Unidentified curved bacilli in the stomach of patients with gastritis and peptic ulceration, Lancet 1, 1311-1315.
    • (1984) Lancet , vol.1 , pp. 1311-1315
    • Marshall, B.J.1    Warren, J.R.2
  • 2
    • 0027213922 scopus 로고
    • Regression of primary low-grade B-cell gastric lymphoma of mucosa-associated lymphoid tissue type after eradication of Helicobacter pylori
    • Wotherspoon, A. C., Doglioni, C., Diss, T. C., Pan, L., Moschini, A., de Boni, M., and Isaacson, P. G. (1993) Regression of primary low-grade B-cell gastric lymphoma of mucosa-associated lymphoid tissue type after eradication of Helicobacter pylori, Lancet 342, 575-577.
    • (1993) Lancet , vol.342 , pp. 575-577
    • Wotherspoon, A.C.1    Doglioni, C.2    Diss, T.C.3    Pan, L.4    Moschini, A.5    de Boni, M.6    Isaacson, P.G.7
  • 5
    • 49249102613 scopus 로고    scopus 로고
    • Epidemiology of Helicobacter pylori infection
    • Bruce, M. G., and Maaroos, H. I. (2008) Epidemiology of Helicobacter pylori infection, Helicobacter 13, 1-6.
    • (2008) Helicobacter , vol.13 , pp. 1-6
    • Bruce, M.G.1    Maaroos, H.I.2
  • 6
    • 34447092208 scopus 로고    scopus 로고
    • Immunology of Helicobacter pylori: Insights into the failure of the immune response and perspectives on vaccine studies
    • Wilson, K. T., and Crabtree, J. E. (2007) Immunology of Helicobacter pylori: insights into the failure of the immune response and perspectives on vaccine studies, Gastroenterology 133, 288-308.
    • (2007) Gastroenterology , vol.133 , pp. 288-308
    • Wilson, K.T.1    Crabtree, J.E.2
  • 7
    • 39749133744 scopus 로고    scopus 로고
    • Helicobacter pylori vaccine: From past to future
    • Agarwal, K., and Agarwal, S. (2008) Helicobacter pylori vaccine: from past to future, Mayo Clin. Proc. 83, 169-175.
    • (2008) Mayo Clin. Proc , vol.83 , pp. 169-175
    • Agarwal, K.1    Agarwal, S.2
  • 8
    • 0028863316 scopus 로고
    • New options in eradication of Helicobacter pylori
    • Seppala, K., and Nuutinen, H. (1995) New options in eradication of Helicobacter pylori, Ann. Med. 27, 601-604.
    • (1995) Ann. Med , vol.27 , pp. 601-604
    • Seppala, K.1    Nuutinen, H.2
  • 9
    • 0032034028 scopus 로고    scopus 로고
    • Primary and acquired Helicobacter pylori resistance to clarithromycin, metronidazole, and amoxicillin-influence on treatment outcome
    • Adamek, R. J., Suerbaum, S., Pfaffenbach, B., and Opferkuch, W. (1998) Primary and acquired Helicobacter pylori resistance to clarithromycin, metronidazole, and amoxicillin-influence on treatment outcome, Am. J. Gastroenterol. 93, 386-389.
    • (1998) Am. J. Gastroenterol , vol.93 , pp. 386-389
    • Adamek, R.J.1    Suerbaum, S.2    Pfaffenbach, B.3    Opferkuch, W.4
  • 10
    • 0031693586 scopus 로고    scopus 로고
    • Antimicrobial resistance in Helicobacter pylori: A global overview
    • Glupczynski, Y. (1998) Antimicrobial resistance in Helicobacter pylori: a global overview, Acta Gastroenterol. Belg. 61, 357-366.
    • (1998) Acta Gastroenterol. Belg , vol.61 , pp. 357-366
    • Glupczynski, Y.1
  • 11
  • 12
    • 12944284656 scopus 로고    scopus 로고
    • Tetracycline-resistant clinical Helicobacter pylori isolates with and without mutations in 16S rRNA-encoding genes
    • Wu, J. Y., Kim, J. J., Reddy, R., Wang, W. M., Graham, D. Y., and Kwon, D. H. (2005) Tetracycline-resistant clinical Helicobacter pylori isolates with and without mutations in 16S rRNA-encoding genes, Antimicrob. Agents Chemother. 49, 578-583.
    • (2005) Antimicrob. Agents Chemother , vol.49 , pp. 578-583
    • Wu, J.Y.1    Kim, J.J.2    Reddy, R.3    Wang, W.M.4    Graham, D.Y.5    Kwon, D.H.6
  • 14
    • 44949243126 scopus 로고    scopus 로고
    • New concepts of resistance in the treatment of Helicobacter pylori infections
    • Graham, D. Y., and Shiotani, A. (2008) New concepts of resistance in the treatment of Helicobacter pylori infections, Nat. Clin. Pract. Gastroenterol. Hepatol. 5, 321-331.
    • (2008) Nat. Clin. Pract. Gastroenterol. Hepatol , vol.5 , pp. 321-331
    • Graham, D.Y.1    Shiotani, A.2
  • 15
    • 4544347056 scopus 로고    scopus 로고
    • Basis for the management of drug-resistant Helicobacter pylori infection
    • Mégraud, F. (2004) Basis for the management of drug-resistant Helicobacter pylori infection, Drugs 64, 1893-1904.
    • (2004) Drugs , vol.64 , pp. 1893-1904
    • Mégraud, F.1
  • 17
    • 0036145495 scopus 로고    scopus 로고
    • Crystal structure of oxidized flavodoxin, an essential protein in Helicobacter pylori
    • Freigang, J., Diederichs, K., Schafer, K. P., Welte, W., and Paul, R. (2002) Crystal structure of oxidized flavodoxin, an essential protein in Helicobacter pylori, Protein Sci. 11, 253-261.
    • (2002) Protein Sci , vol.11 , pp. 253-261
    • Freigang, J.1    Diederichs, K.2    Schafer, K.P.3    Welte, W.4    Paul, R.5
  • 18
    • 14744268574 scopus 로고    scopus 로고
    • Towards a new therapeutic target: Helicobacter pylori flavodoxin
    • Cremades, N., Bueno, M., Toja, M., and Sancho, J. (2005) Towards a new therapeutic target: Helicobacter pylori flavodoxin, Biophys. Chem. 115, 267-276.
    • (2005) Biophys. Chem , vol.115 , pp. 267-276
    • Cremades, N.1    Bueno, M.2    Toja, M.3    Sancho, J.4
  • 19
    • 33646052947 scopus 로고    scopus 로고
    • Flavodoxins: Sequence, folding, binding, function and beyond
    • Sancho, J. (2006) Flavodoxins: sequence, folding, binding, function and beyond, Cell. Mol. Life Sci. 63, 855-864.
    • (2006) Cell. Mol. Life Sci. 63 , pp. 855-864
    • Sancho, J.1
  • 20
    • 0029046363 scopus 로고
    • Identification of carboxylation enzymes and characterization of a novel four-subunit pyruvate:flavodoxin oxidoreductase from Helicobacter pylori
    • Hughes, N. J., Chalk, P. A., Clayton, C. L., and Kelly, D. J. (1995) Identification of carboxylation enzymes and characterization of a novel four-subunit pyruvate:flavodoxin oxidoreductase from Helicobacter pylori, J. Bacteriol. 177, 3953-3959.
    • (1995) J. Bacteriol , vol.177 , pp. 3953-3959
    • Hughes, N.J.1    Chalk, P.A.2    Clayton, C.L.3    Kelly, D.J.4
  • 21
    • 34347386473 scopus 로고    scopus 로고
    • St Maurice, M., Cremades, N., Croxen, M. A., Sisson, G., Sancho, J., and Hoffman, P. S. (2007) Flavodoxin:Quinone Reductase (FqrB): a redox partner of pyruvate:ferredoxin oxidoreductase that reversibly couples pyruvate oxidation to NADPH production in Helicobacter pylori and Campylobacter jejuni, J. Bacteriol. 189, 4764-4773.
    • St Maurice, M., Cremades, N., Croxen, M. A., Sisson, G., Sancho, J., and Hoffman, P. S. (2007) Flavodoxin:Quinone Reductase (FqrB): a redox partner of pyruvate:ferredoxin oxidoreductase that reversibly couples pyruvate oxidation to NADPH production in Helicobacter pylori and Campylobacter jejuni, J. Bacteriol. 189, 4764-4773.
  • 22
    • 0035108401 scopus 로고    scopus 로고
    • Essential thioredoxin-dependent peroxiredoxin system from Helicobacter pylori: Genetic and kinetic characterization
    • Baker, L. M., Raudonikiene, A., Hoffman, P. S., and Poole, L. B. (2001) Essential thioredoxin-dependent peroxiredoxin system from Helicobacter pylori: genetic and kinetic characterization, J. Bacteriol. 183, 1961-1973.
    • (2001) J. Bacteriol , vol.183 , pp. 1961-1973
    • Baker, L.M.1    Raudonikiene, A.2    Hoffman, P.S.3    Poole, L.B.4
  • 23
    • 0019321060 scopus 로고
    • Substrate stabilization of lysozyme to thermal and guanidine hydrochloride denaturation
    • Pace, C. N., and McGrath, T. (1980) Substrate stabilization of lysozyme to thermal and guanidine hydrochloride denaturation, J. Biol. Chem. 255, 3862-3865.
    • (1980) J. Biol. Chem , vol.255 , pp. 3862-3865
    • Pace, C.N.1    McGrath, T.2
  • 24
    • 0025281866 scopus 로고
    • Study of strong to ultratight protein interactions using differential scanning calorimetry
    • Brandts, J. F., and Lin, L. N. (1990) Study of strong to ultratight protein interactions using differential scanning calorimetry, Biochemistry 29, 6927-6940.
    • (1990) Biochemistry , vol.29 , pp. 6927-6940
    • Brandts, J.F.1    Lin, L.N.2
  • 25
    • 0026734102 scopus 로고
    • Two-dimensional differential scanning calorimetry: Simultaneous resolution of intrinsic protein structural energetics and ligand binding interactions by global linkage analysis
    • Straume, M., and Freire, E. (1992) Two-dimensional differential scanning calorimetry: simultaneous resolution of intrinsic protein structural energetics and ligand binding interactions by global linkage analysis, Anal. Biochem. 203, 259-268.
    • (1992) Anal. Biochem , vol.203 , pp. 259-268
    • Straume, M.1    Freire, E.2
  • 27
    • 4143121255 scopus 로고    scopus 로고
    • Evaluation of fluorescence-based thermal shift assays for hit identification in drug discovery
    • Lo, M. C., Aulabaugh, A., Jin, G., Cowling, R., Bard, J., Malamas, M., and Ellestad, G. (2004) Evaluation of fluorescence-based thermal shift assays for hit identification in drug discovery, Anal. Biochem. 332, 153-159.
    • (2004) Anal. Biochem , vol.332 , pp. 153-159
    • Lo, M.C.1    Aulabaugh, A.2    Jin, G.3    Cowling, R.4    Bard, J.5    Malamas, M.6    Ellestad, G.7
  • 28
    • 33751559579 scopus 로고    scopus 로고
    • Screening for ligands using a generic and high-throughput light-scattering-based assay
    • Senisterra, G. A., Markin, E., Yamazaki, K., Hui, R., Vedadi, M., and Awrey, D. E. (2006) Screening for ligands using a generic and high-throughput light-scattering-based assay, J. Biomol. Screening 11, 940-948.
    • (2006) J. Biomol. Screening , vol.11 , pp. 940-948
    • Senisterra, G.A.1    Markin, E.2    Yamazaki, K.3    Hui, R.4    Vedadi, M.5    Awrey, D.E.6
  • 29
    • 13944274061 scopus 로고    scopus 로고
    • Grasberger, B. L., Lu, T., Schubert, C., Parks, D. J., Carver, T. E., Koblish, H. K., Cummings, M. D., LaFrance, L. V., Milkiewicz, K. L., Calvo, R. R., Maguire, D., Lattanze, J., Franks, C. F., Zhao, S., Ramachandren, K., Bylebyl, G. R., Zhang, M., Manthey, C. L., Petrella, E. C., Pantoliano, M. W., Deckman, I. C., Spurlino, J. C., Maroney, A. C., Tomczuk, B. E., Molloy, C. J., and Bone, R. F. (2005) Discovery and cocrystal structure of benzodiazepinedione HDM2 antagonists that activate p53 in cells, J. Med. Chem. 48, 909-912.
    • Grasberger, B. L., Lu, T., Schubert, C., Parks, D. J., Carver, T. E., Koblish, H. K., Cummings, M. D., LaFrance, L. V., Milkiewicz, K. L., Calvo, R. R., Maguire, D., Lattanze, J., Franks, C. F., Zhao, S., Ramachandren, K., Bylebyl, G. R., Zhang, M., Manthey, C. L., Petrella, E. C., Pantoliano, M. W., Deckman, I. C., Spurlino, J. C., Maroney, A. C., Tomczuk, B. E., Molloy, C. J., and Bone, R. F. (2005) Discovery and cocrystal structure of benzodiazepinedione HDM2 antagonists that activate p53 in cells, J. Med. Chem. 48, 909-912.
  • 30
    • 16344382388 scopus 로고    scopus 로고
    • Thermodynamic stability of carbonic anhydrase: Measurements of binding affinity and stoichiometry using ThermoFluor
    • Matulis, D., Kranz, J. K., Salemme, F. R., and Todd, M. J. (2005) Thermodynamic stability of carbonic anhydrase: measurements of binding affinity and stoichiometry using ThermoFluor, Biochemistry. 44, 5258-5266.
    • (2005) Biochemistry , vol.44 , pp. 5258-5266
    • Matulis, D.1    Kranz, J.K.2    Salemme, F.R.3    Todd, M.J.4
  • 32
    • 0037107026 scopus 로고    scopus 로고
    • High-throughput cell-based assays in yeast
    • Tucker, C. L. (2002) High-throughput cell-based assays in yeast, Drug Discovery Today 7, S125-130.
    • (2002) Drug Discovery Today , vol.7
    • Tucker, C.L.1
  • 33
    • 38849142536 scopus 로고    scopus 로고
    • The flavodoxin from Helicobacter pylori: Structural determinants of thermostability and FMN cofactor binding
    • Cremades, N., Velazquez-Campoy, A., Freire, E., and Sancho, J. (2008) The flavodoxin from Helicobacter pylori: structural determinants of thermostability and FMN cofactor binding, Biochemistry 47, 627-639.
    • (2008) Biochemistry , vol.47 , pp. 627-639
    • Cremades, N.1    Velazquez-Campoy, A.2    Freire, E.3    Sancho, J.4
  • 34
    • 33847660062 scopus 로고    scopus 로고
    • Antiparasitic drug nitazoxanide inhibits the pyruvate oxidoreductases of Helicobacter pylori and selected anaerobic bacteria and parasites, and Campylobacter jejuni
    • Hoffman, P. S., Sisson, G., Croxen, M. A., Welch, K., Harman, W. D., Cremades, N., and Morash, M. G. (2007) Antiparasitic drug nitazoxanide inhibits the pyruvate oxidoreductases of Helicobacter pylori and selected anaerobic bacteria and parasites, and Campylobacter jejuni, Antimicrob. Agents Chemother. 51, 868-876.
    • (2007) Antimicrob. Agents Chemother , vol.51 , pp. 868-876
    • Hoffman, P.S.1    Sisson, G.2    Croxen, M.A.3    Welch, K.4    Harman, W.D.5    Cremades, N.6    Morash, M.G.7
  • 36
    • 27644544444 scopus 로고    scopus 로고
    • In vitro cytotoxicity assays: Comparison of LDH, neutral red, MTT and protein assay in hepatoma cell lines following exposure to cadmium chloride
    • Fotakis, G., and Timbrell, J. A. (2006) In vitro cytotoxicity assays: comparison of LDH, neutral red, MTT and protein assay in hepatoma cell lines following exposure to cadmium chloride, Toxicol. Lett. 160, 171-177.
    • (2006) Toxicol. Lett , vol.160 , pp. 171-177
    • Fotakis, G.1    Timbrell, J.A.2
  • 37
    • 46149103166 scopus 로고    scopus 로고
    • Application of a high-content multiparameter cytotoxicity assay to prioritize compounds based on toxicity potential in humans
    • Abraham, V. C., Towne, D. L., Waring, J. F., Warrior, U., and Burns, D. J. (2008) Application of a high-content multiparameter cytotoxicity assay to prioritize compounds based on toxicity potential in humans, J. Biomol. Screening 13, 527-537.
    • (2008) J. Biomol. Screening , vol.13 , pp. 527-537
    • Abraham, V.C.1    Towne, D.L.2    Waring, J.F.3    Warrior, U.4    Burns, D.J.5
  • 38
    • 35048859971 scopus 로고    scopus 로고
    • Molecular recognition and screening using a 15N group selective STD NMR method
    • Kover, K. E., Groves, P., Jimenez-Barbero, J., and Batta, G. (2007) Molecular recognition and screening using a 15N group selective STD NMR method, J. Am. Chem. Soc. 129, 11579-11582.
    • (2007) J. Am. Chem. Soc , vol.129 , pp. 11579-11582
    • Kover, K.E.1    Groves, P.2    Jimenez-Barbero, J.3    Batta, G.4
  • 39
    • 41449092838 scopus 로고    scopus 로고
    • Conformational stability of Helicobacter pyloriflavodoxin: Fit to function at pH 5
    • Cremades, N., Bueno, M., Neira, J. L., Velazquez-Campoy, A., and Sancho, J. (2008) Conformational stability of Helicobacter pyloriflavodoxin: fit to function at pH 5, J. Biol. Chem. 283, 2883-2895.
    • (2008) J. Biol. Chem , vol.283 , pp. 2883-2895
    • Cremades, N.1    Bueno, M.2    Neira, J.L.3    Velazquez-Campoy, A.4    Sancho, J.5
  • 41
    • 0014669476 scopus 로고
    • Purification and characterization of flavodoxin from Peptostreptococcus elsdenii
    • Mayhew, S. G., and Massey, V. (1969) Purification and characterization of flavodoxin from Peptostreptococcus elsdenii, J. Biol. Chem. 244, 794-802.
    • (1969) J. Biol. Chem , vol.244 , pp. 794-802
    • Mayhew, S.G.1    Massey, V.2
  • 42
    • 0035289779 scopus 로고    scopus 로고
    • Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings
    • Lipinski, C. A., Lombardo, F., Dominy, B. W., and Feeney, P. J. (2001) Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings, Adv. Drug Delivery Rev. 46, 3-26.
    • (2001) Adv. Drug Delivery Rev , vol.46 , pp. 3-26
    • Lipinski, C.A.1    Lombardo, F.2    Dominy, B.W.3    Feeney, P.J.4
  • 43
    • 0000892020 scopus 로고    scopus 로고
    • Clustering of large databases of compounds: Using the MDL "keys" as structural descriptors
    • McGregor, M. J., and Pallai, P. V. (1997) Clustering of large databases of compounds: using the MDL "keys" as structural descriptors, J. Chem. Inf. Comput. Sci. 37, 443-448.
    • (1997) J. Chem. Inf. Comput. Sci , vol.37 , pp. 443-448
    • McGregor, M.J.1    Pallai, P.V.2
  • 44
    • 0018588511 scopus 로고
    • Stability of proteins: Small globular proteins
    • Privalov, P. L. (1979) Stability of proteins: small globular proteins, Adv. Protein Chem. 33, 167-241.
    • (1979) Adv. Protein Chem , vol.33 , pp. 167-241
    • Privalov, P.L.1


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