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Volumn 25, Issue 1, 2012, Pages 95-102

Inhibition of fumarase by bismuth(III): Implications for the tricarboxylic acid cycle as a potential target of bismuth drugs in Helicobacter pylori

Author keywords

Bismuth; Fumarase; Helicobacter pylori; Tricarboxylic acid cycle

Indexed keywords

BISMUTH; FUMARATE HYDRATASE; MALIC ACID; TRICARBOXYLIC ACID; BACTERIAL PROTEIN;

EID: 84857699968     PISSN: 09660844     EISSN: 15728773     Source Type: Journal    
DOI: 10.1007/s10534-011-9485-7     Document Type: Article
Times cited : (26)

References (44)
  • 1
    • 6044221427 scopus 로고    scopus 로고
    • Exploiting the right side of the Ramachandran plot: Substitution of glycines by D-alanine can significantly increase protein stability
    • Anil B, Song B, Tang Y, Raleigh DP (2004) Exploiting the right side of the Ramachandran plot: substitution of glycines by D-alanine can significantly increase protein stability. J Am Chem Soc 126:13194-13195
    • (2004) J Am Chem Soc , vol.126 , pp. 13194-13195
    • Anil, B.1    Song, B.2    Tang, Y.3    Raleigh, D.P.4
  • 2
    • 27944508350 scopus 로고    scopus 로고
    • Expression and intracellular localization of Pyk2 in normal and v-src transformed chicken epiphyseal chondrocytes
    • Arcucci A, Montagnani S, Gionti E (2006) Expression and intracellular localization of Pyk2 in normal and v-src transformed chicken epiphyseal chondrocytes. Biochimie 88:77-84
    • (2006) Biochimie , vol.88 , pp. 77-84
    • Arcucci, A.1    Montagnani, S.2    Gionti, E.3
  • 3
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: A web-based environment for protein structure homology modelling
    • Arnold K, Bordoli L, Kopp J (2006) The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling. Bioinformatics 22:195-201
    • (2006) Bioinformatics , vol.22 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3
  • 5
    • 0023197923 scopus 로고
    • Gastric Campylobacter-like organisms, gastritis, and peptic ulcer disease
    • Blaser MJ (1987) Gastric Campylobacter-like organisms, gastritis, and peptic ulcer disease. Gastroenterology 93:371-383
    • (1987) Gastroenterology , vol.93 , pp. 371-383
    • Blaser, M.J.1
  • 7
    • 0033565832 scopus 로고    scopus 로고
    • Role of accurate mass measurement (±10 ppm) in protein identification strategies employing MS or MS/MS and database searching
    • Clauser KR, Baker P, Burlingame AL (1999) Role of accurate mass measurement (±10 ppm) in protein identification strategies employing MS or MS/MS and database searching. Anal Chem 71:2871-2882
    • (1999) Anal Chem , vol.71 , pp. 2871-2882
    • Clauser, K.R.1    Baker, P.2    Burlingame, A.L.3
  • 9
    • 47249162533 scopus 로고    scopus 로고
    • A histidine-rich and cysteine-rich metal-binding domain at the C terminus of heat shock protein A from Helicobacter pylori: Implication for nickel homeostasis and bismuth susceptibility
    • Cun S, Li H, Ge R, Lin MC, Sun H (2008) A histidine-rich and cysteine-rich metal-binding domain at the C terminus of heat shock protein A from Helicobacter pylori: implication for nickel homeostasis and bismuth susceptibility. J Biol Chem 283:15142-15151
    • (2008) J Biol Chem , vol.283 , pp. 15142-15151
    • Cun, S.1    Li, H.2    Ge, R.3    Lin, M.C.4    Sun, H.5
  • 11
    • 0035873182 scopus 로고    scopus 로고
    • Neutrophil-activating protein (HPNAP) versus ferritin (Pfr): Comparison of synthesis in Helicobacter pylori
    • Dundon WG, Polenghi A, Del Guidice G, Rappuoli R, Montecucco C (2001) Neutrophil-activating protein (HPNAP) versus ferritin (Pfr): comparison of synthesis in Helicobacter pylori. FEMS Microbiol Lett 199:143-149
    • (2001) FEMS Microbiol Lett , vol.199 , pp. 143-149
    • Dundon, W.G.1    Polenghi, A.2    Del Guidice, G.3    Rappuoli, R.4    Montecucco, C.5
  • 12
    • 3042934967 scopus 로고
    • Tissue sulfhydryl groups
    • Ellman GL (1959) Tissue sulfhydryl groups. Arch Biochem Biophys 82:70-77
    • (1959) Arch Biochem Biophys , vol.82 , pp. 70-77
    • Ellman, G.L.1
  • 13
    • 0036249007 scopus 로고    scopus 로고
    • Potential of fumarate reductase as a novel therapeutic target in Helicobacter pylori infection
    • Ge Z (2002) Potential of fumarate reductase as a novel therapeutic target in Helicobacter pylori infection. Expert Opin Ther Targets 6:135-146
    • (2002) Expert Opin Ther Targets , vol.6 , pp. 135-146
    • Ge, Z.1
  • 14
    • 34248380121 scopus 로고    scopus 로고
    • Bioinorganic chemistry of bismuth and antimony: Target sites of metallodrugs
    • Ge R, Sun H (2007) Bioinorganic chemistry of bismuth and antimony: target sites of metallodrugs. Acc Chem Res 40:267-274
    • (2007) Acc Chem Res , vol.40 , pp. 267-274
    • Ge, R.1    Sun, H.2
  • 15
    • 0033679563 scopus 로고    scopus 로고
    • Fumarate reductase is essential for Helicobacter pyloricolonization of the mouse stomach
    • Ge Z, Feng Y, Dangler CA, Xu S, Taylor NS, Fox JG (2000) Fumarate reductase is essential for Helicobacter pyloricolonization of the mouse stomach. Microb Pathog 29:279-287
    • (2000) Microb Pathog , vol.29 , pp. 279-287
    • Ge, Z.1    Feng, Y.2    Dangler, C.A.3    Xu, S.4    Taylor, N.S.5    Fox, J.G.6
  • 16
    • 30044451654 scopus 로고    scopus 로고
    • Expression and characterization of a histidinerich protein, Hpn: Potential for Ni2? storage in Helicobacter pylori
    • Ge R, Watt RM, Sun X, Tanner JA, He QY, Huang JD, Sun H (2006a) Expression and characterization of a histidinerich protein, Hpn: potential for Ni2? storage in Helicobacter pylori. Biochem J 393:285-293
    • (2006) Biochem J , vol.393 , pp. 285-293
    • Ge, R.1    Watt, R.M.2    Sun, X.3    Tanner, J.A.4    He, Q.Y.5    Huang, J.D.6    Sun, H.7
  • 17
    • 33748372299 scopus 로고    scopus 로고
    • Thermodynamic and kinetic aspects of metal binding to the histidine-rich protein, Hpn
    • Ge R, Zhang Y, Sun X, Watt RM, He QY, Huang JD, Wilcox DE, Sun H (2006b) Thermodynamic and kinetic aspects of metal binding to the histidine-rich protein, Hpn. J Am Chem Soc 128:11330-11331
    • (2006) J Am Chem Soc , vol.128 , pp. 11330-11331
    • Ge, R.1    Zhang, Y.2    Sun, X.3    Watt, R.M.4    He, Q.Y.5    Huang, J.D.6    Wilcox, D.E.7    Sun, H.8
  • 19
    • 0022383317 scopus 로고
    • The fumarase genes of Escherichia coli: Location of the fumB gene and discovery of a new gene (fumC)
    • Guest JR, Miles JS, Roberts RE, Woods SA (1985) The fumarase genes of Escherichia coli: location of the fumB gene and discovery of a new gene (fumC). J Gen Microbiol 131:2971-2984
    • (1985) J Gen Microbiol , vol.131 , pp. 2971-2984
    • Guest, J.R.1    Miles, J.S.2    Roberts, R.E.3    Woods, S.A.4
  • 20
    • 0037541161 scopus 로고    scopus 로고
    • Serum biomarkers of hepatitis B virus infected liver inflammation: A proteomic study
    • He QY, Lau GK, Zhou Y, Yuen ST, Lin MC, Kung HF, Chiu JF (2003) Serum biomarkers of hepatitis B virus infected liver inflammation: a proteomic study. Proteomics 3:666-674
    • (2003) Proteomics , vol.3 , pp. 666-674
    • He, Q.Y.1    Lau, G.K.2    Zhou, Y.3    Yuen, S.T.4    Lin, M.C.5    Kung, H.F.6    Chiu, J.F.7
  • 23
    • 0030984635 scopus 로고    scopus 로고
    • The actions of bismuth in the treatment of Helicobacter pylori infection
    • Lambert JR, Midolo P (1997) The actions of bismuth in the treatment of Helicobacter pylori infection. Aliment Pharmacol Ther 11:27-33
    • (1997) Aliment Pharmacol Ther , vol.11 , pp. 27-33
    • Lambert, J.R.1    Midolo, P.2
  • 25
    • 4544347056 scopus 로고    scopus 로고
    • Basis for the management of drug-resistant Helicobacter pylori infection
    • Megraud F (2004) Basis for the management of drug-resistant Helicobacter pylori infection. Drugs 64:1893-1904
    • (2004) Drugs , vol.64 , pp. 1893-1904
    • Megraud, F.1
  • 26
    • 0029113366 scopus 로고
    • Fumarate reductase: A target for therapeutic intervention against Helicobacter pylori
    • Mendz GL, Hazell SL, Srinivasan S (1995) Fumarate reductase: a target for therapeutic intervention against Helicobacter pylori. Arch Biochem Biophys 321:153-159
    • (1995) Arch Biochem Biophys , vol.321 , pp. 153-159
    • Mendz, G.L.1    Hazell, S.L.2    Srinivasan, S.3
  • 27
    • 14644390842 scopus 로고    scopus 로고
    • A survey of left-handed helices in protein structures
    • Novotny M, Kleywegt GJ (2005) A survey of left-handed helices in protein structures. J Mol Biol 347:231-241
    • (2005) J Mol Biol , vol.347 , pp. 231-241
    • Novotny, M.1    Kleywegt, G.J.2
  • 29
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set
    • Sreerama N, WoodyRW(2000) Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set. Anal Biochem 287:252-260
    • (2000) Anal Biochem , vol.287 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 30
    • 33846816976 scopus 로고    scopus 로고
    • HIF and fumarate hydratase in renal cancer
    • Sudarshan S, Linehan WM, Neckers L (2007) HIF and fumarate hydratase in renal cancer. Br J Cancer 96:403-407
    • (2007) Br J Cancer , vol.96 , pp. 403-407
    • Sudarshan, S.1    Linehan, W.M.2    Neckers, L.3
  • 31
    • 0037293217 scopus 로고    scopus 로고
    • Binding of bismuth to serum proteins: Implication for targets of Bi(III) in blood plasma
    • Sun H, Szeto KY (2003) Binding of bismuth to serum proteins: implication for targets of Bi(III) in blood plasma. J Inorg Biochem 94:114-120
    • (2003) J Inorg Biochem , vol.94 , pp. 114-120
    • Sun, H.1    Szeto, K.Y.2
  • 32
    • 0032855503 scopus 로고    scopus 로고
    • Interactions of bismuth complexes with metallothionein(II)
    • Sun H, Li H, Harvey I, Sadler PJ (1999) Interactions of bismuth complexes with metallothionein(II). J Biol Chem 274:29094-29101
    • (1999) J Biol Chem , vol.274 , pp. 29094-29101
    • Sun, H.1    Li, H.2    Harvey, I.3    Sadler, P.J.4
  • 33
    • 53049109507 scopus 로고    scopus 로고
    • Identification of proteins related to nickel homeostasis in Helicobacter pylori by immobilized metal affinity chromatography and two-dimensional gel electrophoresis
    • Sun X, Ge R, Chiu JF, Sun H, He QY (2008) Identification of proteins related to nickel homeostasis in Helicobacter pylori by immobilized metal affinity chromatography and two-dimensional gel electrophoresis. Met Based Drugs 2008:289490
    • (2008) Met Based Drugs , vol.2008 , pp. 289490
    • Sun, X.1    Ge, R.2    Chiu, J.F.3    Sun, H.4    He, Q.Y.5
  • 34
    • 67449161823 scopus 로고    scopus 로고
    • Iron depletion decreases proliferation and induces apoptosis in a human colonic adenocarcinoma cell line, Caco2
    • Sun X, Ge R, Cai Z, Sun H, He Q-Y (2009) Iron depletion decreases proliferation and induces apoptosis in a human colonic adenocarcinoma cell line, Caco2. J Inorg Biochem 103:1074-1081
    • (2009) J Inorg Biochem , vol.103 , pp. 1074-1081
    • Sun, X.1    Ge, R.2    Cai, Z.3    Sun, H.4    He, Q.-Y.5
  • 35
    • 78649934102 scopus 로고    scopus 로고
    • Iron-containing lipoprotein SiaAin SiaABC, the primary hemetransporter of Streptococcus pyogenes
    • Sun X, Ge R, Zhang D, Sun H, He QY (2010) Iron-containing lipoprotein SiaAin SiaABC, the primary hemetransporter of Streptococcus pyogenes. J Biol Inorg Chem 15:1265-1273
    • (2010) J Biol Inorg Chem , vol.15 , pp. 1265-1273
    • Sun, X.1    Ge, R.2    Zhang, D.3    Sun, H.4    He, Q.Y.5
  • 37
    • 0034031992 scopus 로고    scopus 로고
    • Electrical conductance of mouse connexin45 gap junction channels is modulated by phosphorylation
    • van Veen TA, van Rijen HV, Jongsma HJ (2000) Electrical conductance of mouse connexin45 gap junction channels is modulated by phosphorylation. Cardiovasc Res 46:496-510
    • (2000) Cardiovasc Res , vol.46 , pp. 496-510
    • Van Veen, T.A.1    Van Rijen, H.V.2    Jongsma, H.J.3
  • 38
    • 0029854921 scopus 로고    scopus 로고
    • Crystallographic studies of the catalytic and a second site in fumarase C from Escherichia coli
    • Weaver T, Banaszak L (1996) Crystallographic studies of the catalytic and a second site in fumarase C from Escherichia coli. Biochemistry 35:13955-13965
    • (1996) Biochemistry , vol.35 , pp. 13955-13965
    • Weaver, T.1    Banaszak, L.2
  • 40
    • 0023909061 scopus 로고
    • Two biochemically distinct classes of fumarase in Escherichia coli
    • Woods SA, Schwartzbach SD, Guest JR (1988) Two biochemically distinct classes of fumarase in Escherichia coli. Biochim Biophys Acta 954:14-26
    • (1988) Biochim Biophys Acta , vol.954 , pp. 14-26
    • Woods, S.A.1    Schwartzbach, S.D.2    Guest, J.R.3
  • 41
    • 0036724705 scopus 로고    scopus 로고
    • Alternative and rescue treatment regimens for Helicobacter pylori eradication
    • Xia HH, Wong BC, Talley NJ, Lam SK (2002) Alternative and rescue treatment regimens for Helicobacter pylori eradication. Expert Opin Pharmacother 3:1301-1311
    • (2002) Expert Opin Pharmacother , vol.3 , pp. 1301-1311
    • Xia, H.H.1    Wong, B.C.2    Talley, N.J.3    Lam, S.K.4
  • 43
    • 77950553262 scopus 로고    scopus 로고
    • Fumarase: A mitochondrial metabolic enzyme and a cytosolic/nuclear component of the DNA damage response
    • Yogev O, Singer E, Shaulian E, Goldberg M, Fox TD, Pines O (2010) Fumarase: a mitochondrial metabolic enzyme and a cytosolic/nuclear component of the DNA damage response. PLoS Biol 8:e1000328
    • (2010) PLoS Biol , vol.8
    • Yogev, O.1    Singer, E.2    Shaulian, E.3    Goldberg, M.4    Fox, T.D.5    Pines, O.6
  • 44
    • 33747885475 scopus 로고    scopus 로고
    • Inhibition of urease by bismuth( III): Implications for the mechanisms of action of bismuth drugs
    • Zhang L, Mulrooney SB, Leung FK, Zeng YB, Ko BBC, Hausinger RP, Sun H (2006) Inhibition of urease by bismuth( III): implications for the mechanisms of action of bismuth drugs. Biometals 19:503-511
    • (2006) Biometals , vol.19 , pp. 503-511
    • Zhang, L.1    Mulrooney, S.B.2    Leung, F.K.3    Zeng, Y.B.4    Ko, B.B.C.5    Hausinger, R.P.6    Sun, H.7


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