메뉴 건너뛰기




Volumn 193, Issue 6, 2011, Pages 1359-1368

Effects of metal on the biochemical properties of Helicobacter pylori HypB, a maturation factor of [NiFe]-hydrogenase and urease

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; GUANOSINE TRIPHOSPHATASE; NICKEL IRON HYDROGENASE; PROTEIN HYPB; UNCLASSIFIED DRUG; UREASE;

EID: 79952385857     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.01333-10     Document Type: Article
Times cited : (33)

References (72)
  • 1
    • 7444271910 scopus 로고    scopus 로고
    • A high-performance liquid chromatography method for determining transition metal content in proteins
    • Atanassova, A., R. Lam, and D. B. Zamble. 2004. A high-performance liquid chromatography method for determining transition metal content in proteins. Anal. Biochem. 335:103-111.
    • (2004) Anal. Biochem. , vol.335 , pp. 103-111
    • Atanassova, A.1    Lam, R.2    Zamble, D.B.3
  • 2
    • 21844469960 scopus 로고    scopus 로고
    • Escherichia coli HypA is a zinc metalloprotein with a weak affinity for nickel
    • Atanassova, A., and D. B. Zamble. 2005. Escherichia coli HypA is a zinc metalloprotein with a weak affinity for nickel. J. Bacteriol. 187:4689-4697.
    • (2005) J. Bacteriol. , vol.187 , pp. 4689-4697
    • Atanassova, A.1    Zamble, D.B.2
  • 3
    • 0041559754 scopus 로고    scopus 로고
    • Dependence of Helicobacter pylori urease activity on the nickel-sequestering ability of the UreE accessory protein
    • Benoit, S., and R. J. Maier. 2003. Dependence of Helicobacter pylori urease activity on the nickel-sequestering ability of the UreE accessory protein. J. Bacteriol. 185:4787-4795.
    • (2003) J. Bacteriol. , vol.185 , pp. 4787-4795
    • Benoit, S.1    Maier, R.J.2
  • 5
    • 77954583264 scopus 로고    scopus 로고
    • Mutagenesis of Klebsiella aerogenes UreG to probe nickel binding and interactions with other Urease-related proteins
    • Boer, J. L., S. Quiroz-Valenzuela, K. L. Anderson, and R. P. Hausinger. 2010. Mutagenesis of Klebsiella aerogenes UreG to probe nickel binding and interactions with other Urease-related proteins. Biochemistry 49:5859-5869.
    • (2010) Biochemistry , vol.49 , pp. 5859-5869
    • Boer, J.L.1    Quiroz-Valenzuela, S.2    Anderson, K.L.3    Hausinger, R.P.4
  • 6
    • 0025010979 scopus 로고
    • The GTPase superfamily: A conserved switch for diverse cell functions
    • Bourne, H. R., D. A. Sanders, and F. McCormick. 1990. The GTPase superfamily: a conserved switch for diverse cell functions. Nature 348:125-132.
    • (1990) Nature , vol.348 , pp. 125-132
    • Bourne, H.R.1    Sanders, D.A.2    McCormick, F.3
  • 7
    • 0025830469 scopus 로고
    • A method to identify protein sequences that fold into a known three-dimensional structure
    • Bowie, J. U., R. Luthy, and D. Eisenberg. 1991. A method to identify protein sequences that fold into a known three-dimensional structure. Science 253:164-170. (Pubitemid 21917131)
    • (1991) Science , vol.253 , Issue.5016 , pp. 164-170
    • Bowie, J.U.1    Luthy, R.2    Eisenberg, D.3
  • 8
    • 54849406991 scopus 로고    scopus 로고
    • A high-affinity metal-binding peptide from Escherichia coli HypB
    • Chan Chung, K. C., et al. 2008. A high-affinity metal-binding peptide from Escherichia coli HypB. J. Am. Chem. Soc. 130:14056-14057.
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 14056-14057
    • Chan Chung, K.C.1
  • 9
    • 0003055099 scopus 로고    scopus 로고
    • Nickel-containing enzymes
    • I. Bertini, A. Sigel, and H. Sigel (ed.), Marcel Dekker, New York, NY
    • Ciurli, S., and S. Mangani. 2001. Nickel-containing enzymes, p. 669-707. In I. Bertini, A. Sigel, and H. Sigel (ed.), Handbook on metalloproteins. Marcel Dekker, New York, NY.
    • (2001) Handbook on Metalloproteins , pp. 669-707
    • Ciurli, S.1    Mangani, S.2
  • 10
    • 0027180507 scopus 로고
    • Verification of protein structures: patterns of nonbonded atomic interactions
    • Colovos, C., and T. O. Yeates. 1993. Verification of protein structures: patterns of nonbonded atomic interactions. Protein Sci. 2:1511-1519.
    • (1993) Protein Sci. , vol.2 , pp. 1511-1519
    • Colovos, C.1    Yeates, T.O.2
  • 11
    • 0033591290 scopus 로고    scopus 로고
    • Helicobacter pylori virulence and genetic geography
    • DOI 10.1126/science.284.5418.1328
    • Covacci, A., J. L. Telford, G. Del Giudice, J. Parsonnet, and R. Rappuoli. 1999. Helicobacter pylori virulence and genetic geography. Science 284:1328-1333. (Pubitemid 29289653)
    • (1999) Science , vol.284 , Issue.5418 , pp. 1328-1333
    • Covacci, A.1    Telford, J.L.2    Del, G.G.3    Parsonnet, J.4    Rappuoli, R.5
  • 12
    • 0035976958 scopus 로고    scopus 로고
    • Metal ion binding and coordination geometry for wild type and mutants of metallo-beta-lactamase from Bacillus cereus 569/H/9 (BcII)
    • de Seny, D., et al. 2001. Metal ion binding and coordination geometry for wild type and mutants of metallo-beta-lactamase from Bacillus cereus 569/H/9 (BcII) J. Biol. Chem. 276:45065-45078.
    • (2001) J. Biol. Chem. , vol.276 , pp. 45065-45078
    • De Seny, D.1
  • 13
    • 56249119177 scopus 로고    scopus 로고
    • Structural and biological analysis of the metal sites of Escherichia coli hydrogenase accessory protein HypB
    • Dias, A. V., et al. 2008. Structural and biological analysis of the metal sites of Escherichia coli hydrogenase accessory protein HypB. Biochemistry 47:11981-11991.
    • (2008) Biochemistry , vol.47 , pp. 11981-11991
    • Dias, A.V.1
  • 15
    • 0028122564 scopus 로고
    • Effect of gastric pH on urease-dependent colonization of gnotobiotic piglets by Helicobacter pylori
    • Eaton, K. A., and S. Krakowka. 1994. Effect of gastric pH on urease-dependent colonization of gnotobiotic piglets by Helicobacter pylori. Infect. Immun. 62:3604-3607.
    • (1994) Infect. Immun. , vol.62 , pp. 3604-3607
    • Eaton, K.A.1    Krakowka, S.2
  • 16
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera: A visualization system for exploratory research and analysis
    • Eric, F. P., et al. 2004. UCSF Chimera: a visualization system for exploratory research and analysis. J. Comp. Chem. 25:1605-1612.
    • (2004) J. Comp. Chem. , vol.25 , pp. 1605-1612
    • Eric, F.P.1
  • 17
    • 49649114605 scopus 로고    scopus 로고
    • Protein structure modeling with MODELLER
    • B. Kobe, M. Guss, and T. Huber (ed.), Humana Press, Totowa, NJ
    • Eswar, N., D. Eramian, B. Webb, M.-Y. Shen, and A. Sali. 2008. Protein structure modeling with MODELLER, p. 145-159. In B. Kobe, M. Guss, and T. Huber (ed.), Structural proteomics: high-throughput methods, vol. 426. Humana Press, Totowa, NJ.
    • (2008) Structural Proteomics: High-throughput Methods , vol.426 , pp. 145-159
    • Eswar, N.1    Eramian, D.2    Webb, B.3    Shen, M.-Y.4    Sali, A.5
  • 18
    • 0028911174 scopus 로고
    • HypB protein of Bradyrhizobium japonicum is a metal-binding GTPase capable of binding 18 divalent nickel ions per dimer
    • Fu, C., J. W. Olson, and R. J. Maier. 1995. HypB protein of Bradyrhizobium japonicum is a metal-binding GTPase capable of binding 18 divalent nickel ions per dimer. Proc. Natl. Acad. Sci. U. S. A. 92:2333-2337.
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 2333-2337
    • Fu, C.1    Olson, J.W.2    Maier, R.J.3
  • 19
    • 33748749374 scopus 로고    scopus 로고
    • Structural insights into HypB, a GTP-binding protein that regulates metal binding
    • Gasper, R., A. Scrima, and A. Wittinghofer. 2006. Structural insights into HypB, a GTP-binding protein that regulates metal binding. J. Biol. Chem. 281:27492-27502.
    • (2006) J. Biol. Chem. , vol.281 , pp. 27492-27502
    • Gasper, R.1    Scrima, A.2    Wittinghofer, A.3
  • 20
    • 0042915887 scopus 로고    scopus 로고
    • Metal and redox modulation of cysteine protein function
    • Giles, N. M., et al. 2003. Metal and redox modulation of cysteine protein function. Chem. Biol. 10:677-693.
    • (2003) Chem. Biol. , vol.10 , pp. 677-693
    • Giles, N.M.1
  • 21
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill, S. C., and P. H. von Hippel. 1989. Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182:319-326.
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 22
    • 33845916036 scopus 로고    scopus 로고
    • Metal-binding studies and EPR spectroscopy of the manganese transport regulator MntR
    • Golynskiy, M. V., W. A. Gunderson, M. P. Hendrich, and S. M. Cohen. 2006. Metal-binding studies and EPR spectroscopy of the manganese transport regulator MntR. Biochemistry 45:15359-15372.
    • (2006) Biochemistry , vol.45 , pp. 15359-15372
    • Golynskiy, M.V.1    Gunderson, W.A.2    Hendrich, M.P.3    Cohen, S.M.4
  • 23
    • 0036810021 scopus 로고    scopus 로고
    • Redox-regulated molecular chaperones
    • Graf, P. C. F., and U. Jakob. 2002. Redox-regulated molecular chaperones. Cell Mol. Life Sci. 59:1624-1631.
    • (2002) Cell Mol. Life Sci. , vol.59 , pp. 1624-1631
    • Graf, P.C.F.1    Jakob, U.2
  • 24
    • 70449732603 scopus 로고    scopus 로고
    • A subset of the diverse COG0523 family of putative metal chaperones is linked to zinc homeostasis in all kingdoms of life
    • Haas, C., et al. 2009. A subset of the diverse COG0523 family of putative metal chaperones is linked to zinc homeostasis in all kingdoms of life. BMC Genomics 10:470-491.
    • (2009) BMC Genomics , vol.10 , pp. 470-491
    • Haas, C.1
  • 25
    • 70449096096 scopus 로고    scopus 로고
    • Helicobacter pylori and gastric adenocarcinoma
    • Herrera, V., and J. Parsonnet. 2009. Helicobacter pylori and gastric adenocarcinoma. Clin. Microbiol. Infect. 15:971-976.
    • (2009) Clin. Microbiol. Infect. , vol.15 , pp. 971-976
    • Herrera, V.1    Parsonnet, J.2
  • 26
    • 0022051541 scopus 로고
    • The use of 4-(2-pyridylazo) resorcinol in studies of zinc release from Escherichia coli aspartate transcarbamoylase
    • Hunt, J. B., S. H. Neece, and A. Ginsburg. 1985. The use of 4-(2-pyridylazo) resorcinol in studies of zinc release from Escherichia coli aspartate transcarbamoylase. Anal. Biochem. 146:150-157.
    • (1985) Anal. Biochem. , vol.146 , pp. 150-157
    • Hunt, J.B.1    Neece, S.H.2    Ginsburg, A.3
  • 27
  • 28
    • 73149095411 scopus 로고    scopus 로고
    • CooC1 from Carboxydothermus hydrogenoformans is a nickel-binding ATPase
    • Jeoung, J.-H., T. Giese, M. Grunwald, and H. Dobbek. 2009. CooC1 from Carboxydothermus hydrogenoformans is a nickel-binding ATPase. Biochemistry 48:11505-11513.
    • (2009) Biochemistry , vol.48 , pp. 11505-11513
    • Jeoung, J.-H.1    Giese, T.2    Grunwald, M.3    Dobbek, H.4
  • 29
    • 77649270822 scopus 로고    scopus 로고
    • Crystal structure of the ATP-dependent maturation factor of Ni,Fe-containing carbon monoxide dehydrogenases
    • Jeoung, J.-H., T. Giese, M. Grünwald, and H. Dobbek. 2009. Crystal structure of the ATP-dependent maturation factor of Ni,Fe-containing carbon monoxide dehydrogenases. J. Mol. Biol. 396:1165-1179.
    • (2009) J. Mol. Biol. , vol.396 , pp. 1165-1179
    • Jeoung, J.-H.1    Giese, T.2    Grünwald, M.3    Dobbek, H.4
  • 31
    • 23444456924 scopus 로고    scopus 로고
    • How to study proteins by circular dichroism
    • Kelly, S. M., T. J. Jess, and N. C. Price. 2005. How to study proteins by circular dichroism. Biochim. Biophys. Acta 1751:119-139.
    • (2005) Biochim. Biophys. Acta , vol.1751 , pp. 119-139
    • Kelly, S.M.1    Jess, T.J.2    Price, N.C.3
  • 32
    • 33846043578 scopus 로고    scopus 로고
    • A dynamic Zn site in Helicobacter pylori HypA: A potential mechanism for metal-specific protein activity
    • Kennedy, D. C., R. W. Herbst, J. S. Iwig, P. T. Chivers, and M. J. Maroney. 2007. A dynamic Zn site in Helicobacter pylori HypA: a potential mechanism for metal-specific protein activity. J. Am. Chem. Soc. 129:16-17.
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 16-17
    • Kennedy, D.C.1    Herbst, R.W.2    Iwig, J.S.3    Chivers, P.T.4    Maroney, M.J.5
  • 33
    • 0029902679 scopus 로고    scopus 로고
    • Program DYNAFIT for the analysis of enzyme kinetic data: Application to HIV proteinase
    • Kuzmic, P. 1996. Program DYNAFIT for the analysis of enzyme kinetic data: application to HIV proteinase. Anal. Biochem. 237:260-273.
    • (1996) Anal. Biochem. , vol.237 , pp. 260-273
    • Kuzmic, P.1
  • 34
  • 35
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., M. W. MacArthur, D. S. Moss, and J. M. Thornton. 1993. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26:283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 36
    • 24644474525 scopus 로고    scopus 로고
    • Metal-binding activity of the Escherichia coli hydrogenase maturation factor HypB
    • Leach, M. R., S. Sandal, H. Sun, and D. B. Zamble. 2005. Metal-binding activity of the Escherichia coli hydrogenase maturation factor HypB. Biochemistry 44:12229-12238.
    • (2005) Biochemistry , vol.44 , pp. 12229-12238
    • Leach, M.R.1    Sandal, S.2    Sun, H.3    Zamble, D.B.4
  • 37
    • 34047134687 scopus 로고    scopus 로고
    • Metallocenter assembly of the hydrogenase enzymes
    • Leach, M. R., and D. B. Zamble. 2007. Metallocenter assembly of the hydrogenase enzymes. Curr. Opin. Chem. Biol. 11:159-165.
    • (2007) Curr. Opin. Chem. Biol. , vol.11 , pp. 159-165
    • Leach, M.R.1    Zamble, D.B.2
  • 38
    • 0036295212 scopus 로고    scopus 로고
    • Classification and evolution of P-loop GTPases and related ATPases
    • Leipe, D. D., Y. I. Wolf, E. V. Koonin, and L. Aravind. 2002. Classification and evolution of P-loop GTPases and related ATPases. J. Mol. Biol. 317:41-72.
    • (2002) J. Mol. Biol. , vol.317 , pp. 41-72
    • Leipe, D.D.1    Wolf, Y.I.2    Koonin, E.V.3    Aravind, L.4
  • 39
    • 0003482420 scopus 로고
    • 2nd ed., Elsevier Science B.V., Amsterdam, Netherlands
    • Lever, A. B. P. 1984. Inorganic electronic spectroscopy, 2nd ed., vol. 33. Elsevier Science B.V., Amsterdam, Netherlands.
    • (1984) Inorganic Electronic Spectroscopy , vol.33
    • Lever, A.B.P.1
  • 40
    • 70350680999 scopus 로고    scopus 로고
    • Nickel homeostasis and nickel regulation: An overview
    • Li, Y., and D. B. Zamble. 2009. Nickel homeostasis and nickel regulation: an overview. Chem. Rev. 109:4617-4643.
    • (2009) Chem. Rev. , vol.109 , pp. 4617-4643
    • Li, Y.1    Zamble, D.B.2
  • 41
    • 0026610767 scopus 로고
    • Assessment of protein models with three-dimensional profiles
    • Luthy, R., J. U. Bowie, and D. Eisenberg. 1992. Assessment of protein models with three-dimensional profiles. Nature 356:83-85.
    • (1992) Nature , vol.356 , pp. 83-85
    • Luthy, R.1    Bowie, J.U.2    Eisenberg, D.3
  • 42
    • 25844494381 scopus 로고    scopus 로고
    • Comparative protein structure modeling
    • J. M. Walker (ed.), Humana Press, Totowa, NJ
    • Madhusudhan, M. S., et al. 2005. Comparative protein structure modeling, p. 831-860. In J. M. Walker (ed.), The proteomics protocols handbook. Humana Press, Totowa, NJ.
    • (2005) The Proteomics Protocols Handbook , pp. 831-860
    • Madhusudhan, M.S.1
  • 43
    • 34248656478 scopus 로고    scopus 로고
    • Nickel-binding and accessory proteins facilitating Ni-enzyme maturation in Helicobacter pylori
    • DOI 10.1007/s10534-006-9061-8, Biometals: function and transport in bacteria, fungi, and humans
    • Maier, R. J., S. Benoit, and S. Seshadri. 2007. Nickel-binding and accessory proteins facilitating Ni-enzyme maturation in Helicobacter pylori. Biometals 20:655-664. (Pubitemid 46776575)
    • (2007) BioMetals , vol.20 , Issue.3-4 , pp. 655-664
    • Maier, R.J.1    Benoit, S.L.2    Seshadri, S.3
  • 44
    • 0027450599 scopus 로고
    • The product of the hypB gene, which is required for nickel incorporation into hydrogenases, is a novel guanine nucleotide-binding protein
    • Maier, T., A. Jacobi, M. Sauter, and A. Böck. 1993. The product of the hypB gene, which is required for nickel incorporation into hydrogenases, is a novel guanine nucleotide-binding protein. J. Bacteriol. 175:630-635. (Pubitemid 23046922)
    • (1993) Journal of Bacteriology , vol.175 , Issue.3 , pp. 630-635
    • Maier, T.1    Jacobi, A.2    Sauter, M.3    Bock, A.4
  • 45
    • 0029054222 scopus 로고
    • GTP hydrolysis by HypB is essential for nickel insertion into hydrogenases of Escherichia coli
    • Maier, T., F. Lottspeich, and A. Bock. 1995. GTP hydrolysis by HypB is essential for nickel insertion into hydrogenases of Escherichia coli. Eur. J. Biochem. 230:133-138.
    • (1995) Eur. J. Biochem. , vol.230 , pp. 133-138
    • Maier, T.1    Lottspeich, F.2    Bock, A.3
  • 46
    • 70249086988 scopus 로고    scopus 로고
    • Fluorescent probes for the structure and function of metallothionein
    • Maret, W. 2009. Fluorescent probes for the structure and function of metallothionein. J. Chromatogr. B Anal. Technol. Biomed. Life Sci. 877:3378-3383.
    • (2009) J. Chromatogr. B Anal. Technol. Biomed. Life Sci. , vol.877 , pp. 3378-3383
    • Maret, W.1
  • 47
    • 0141681866 scopus 로고    scopus 로고
    • Roles of conserved nucleotide-binding domains in accessory proteins, HypB and UreG, in the maturation of nickel-enzymes required for efficient Helicobacter pylori colonization
    • Mehta, N., S. Benoit, and R. J. Maier. 2003. Roles of conserved nucleotide-binding domains in accessory proteins, HypB and UreG, in the maturation of nickel-enzymes required for efficient Helicobacter pylori colonization. Microb. Pathog. 35:229-234.
    • (2003) Microb. Pathog. , vol.35 , pp. 229-234
    • Mehta, N.1    Benoit, S.2    Maier, R.J.3
  • 48
    • 0037307747 scopus 로고    scopus 로고
    • Characterization of Helicobacter pylori nickel metabolism accessory proteins needed for maturation of both urease and hydrogenase
    • Mehta, N., J. W. Olson, and R. J. Maier. 2003. Characterization of Helicobacter pylori nickel metabolism accessory proteins needed for maturation of both urease and hydrogenase. J. Bacteriol. 185:726-734.
    • (2003) J. Bacteriol. , vol.185 , pp. 726-734
    • Mehta, N.1    Olson, J.W.2    Maier, R.J.3
  • 49
    • 33749578940 scopus 로고    scopus 로고
    • Statistical potential for assessment and prediction of protein structures
    • Min-yi, S., and S. Andrej. 2006. Statistical potential for assessment and prediction of protein structures. Protein Sci. 15:2507-2524.
    • (2006) Protein Sci. , vol.15 , pp. 2507-2524
    • Min-yi, S.1    Andrej, S.2
  • 51
    • 0002377269 scopus 로고    scopus 로고
    • Urease
    • S. L. Hazell, G. L. Mendz, and H. L. T. Mobley (ed.), ASM Press, Washington, DC
    • Mobley, H. L. T. 2001. Urease, p. 179-191. In S. L. Hazell, G. L. Mendz, and H. L. T. Mobley (ed.), Helicobacter pylori: physiology and genetics. ASM Press, Washington, DC.
    • (2001) Helicobacter Pylori: Physiology and Genetics , pp. 179-191
    • Mobley, H.L.T.1
  • 52
    • 0024206251 scopus 로고
    • Kinetic analysis of the hydrolysis of GTP by p21N-ras. The basal GTPase mechanism
    • Neal, S. E., J. F. Eccleston, A. Hall, and M. R. Webb. 1988. Kinetic analysis of the hydrolysis of GTP by p21N-ras. The basal GTPase mechanism. J. Biol. Chem. 263:19718-19722.
    • (1988) J. Biol. Chem. , vol.263 , pp. 19718-19722
    • Neal, S.E.1    Eccleston, J.F.2    Hall, A.3    Webb, M.R.4
  • 53
    • 0034053033 scopus 로고    scopus 로고
    • Dual roles of Bradyrhizobium japonicum nickelin protein in nickel storage and GTP-dependent Ni mobilization
    • Olson, J. W., and R. J. Maier. 2000. Dual roles of Bradyrhizobium japonicum nickelin protein in nickel storage and GTP-dependent Ni mobilization. J. Bacteriol. 182:1702-1705.
    • (2000) J. Bacteriol. , vol.182 , pp. 1702-1705
    • Olson, J.W.1    Maier, R.J.2
  • 54
    • 0037195612 scopus 로고    scopus 로고
    • Molecular hydrogen as an energy source for Helicobacter pylori
    • Olson, J. W., and R. J. Maier. 2002. Molecular hydrogen as an energy source for Helicobacter pylori. Science 298:1788-1790.
    • (2002) Science , vol.298 , pp. 1788-1790
    • Olson, J.W.1    Maier, R.J.2
  • 55
    • 0035191007 scopus 로고    scopus 로고
    • Requirement of nickel metabolism proteins HypA and HypB for full activity of both hydrogenase and urease in Helicobacter pylori
    • Olson, J. W., N. S. Mehta, and R. J. Maier. 2001. Requirement of nickel metabolism proteins HypA and HypB for full activity of both hydrogenase and urease in Helicobacter pylori. Mol. Microbiol. 39:176-182.
    • (2001) Mol. Microbiol. , vol.39 , pp. 176-182
    • Olson, J.W.1    Mehta, N.S.2    Maier, R.J.3
  • 56
  • 57
    • 0028102344 scopus 로고
    • Purification of Rhizobium leguminosarum HypB, a nickel-binding protein required for hydrogenase synthesis
    • Rey, L., J. Imperial, J. M. Palacios, and T. Ruiz-Argueso. 1994. Purification of Rhizobium leguminosarum HypB, a nickel-binding protein required for hydrogenase synthesis. J. Bacteriol. 176:6066-6073. (Pubitemid 24309946)
    • (1994) Journal of Bacteriology , vol.176 , Issue.19 , pp. 6066-6073
    • Rey, L.1    Imperial, J.2    Palacios, J.-M.3    Ruiz-Argueso, T.4
  • 58
    • 0027136282 scopus 로고
    • Comparative protein modeling by satisfaction of spatial restraints
    • Sali, A., and T. L. Blundell. 1993. Comparative protein modeling by satisfaction of spatial restraints. J. Mol. Biol. 234:779-815.
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 59
    • 0031961778 scopus 로고    scopus 로고
    • The role of internal urease in acid resistance of Helicobacter pylori
    • DOI 10.1016/S0016-5085(98)70633-X
    • Scott, D. R., et al. 1998. The role of internal urease in acid resistance of Helicobacter pylori. Gastroenterol. 114:58-70. (Pubitemid 28020955)
    • (1998) Gastroenterology , vol.114 , Issue.1 , pp. 58-70
    • Scott, D.R.1    Weeks, D.2    Hong, C.3    Postius, S.4    Melchers, K.5    Sachs, G.6
  • 60
    • 77955689110 scopus 로고    scopus 로고
    • Crystal structures of apo and metal-bound forms of the UreE protein from Helicobacter pylori: Role of multiple metal binding sites
    • Shi, R., et al. 2010. Crystal structures of apo and metal-bound forms of the UreE protein from Helicobacter pylori: role of multiple metal binding sites. Biochemistry 49:7080-7088.
    • (2010) Biochemistry , vol.49 , pp. 7080-7088
    • Shi, R.1
  • 61
    • 0027337975 scopus 로고
    • 2+ ion concentration with the fluorescent probe mag-fura-2 (furaptra)
    • 2+ ion concentration with the fluorescent probe mag-fura-2 (furaptra). J. Biochem. Biophys. Methods 27:25-37.
    • (1993) J. Biochem. Biophys. Methods , vol.27 , pp. 25-37
    • Simons, T.J.B.1
  • 62
    • 0027490731 scopus 로고
    • Recognition of errors in three-dimensional structures of proteins
    • DOI 10.1002/prot.340170404
    • Sippl, M. J. 1993. Recognition of errors in three-dimensional structures of proteins. Proteins 17:355-362. (Pubitemid 23358545)
    • (1993) Proteins: Structure, Function and Genetics , vol.17 , Issue.4 , pp. 355-362
    • Sippl, M.J.1
  • 63
    • 0030920782 scopus 로고    scopus 로고
    • G protein mechanisms: Insights from structural analysis
    • Sprang, S. R. 1997. G protein mechanisms: insights from structural analysis. Annu. Rev. Biochem. 66:639-678.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 639-678
    • Sprang, S.R.1
  • 64
    • 56849102578 scopus 로고    scopus 로고
    • In vivo interactome of Helicobacter pylori urease revealed by tandem affinity purification
    • Stingl, K., et al. 2008. In vivo interactome of Helicobacter pylori urease revealed by tandem affinity purification. Mol. Cell Proteom. 7:2429-2441.
    • (2008) Mol. Cell Proteom. , vol.7 , pp. 2429-2441
    • Stingl, K.1
  • 67
    • 35748974830 scopus 로고    scopus 로고
    • Occurrence, classification, and biological function of hydrogenases: An overview
    • Vignais, P. M., and B. Billoud. 2007. Occurrence, classification, and biological function of hydrogenases: an overview. Chem. Rev. 107:4206-4272.
    • (2007) Chem. Rev. , vol.107 , pp. 4206-4272
    • Vignais, P.M.1    Billoud, B.2
  • 68
    • 70350728386 scopus 로고    scopus 로고
    • Crystal structure of HypA, a nickel-binding metallochaperone for [NiFe] hydrogenase maturation
    • Watanabe, S., et al. 2009. Crystal structure of HypA, a nickel-binding metallochaperone for [NiFe] hydrogenase maturation. J. Mol. Biol. 394:448-459.
    • (2009) J. Mol. Biol. , vol.394 , pp. 448-459
    • Watanabe, S.1
  • 69
    • 67651221840 scopus 로고    scopus 로고
    • Structure of a nickel chaperone, HypA, from Helicobacter pylori reveals two distinct metal binding sites
    • Xia, W., H. Li, K.-H. Sze, and H. Sun. 2009. Structure of a nickel chaperone, HypA, from Helicobacter pylori reveals two distinct metal binding sites. J. Am. Chem. Soc. 131:10031-10040.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 10031-10040
    • Xia, W.1    Li, H.2    Sze, K.-H.3    Sun, H.4
  • 71
    • 58949095956 scopus 로고    scopus 로고
    • Zn(II)- linked dimerization of UreG from Helicobacter pylori, a chaperone involved in nickel trafficking and urease activation
    • Zambelli, B., P. Turano, F. Musiani, P. Neyroz, and S. Ciurli. 2009. Zn(II)- linked dimerization of UreG from Helicobacter pylori, a chaperone involved in nickel trafficking and urease activation. Proteins 74:222-239.
    • (2009) Proteins , vol.74 , pp. 222-239
    • Zambelli, B.1    Turano, P.2    Musiani, F.3    Neyroz, P.4    Ciurli, S.5
  • 72
    • 64649090344 scopus 로고    scopus 로고
    • Cysteine oxidation regulates the RNA-binding activity of iron regulatory protein 2
    • Zumbrennen, K. B., M. L. Wallander, S. J. Romney, and E. A. Leibold. 2009. Cysteine oxidation regulates the RNA-binding activity of iron regulatory protein 2. Mol. Cell. Biol. 29:2219-2229.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 2219-2229
    • Zumbrennen, K.B.1    Wallander, M.L.2    Romney, S.J.3    Leibold, E.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.