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Volumn 94, Issue 12, 2008, Pages 5053-5064

Structure of the cytosolic part of the subunit b-dimer of Escherichia coli F0F1-ATP synthase

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN SUBUNIT; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE;

EID: 45849114753     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1529/biophysj.107.121038     Document Type: Article
Times cited : (13)

References (85)
  • 1
    • 0031008228 scopus 로고    scopus 로고
    • The ATP synthase - a splendid molecular machine
    • Boyer, P. D. 1997. The ATP synthase - a splendid molecular machine. Annu. Rev. Biochem. 66:717-749.
    • (1997) Annu. Rev. Biochem , vol.66 , pp. 717-749
    • Boyer, P.D.1
  • 2
    • 0037085010 scopus 로고    scopus 로고
    • The molecular mechanism of ATP synthesis by F1F0-ATP synthase
    • Senior, A. E., S. Nadanaciva, and J. Weber. 2002. The molecular mechanism of ATP synthesis by F1F0-ATP synthase. Biochim. Biophys. Acta. 1553:188-211.
    • (2002) Biochim. Biophys. Acta , vol.1553 , pp. 188-211
    • Senior, A.E.1    Nadanaciva, S.2    Weber, J.3
  • 3
  • 4
    • 0030724471 scopus 로고    scopus 로고
    • The subunit delta-subunit b domain of the Escherichia coli F1F0 ATPase. The b subunits interact with F1 as a dimer and through the delta subunit
    • Rodgers, A. J., S. Wilkens, R. Aggeler, M. B. Morris, S. M. Howitt, and R. A. Capaldi. 1997. The subunit delta-subunit b domain of the Escherichia coli F1F0 ATPase. The b subunits interact with F1 as a dimer and through the delta subunit. J. Biol. Chem. 272:31058-31064.
    • (1997) J. Biol. Chem , vol.272 , pp. 31058-31064
    • Rodgers, A.J.1    Wilkens, S.2    Aggeler, R.3    Morris, M.B.4    Howitt, S.M.5    Capaldi, R.A.6
  • 5
    • 0032502352 scopus 로고    scopus 로고
    • Characterization of a b2delta complex from Escherichia coli ATP synthase
    • Dunn, S. D., and J. Chandler. 1998. Characterization of a b2delta complex from Escherichia coli ATP synthase. J. Biol. Chem. 273:8646-8651.
    • (1998) J. Biol. Chem , vol.273 , pp. 8646-8651
    • Dunn, S.D.1    Chandler, J.2
  • 7
    • 2642707545 scopus 로고    scopus 로고
    • ATP synthase's second stalk comes into focus
    • Wilkens, S., and R. A. Capaldi. 1998. ATP synthase's second stalk comes into focus. Nature. 393:29.
    • (1998) Nature , vol.393 , pp. 29
    • Wilkens, S.1    Capaldi, R.A.2
  • 8
    • 0038715067 scopus 로고    scopus 로고
    • Direct interaction of subunits a and b of the F0 complex of Escherichia coli ATP synthase by forming an ab2 subcomplex
    • Stalz, W., J. Greie, G. Deckers-Hebestreit, and K. Altendorf. 2003. Direct interaction of subunits a and b of the F0 complex of Escherichia coli ATP synthase by forming an ab2 subcomplex. J. Biol. Chem. 278:27068-27071.
    • (2003) J. Biol. Chem , vol.278 , pp. 27068-27071
    • Stalz, W.1    Greie, J.2    Deckers-Hebestreit, G.3    Altendorf, K.4
  • 9
    • 0034737966 scopus 로고    scopus 로고
    • A model for the structure of subunit a of the Escherichia coli ATP synthase and its role in proton translocation
    • Vik, S. B., J. C. Long, T. Wada, and D. Zhang. 2000. A model for the structure of subunit a of the Escherichia coli ATP synthase and its role in proton translocation. Biochim. Biophys. Acta. 1458:457-466.
    • (2000) Biochim. Biophys. Acta , vol.1458 , pp. 457-466
    • Vik, S.B.1    Long, J.C.2    Wada, T.3    Zhang, D.4
  • 10
    • 0037458716 scopus 로고    scopus 로고
    • Aqueous access channels in subunit a of rotary ATP synthase
    • Angevine, C. M., and R. H. Fillingame. 2003. Aqueous access channels in subunit a of rotary ATP synthase. J. Biol. Chem. 278:6066-6074.
    • (2003) J. Biol. Chem , vol.278 , pp. 6066-6074
    • Angevine, C.M.1    Fillingame, R.H.2
  • 11
    • 0037809269 scopus 로고    scopus 로고
    • Close proximity of a cytoplasmic loop of subunit a with c subunits of the ATP synthase from Escherichia coli
    • Zhang, D., and S. B. Vik. 2003. Close proximity of a cytoplasmic loop of subunit a with c subunits of the ATP synthase from Escherichia coli. J. Biol. Chem. 278:12319-12324.
    • (2003) J. Biol. Chem , vol.278 , pp. 12319-12324
    • Zhang, D.1    Vik, S.B.2
  • 13
    • 0032947857 scopus 로고    scopus 로고
    • Transient accumulation of elastic energy in proton translocating ATP synthase
    • Cherepanov, D. A., A. Y. Mulkidjanian, and W. Junge. 1999. Transient accumulation of elastic energy in proton translocating ATP synthase. FEBS Lett. 449:1-6.
    • (1999) FEBS Lett , vol.449 , pp. 1-6
    • Cherepanov, D.A.1    Mulkidjanian, A.Y.2    Junge, W.3
  • 14
    • 0033609010 scopus 로고    scopus 로고
    • ATP synthase and other motor proteins
    • Junge, W. 1999. ATP synthase and other motor proteins. Proc. Natl. Acad. Sci. USA. 96:4735-4737.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 4735-4737
    • Junge, W.1
  • 15
    • 0028114231 scopus 로고
    • Structure at 2.8 Å resolution of F1-ATPase from bovine heart mitochondria
    • Abrahams, J. P., A. G. Leslie, R. Lutter, and J. E. Walker. 1994. Structure at 2.8 Å resolution of F1-ATPase from bovine heart mitochondria. Nature. 370:621-628.
    • (1994) Nature , vol.370 , pp. 621-628
    • Abrahams, J.P.1    Leslie, A.G.2    Lutter, R.3    Walker, J.E.4
  • 17
    • 0041819514 scopus 로고    scopus 로고
    • The structure of bovine F1-ATPase in complex with its regulatory protein IF1
    • Cabezón, E., M. G. Montgomery, A. G. W. Leslie, and J. E. Walker. 2003. The structure of bovine F1-ATPase in complex with its regulatory protein IF1. Nat. Struct. Biol. 10:744-750.
    • (2003) Nat. Struct. Biol , vol.10 , pp. 744-750
    • Cabezón, E.1    Montgomery, M.G.2    Leslie, A.G.W.3    Walker, J.E.4
  • 18
    • 7144224771 scopus 로고    scopus 로고
    • The crystal structure of the nucleotide-free alpha 3 beta 3 subcomplex of F1-ATPase from the thermophilic Bacillus PS3 is a symmetric trimer
    • Shirakihara, Y., A. G. Leslie, J. P. Abrahams, J. E. Walker, T. Ueda, Y. Sekimoto, M. Kambara, K. Saika, Y. Kagawa, and M. Yoshida. 1997. The crystal structure of the nucleotide-free alpha 3 beta 3 subcomplex of F1-ATPase from the thermophilic Bacillus PS3 is a symmetric trimer. Structure. 5:825-836.
    • (1997) Structure , vol.5 , pp. 825-836
    • Shirakihara, Y.1    Leslie, A.G.2    Abrahams, J.P.3    Walker, J.E.4    Ueda, T.5    Sekimoto, Y.6    Kambara, M.7    Saika, K.8    Kagawa, Y.9    Yoshida, M.10
  • 19
    • 0032529839 scopus 로고    scopus 로고
    • The 2.8-Å structure of rat liver F1-ATPase: Configuration of a critical intermediate in ATP synthesis/hydrolysis
    • Bianchet, M. A., J. Hullihen, P. L. Pedersen, and L. M. Amzel. 1998. The 2.8-Å structure of rat liver F1-ATPase: configuration of a critical intermediate in ATP synthesis/hydrolysis. Proc. Natl. Acad. Sci. USA. 95:11065-11070.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 11065-11070
    • Bianchet, M.A.1    Hullihen, J.2    Pedersen, P.L.3    Amzel, L.M.4
  • 20
    • 0033607504 scopus 로고    scopus 로고
    • Molecular architecture of the rotary motor in ATP synthase
    • Stock, D., A. G. Leslie, and J. E. Walker. 1999. Molecular architecture of the rotary motor in ATP synthase. Science. 286:1700-1705.
    • (1999) Science , vol.286 , pp. 1700-1705
    • Stock, D.1    Leslie, A.G.2    Walker, J.E.3
  • 21
    • 0028970620 scopus 로고
    • Structural features of the epsilon subunit of the Escherichia coli ATP synthase determined by NMR spectroscopy
    • Wilkens, S., F. W. Dahlquist, L. P. McIntosh, L. W. Donaldson, and R. A. Capaldi. 1995. Structural features of the epsilon subunit of the Escherichia coli ATP synthase determined by NMR spectroscopy. Nat. Struct. Biol. 2:961-967.
    • (1995) Nat. Struct. Biol , vol.2 , pp. 961-967
    • Wilkens, S.1    Dahlquist, F.W.2    McIntosh, L.P.3    Donaldson, L.W.4    Capaldi, R.A.5
  • 22
    • 0031055743 scopus 로고    scopus 로고
    • Solution structure of the N-terminal domain of the delta subunit of the E. coli ATP synthase
    • Wilkens, S., S. D. Dunn, J. Chandler, F. W. Dahlquist, and R. A. Capaldi. 1997. Solution structure of the N-terminal domain of the delta subunit of the E. coli ATP synthase. Nat. Struct. Biol. 4:198-201.
    • (1997) Nat. Struct. Biol , vol.4 , pp. 198-201
    • Wilkens, S.1    Dunn, S.D.2    Chandler, J.3    Dahlquist, F.W.4    Capaldi, R.A.5
  • 23
    • 0030611634 scopus 로고    scopus 로고
    • Crystal structure of the epsilon subunit of the proton-translocating ATP synthase from Escherichia coli
    • Uhlin, U., G. B. Cox, and J. M. Guss. 1997. Crystal structure of the epsilon subunit of the proton-translocating ATP synthase from Escherichia coli. Structure. 5:1219-1230.
    • (1997) Structure , vol.5 , pp. 1219-1230
    • Uhlin, U.1    Cox, G.B.2    Guss, J.M.3
  • 24
    • 0037457911 scopus 로고    scopus 로고
    • Helix packing in subunit a of the Escherichia coli ATP synthase as determined by chemical labeling and proteolysis of the cysteine-substituted protein
    • Zhang, D., and S. B. Vik. 2003. Helix packing in subunit a of the Escherichia coli ATP synthase as determined by chemical labeling and proteolysis of the cysteine-substituted protein. Biochemistry. 42:331-337.
    • (2003) Biochemistry , vol.42 , pp. 331-337
    • Zhang, D.1    Vik, S.B.2
  • 25
    • 0021756359 scopus 로고    scopus 로고
    • 19. The unc operon. Nucleotide sequence, regulation and structure of ATP-synthase
    • Walker, J. E., M. Saraste, and N. J. Gay. 19. The unc operon. Nucleotide sequence, regulation and structure of ATP-synthase. Biochim. Biophys. Acta. 768:164-200.
    • Biochim. Biophys. Acta , vol.768 , pp. 164-200
    • Walker, J.E.1    Saraste, M.2    Gay, N.J.3
  • 26
    • 0026655905 scopus 로고
    • The polar domain of the b subunit of Escherichia coli F1F0-ATPase forms an elongated dimer that interacts with the F1 sector
    • Dunn, S. D. 1992. The polar domain of the b subunit of Escherichia coli F1F0-ATPase forms an elongated dimer that interacts with the F1 sector. J. Biol. Chem. 267:7630-7636.
    • (1992) J. Biol. Chem , vol.267 , pp. 7630-7636
    • Dunn, S.D.1
  • 29
    • 0034032665 scopus 로고    scopus 로고
    • Secondary structure composition of reconstituted subunit b of the Escherichia coli ATP synthase
    • Greie, J. C., G. Deckers-Hebestreit, and K. Altendorf. 2000. Secondary structure composition of reconstituted subunit b of the Escherichia coli ATP synthase. Eur. J. Biochem. 267:3040-3048.
    • (2000) Eur. J. Biochem , vol.267 , pp. 3040-3048
    • Greie, J.C.1    Deckers-Hebestreit, G.2    Altendorf, K.3
  • 31
    • 0030826421 scopus 로고    scopus 로고
    • Dimerization interactions of the b subunit of the Escherichia coli F1F0-ATPase
    • McLachlin, D. T., and S. D. Dunn. 1997. Dimerization interactions of the b subunit of the Escherichia coli F1F0-ATPase. J. Biol. Chem. 272:21233-21239.
    • (1997) J. Biol. Chem , vol.272 , pp. 21233-21239
    • McLachlin, D.T.1    Dunn, S.D.2
  • 34
    • 0037188394 scopus 로고    scopus 로고
    • The "second stalk" of Escherichia coli ATP synthase: Structure of the isolated dimerization domain
    • Del Rizzo, P. A., Y. Bi, S. D. Dunn, and B. H. Shilton. 2002. The "second stalk" of Escherichia coli ATP synthase: structure of the isolated dimerization domain. Biochemistry. 41:6875-68.
    • (2002) Biochemistry , vol.41 , pp. 6875-6968
    • Del Rizzo, P.A.1    Bi, Y.2    Dunn, S.D.3    Shilton, B.H.4
  • 35
    • 33750951013 scopus 로고    scopus 로고
    • ATP synthase b subunit dimerization domain: A right-handed coiled coil with offset helices
    • Del Rizzo, P. A., Y. Bi, and S. D. Dunn. 2006. ATP synthase b subunit dimerization domain: a right-handed coiled coil with offset helices. J. Mol. Biol. 364:735-746.
    • (2006) J. Mol. Biol , vol.364 , pp. 735-746
    • Del Rizzo, P.A.1    Bi, Y.2    Dunn, S.D.3
  • 36
    • 20444460846 scopus 로고    scopus 로고
    • Distances between the b-subunits in the tether domain of F0F1-ATP synthase from E. coli
    • Steigmiller, S., M. Börsch, P. Gräber, and M. Huber. 2005. Distances between the b-subunits in the tether domain of F0F1-ATP synthase from E. coli. Biochim. Biophys. Acta. 1708:143-153.
    • (2005) Biochim. Biophys. Acta , vol.1708 , pp. 143-153
    • Steigmiller, S.1    Börsch, M.2    Gräber, P.3    Huber, M.4
  • 37
    • 0032561169 scopus 로고    scopus 로고
    • Deletions in the second stalk of F1F0-ATP synthase in Escherichia coli
    • Sorgen, P. L., T. L. Caviston, R. C. Perry, and B. D. Cain. 1998. Deletions in the second stalk of F1F0-ATP synthase in Escherichia coli. J. Biol. Chem. 273:27873-27878.
    • (1998) J. Biol. Chem , vol.273 , pp. 27873-27878
    • Sorgen, P.L.1    Caviston, T.L.2    Perry, R.C.3    Cain, B.D.4
  • 39
    • 0041816462 scopus 로고    scopus 로고
    • Integration of b subunits of unequal lengths into F1F0-ATP synthase
    • Grabar, T. B., and B. D. Cain. 2003. Integration of b subunits of unequal lengths into F1F0-ATP synthase. J. Biol. Chem. 278:34751-34756.
    • (2003) J. Biol. Chem , vol.278 , pp. 34751-34756
    • Grabar, T.B.1    Cain, B.D.2
  • 40
    • 3843142876 scopus 로고    scopus 로고
    • Genetic complementation between mutant b subunits in F1F0 ATP synthase
    • Grabar, T. B., and B. D. Cain. 2004. Genetic complementation between mutant b subunits in F1F0 ATP synthase. J. Biol. Chem. 279:31205-31211.
    • (2004) J. Biol. Chem , vol.279 , pp. 31205-31211
    • Grabar, T.B.1    Cain, B.D.2
  • 41
    • 20044373685 scopus 로고    scopus 로고
    • Manipulating the length of the b subunit F1 binding domain in F1F0 ATP synthase from Escherichia coli
    • Bhatt, D., S. P. Cole, T. B. Grabar, S. B. Claggett, and B. D. Cain. 2005. Manipulating the length of the b subunit F1 binding domain in F1F0 ATP synthase from Escherichia coli. J. Bioenerg. Biomembr. 37:67-74.
    • (2005) J. Bioenerg. Biomembr , vol.37 , pp. 67-74
    • Bhatt, D.1    Cole, S.P.2    Grabar, T.B.3    Claggett, S.B.4    Cain, B.D.5
  • 42
    • 34547642853 scopus 로고    scopus 로고
    • Functional incorporation of chimeric b subunits into F1F0 ATP synthase
    • Claggett, S. B., T. B. Grabar, S. D. Dunn, and B. D. Cain. 2007. Functional incorporation of chimeric b subunits into F1F0 ATP synthase. J. Bacteriol. 189:5463-5471.
    • (2007) J. Bacteriol , vol.189 , pp. 5463-5471
    • Claggett, S.B.1    Grabar, T.B.2    Dunn, S.D.3    Cain, B.D.4
  • 44
    • 33745713048 scopus 로고    scopus 로고
    • The peripheral stalk of the mitochondrial ATP synthase
    • Walker, J. E., and V. K. Dickson. 2006. The peripheral stalk of the mitochondrial ATP synthase. Biochim. Biophys. Acta. 1757:286-296.
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 286-296
    • Walker, J.E.1    Dickson, V.K.2
  • 45
    • 33748986212 scopus 로고    scopus 로고
    • ATP synthase: Subunit-subunit interactions in the stator stalk
    • Weber, J. 2006. ATP synthase: subunit-subunit interactions in the stator stalk. Biochim. Biophys. Acta. 1757:1162-1170.
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 1162-1170
    • Weber, J.1
  • 46
    • 33846658425 scopus 로고    scopus 로고
    • ATP synthase - the structure of the stator stalk
    • Weber, J. 2007. ATP synthase - the structure of the stator stalk. Trends Biochem. Sci. 32:53-56.
    • (2007) Trends Biochem. Sci , vol.32 , pp. 53-56
    • Weber, J.1
  • 47
    • 0038376003 scopus 로고    scopus 로고
    • Identification of the F1-binding surface on the delta-subunit of ATP synthase
    • Weber, J., S. Wilke-Mounts, and A. E. Senior. 2003. Identification of the F1-binding surface on the delta-subunit of ATP synthase. J. Biol. Chem. 278:13409-13416.
    • (2003) J. Biol. Chem , vol.278 , pp. 13409-13416
    • Weber, J.1    Wilke-Mounts, S.2    Senior, A.E.3
  • 48
    • 0034603824 scopus 로고    scopus 로고
    • Site-directed spin-labeling of the catalytic sites yields insight into structural changes within the F0F1-ATP synthase of Escherichia coli
    • Kersten, M. V., S. D. Dunn, J. G. Wise, and P. D. Vogel. 2000. Site-directed spin-labeling of the catalytic sites yields insight into structural changes within the F0F1-ATP synthase of Escherichia coli. Biochemistry. 39:3856-3860.
    • (2000) Biochemistry , vol.39 , pp. 3856-3860
    • Kersten, M.V.1    Dunn, S.D.2    Wise, J.G.3    Vogel, P.D.4
  • 49
    • 10344239938 scopus 로고    scopus 로고
    • The subunit b dimer of the F0F1-ATP synthase: Interaction with F1-ATPase as deduced by site-specific spin-labeling
    • Motz, C., T. Hornung, M. Kersten, D. T. McLachlin, S. D. Dunn, J. G. Wise, and P. D. Vogel. 2004. The subunit b dimer of the F0F1-ATP synthase: interaction with F1-ATPase as deduced by site-specific spin-labeling. J. Biol. Chem. 279:49074-49081.
    • (2004) J. Biol. Chem , vol.279 , pp. 49074-49081
    • Motz, C.1    Hornung, T.2    Kersten, M.3    McLachlin, D.T.4    Dunn, S.D.5    Wise, J.G.6    Vogel, P.D.7
  • 50
    • 0023833907 scopus 로고
    • Synthesis of a photoaffinity-spin-labeled derivative of ATP and its first application to F1-ATPase
    • Vogel-Claude, P., G. Schäfer, and W. E. Trommer. 1988. Synthesis of a photoaffinity-spin-labeled derivative of ATP and its first application to F1-ATPase. FEBS Lett. 227:107-109.
    • (1988) FEBS Lett , vol.227 , pp. 107-109
    • Vogel-Claude, P.1    Schäfer, G.2    Trommer, W.E.3
  • 51
    • 0026710622 scopus 로고
    • Nucleotide binding sites on mitochondrial F1-ATPase. Electron spin resonance spectroscopy and photolabeling by azido-spin-labeled adenine nucleotides support an adenylate kinase-like orientation
    • Vogel, P. D., J. H. Nett, H. E. Sauer, K. Schmadel, R. L. Cross, and W. E. Trommer. 1992. Nucleotide binding sites on mitochondrial F1-ATPase. Electron spin resonance spectroscopy and photolabeling by azido-spin-labeled adenine nucleotides support an adenylate kinase-like orientation. J. Biol. Chem. 267:11982-11986.
    • (1992) J. Biol. Chem , vol.267 , pp. 11982-11986
    • Vogel, P.D.1    Nett, J.H.2    Sauer, H.E.3    Schmadel, K.4    Cross, R.L.5    Trommer, W.E.6
  • 52
    • 0028242357 scopus 로고
    • Effects of magnesium ions on the relative conformation of nucleotide binding sites of F1-ATPases as studied by electron spin resonance spectroscopy
    • Burgard, S., J. H. Nett, H. E. Sauer, Y. Kagawa, H. J. Schäfer, J. G. Wise, P. D. Vogel, and W. E. Trommer. 1994. Effects of magnesium ions on the relative conformation of nucleotide binding sites of F1-ATPases as studied by electron spin resonance spectroscopy. J. Biol. Chem. 269:17815-17819.
    • (1994) J. Biol. Chem , vol.269 , pp. 17815-17819
    • Burgard, S.1    Nett, J.H.2    Sauer, H.E.3    Kagawa, Y.4    Schäfer, H.J.5    Wise, J.G.6    Vogel, P.D.7    Trommer, W.E.8
  • 53
    • 0040642598 scopus 로고    scopus 로고
    • Asymmetry of catalytic but not of noncatalytic sites on Escherichia coli F1-ATPase in solution as observed using electron spin resonance spectroscopy
    • Lösel, R. M., A. H. Erbes, J. H. Nett, J. G. Wise, G. Berger, G. Girault, and P. D. Vogel. 1996. Asymmetry of catalytic but not of noncatalytic sites on Escherichia coli F1-ATPase in solution as observed using electron spin resonance spectroscopy. Spectrochimica Acta. Part A. 52:73-83.
    • (1996) Spectrochimica Acta. Part A , vol.52 , pp. 73-83
    • Lösel, R.M.1    Erbes, A.H.2    Nett, J.H.3    Wise, J.G.4    Berger, G.5    Girault, G.6    Vogel, P.D.7
  • 54
    • 0029816271 scopus 로고    scopus 로고
    • Nucleotide binding to the heat-shock protein DnaK as studied by ESR spectroscopy
    • Neuhofen, S., H. Theyssen, J. Reinstein, W. E. Trommer, and P. D. Vogel. 1996. Nucleotide binding to the heat-shock protein DnaK as studied by ESR spectroscopy. Eur. J. Biochem. 240:78-82.
    • (1996) Eur. J. Biochem , vol.240 , pp. 78-82
    • Neuhofen, S.1    Theyssen, H.2    Reinstein, J.3    Trommer, W.E.4    Vogel, P.D.5
  • 55
    • 0031029890 scopus 로고    scopus 로고
    • Asymmetry of catalytic but not of noncatalytic sites on Escherichia coli F1-ATPase in solution as observed using electron spin resonance spectroscopy
    • Lösel, R. M., J. G. Wise, and P. D. Vogel. 1997. Asymmetry of catalytic but not of noncatalytic sites on Escherichia coli F1-ATPase in solution as observed using electron spin resonance spectroscopy. Biochemistry. 36:1188-1193.
    • (1997) Biochemistry , vol.36 , pp. 1188-1193
    • Lösel, R.M.1    Wise, J.G.2    Vogel, P.D.3
  • 57
    • 0030831356 scopus 로고    scopus 로고
    • Nucleotide hydrolysis-dependent conformational changes in p21(ras) as studied using ESR spectroscopy
    • Haller, M., U. Hoffmann, T. Schanding, R. S. Goody, and P. D. Vogel. 1997. Nucleotide hydrolysis-dependent conformational changes in p21(ras) as studied using ESR spectroscopy. J. Biol. Chem. 272:30103-30107.
    • (1997) J. Biol. Chem , vol.272 , pp. 30103-30107
    • Haller, M.1    Hoffmann, U.2    Schanding, T.3    Goody, R.S.4    Vogel, P.D.5
  • 58
    • 2442435773 scopus 로고    scopus 로고
    • Association of alpha-subunits with nucleotide-modified beta-subunits induces asymmetry in the catalytic sites of the F1-ATPase alpha3beta3-hexamer
    • Burgard, S., M. Harada, Y. Kagawa, W. E. Trommer, and P. D. Vogel. 2003. Association of alpha-subunits with nucleotide-modified beta-subunits induces asymmetry in the catalytic sites of the F1-ATPase alpha3beta3-hexamer. Cell Biochem. Biophys. 39:175-181.
    • (2003) Cell Biochem. Biophys , vol.39 , pp. 175-181
    • Burgard, S.1    Harada, M.2    Kagawa, Y.3    Trommer, W.E.4    Vogel, P.D.5
  • 59
    • 27144547163 scopus 로고    scopus 로고
    • Nucleotide binding to the multidrug resistance P-glycoprotein as studied by ESR spectroscopy
    • Delannoy, S., I. L. Urbatsch, G. Tombline, A. E. Senior, and P. D. Vogel. 2005. Nucleotide binding to the multidrug resistance P-glycoprotein as studied by ESR spectroscopy. Biochemistry. 44:14010-14019.
    • (2005) Biochemistry , vol.44 , pp. 14010-14019
    • Delannoy, S.1    Urbatsch, I.L.2    Tombline, G.3    Senior, A.E.4    Vogel, P.D.5
  • 60
    • 33747097488 scopus 로고    scopus 로고
    • Insights into the regulation of the ryanodine receptor: Differential effects of Mg2+ and Ca2+ on ATP binding
    • Dias, J. M., C. Szegedi, I. Jóna, and P. D. Vogel. 2006. Insights into the regulation of the ryanodine receptor: differential effects of Mg2+ and Ca2+ on ATP binding. Biochemistry. 45:9408-9415.
    • (2006) Biochemistry , vol.45 , pp. 9408-9415
    • Dias, J.M.1    Szegedi, C.2    Jóna, I.3    Vogel, P.D.4
  • 61
    • 0343906129 scopus 로고
    • Photoaffinity spin labeling
    • R. Zhdanov, editor. Springer, Berlin, Germany
    • Trommer, W. E., and P. D. Vogel. 1992. Photoaffinity spin labeling. In: Bioactive Spin Labels. R. Zhdanov, editor. Springer, Berlin, Germany. 405-427.
    • (1992) Bioactive Spin Labels , pp. 405-427
    • Trommer, W.E.1    Vogel, P.D.2
  • 62
    • 0034530610 scopus 로고    scopus 로고
    • Insights into ATP synthase structure and function using affinity and site-specific spin labeling
    • Vogel, P. D. 2000. Insights into ATP synthase structure and function using affinity and site-specific spin labeling. J. Bioenerg. Biomembr. 32:413-421.
    • (2000) J. Bioenerg. Biomembr , vol.32 , pp. 413-421
    • Vogel, P.D.1
  • 63
    • 0034705529 scopus 로고    scopus 로고
    • A thermodynamic coupling mechanism for the disaggregation of a model peptide substrate by chaperone secB
    • Panse, V. G., P. Vogel, W. E. Trommer, and R. Varadarajan. 2000. A thermodynamic coupling mechanism for the disaggregation of a model peptide substrate by chaperone secB. J. Biol. Chem. 275:18698-18703.
    • (2000) J. Biol. Chem , vol.275 , pp. 18698-18703
    • Panse, V.G.1    Vogel, P.2    Trommer, W.E.3    Varadarajan, R.4
  • 64
    • 0035823523 scopus 로고    scopus 로고
    • Electron spin resonance and fluorescence studies of the bound-state conformation of a model protein substrate to the chaperone SecB
    • Panse, V. G., K. Beena, R. Philipp, W. E. Trommer, P. D. Vogel, and R. Varadarajan. 2001. Electron spin resonance and fluorescence studies of the bound-state conformation of a model protein substrate to the chaperone SecB. J. Biol. Chem. 276:33681-33688.
    • (2001) J. Biol. Chem , vol.276 , pp. 33681-33688
    • Panse, V.G.1    Beena, K.2    Philipp, R.3    Trommer, W.E.4    Vogel, P.D.5    Varadarajan, R.6
  • 65
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 66
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 67
    • 33646127590 scopus 로고    scopus 로고
    • Dipolar coupling between nitroxide spin labels: The development and application of a tether-in-a-cone model
    • Hustedt, E. J., R. A. Stein, L. Sethaphong, S. Brandon, Z. Zhou, and S. C. Desensi. 2006. Dipolar coupling between nitroxide spin labels: the development and application of a tether-in-a-cone model. Biophys. J. 90:340-356.
    • (2006) Biophys. J , vol.90 , pp. 340-356
    • Hustedt, E.J.1    Stein, R.A.2    Sethaphong, L.3    Brandon, S.4    Zhou, Z.5    Desensi, S.C.6
  • 68
    • 0029115328 scopus 로고
    • Determination of the distance between two spin labels attached to a macromolecule
    • Rabenstein, M. D., and Y. K. Shin. 1995. Determination of the distance between two spin labels attached to a macromolecule. Proc. Natl. Acad. Sci. USA. 92:8239-8243.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8239-8243
    • Rabenstein, M.D.1    Shin, Y.K.2
  • 69
    • 0030781782 scopus 로고    scopus 로고
    • Determination of interspin distances between spin labels attached to insulin: Comparison of electron paramagnetic resonance data with the x-ray structure
    • Steinhoff, H. J., N. Radzwill, W. Thevis, V. Lenz, D. Brandenburg, A. Antson, G. Dodson, and A. Wollmer. 1997. Determination of interspin distances between spin labels attached to insulin: comparison of electron paramagnetic resonance data with the x-ray structure. Biophys. J. 73:3287-3298.
    • (1997) Biophys. J , vol.73 , pp. 3287-3298
    • Steinhoff, H.J.1    Radzwill, N.2    Thevis, W.3    Lenz, V.4    Brandenburg, D.5    Antson, A.6    Dodson, G.7    Wollmer, A.8
  • 71
    • 0034029447 scopus 로고    scopus 로고
    • The effect of isodensity surface sampling on ESP derived charges and the effect of adding bondcenters on DMA derived charges
    • Schaftenaar, G., and J. H. Noordik. 2000. The effect of isodensity surface sampling on ESP derived charges and the effect of adding bondcenters on DMA derived charges. J. Comput. Aided Mol. Des. 14:233-242.
    • (2000) J. Comput. Aided Mol. Des , vol.14 , pp. 233-242
    • Schaftenaar, G.1    Noordik, J.H.2
  • 72
    • 0035983171 scopus 로고    scopus 로고
    • Structural determination of spin label immobilization and orientation: A Monte Carlo minimization approach
    • Sale, K., C. Sár, K. A. Sharp, K. Hideg, and P. G. Fajer. 2002. Structural determination of spin label immobilization and orientation: a Monte Carlo minimization approach. J. Magn. Reson. 156:104-112.
    • (2002) J. Magn. Reson , vol.156 , pp. 104-112
    • Sale, K.1    Sár, C.2    Sharp, K.A.3    Hideg, K.4    Fajer, P.G.5
  • 73
    • 0030040323 scopus 로고    scopus 로고
    • Reduced surface: An efficient way to compute molecular surfaces
    • Sanner, M. F., A. J. Olson, and J. C. Spehner. 1996. Reduced surface: an efficient way to compute molecular surfaces. Biopolymers. 38:305-320.
    • (1996) Biopolymers , vol.38 , pp. 305-320
    • Sanner, M.F.1    Olson, A.J.2    Spehner, J.C.3
  • 74
    • 32144456009 scopus 로고    scopus 로고
    • Paircoil2: Improved prediction of coiled coils from sequence
    • McDonnell, A. V., T. Jiang, A. E. Keating, and B. Berger. 2006. Paircoil2: improved prediction of coiled coils from sequence. Bioinformatics. 22:356-358.
    • (2006) Bioinformatics , vol.22 , pp. 356-358
    • McDonnell, A.V.1    Jiang, T.2    Keating, A.E.3    Berger, B.4
  • 75
    • 0030987407 scopus 로고    scopus 로고
    • MultiCoil: A program for predicting two- and three-stranded coiled coils
    • Wolf, E., P. S. Kim, and B. Berger. 1997. MultiCoil: a program for predicting two- and three-stranded coiled coils. Protein Sci. 6:1179-1189.
    • (1997) Protein Sci , vol.6 , pp. 1179-1189
    • Wolf, E.1    Kim, P.S.2    Berger, B.3
  • 76
    • 0029878720 scopus 로고    scopus 로고
    • Humphrey, W., A. Dalke and K. Schulten. 1996. VMD: visual molecular dynamics. J. Mol. Graph. 14:33-38, 27-28.
    • Humphrey, W., A. Dalke and K. Schulten. 1996. VMD: visual molecular dynamics. J. Mol. Graph. 14:33-38, 27-28.
  • 77
    • 0003885069 scopus 로고
    • Addison-Wesley Professional, Upper Saddle River, NJ
    • Ousterhout, J. C. 1994. Tcl and the Tk Toolkit. Addison-Wesley Professional, Upper Saddle River, NJ.
    • (1994) Tcl and the Tk Toolkit
    • Ousterhout, J.C.1
  • 78
    • 0033397980 scopus 로고    scopus 로고
    • Python: A programming language for software integration and development
    • Sanner, M. F. 1999. Python: a programming language for software integration and development. J. Mol. Graph. Model. 17:57-61.
    • (1999) J. Mol. Graph. Model , vol.17 , pp. 57-61
    • Sanner, M.F.1
  • 82
    • 0000920828 scopus 로고
    • The packing of alpha-helices: Simple coiled-coils
    • Crick, F. H. C. 1953. The packing of alpha-helices: simple coiled-coils. Acta Crystallogr. 6:689-697.
    • (1953) Acta Crystallogr , vol.6 , pp. 689-697
    • Crick, F.H.C.1
  • 83
    • 0029957901 scopus 로고    scopus 로고
    • Heptad breaks in alpha-helical coiled coils: Stutters and stammers
    • Brown, J. H., C. Cohen, and D. A. Parry. 1996. Heptad breaks in alpha-helical coiled coils: stutters and stammers. Proteins. 26:134-145.
    • (1996) Proteins , vol.26 , pp. 134-145
    • Brown, J.H.1    Cohen, C.2    Parry, D.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.