메뉴 건너뛰기




Volumn 44, Issue 3, 2011, Pages 311-356

Structural divergence of the rotary ATPases

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE;

EID: 79960112075     PISSN: 00335835     EISSN: 14698994     Source Type: Journal    
DOI: 10.1017/S0033583510000338     Document Type: Article
Times cited : (115)

References (298)
  • 1
    • 0028114231 scopus 로고
    • Structure at 2-8 A resolution of F1-ATPase from bovine heart mitochondria
    • ABRAHAMS, J. P., LESLIE, A. G., LUTTER, R. & WALKER, J. E. (1994). Structure at 2-8 A 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
  • 2
    • 43849085010 scopus 로고    scopus 로고
    • The elastic properties of the structurally characterized Myosin II S2 subdomain: A molecular dynamics and normal mode analysis
    • ADAMOVIC, I., MIJAILOVICH, S. M. & KARPLUS, M. (2008). The elastic properties of the structurally characterized Myosin II S2 subdomain: a molecular dynamics and normal mode analysis. BiophysicalJournal94, 3779-3789.
    • (2008) BiophysicalJournal94 , pp. 3779-3789
    • Adamovic, I.1    Mijailovich, S.M.2    Karplus, M.3
  • 3
    • 0031202120 scopus 로고    scopus 로고
    • 0-ATP synthase complex
    • DOI 10.1074/jbc.272.31.19621
    • AGGELER, R., OGILVIE, I. & CAPALDI, R. (1997). Rotation of the gamma-epsilon subunit domain in the Escherichia coli F1F0-ATP synthase complex. Journal of Biological Chemistry 272, 19621-19624. (Pubitemid 27337767)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.31 , pp. 19621-19624
    • Aggeler, R.1    Ogilvie, I.2    Capaldi, R.A.3
  • 4
    • 0037458716 scopus 로고    scopus 로고
    • Aqueous access channels in subunit a of rotary ATP synthase
    • DOI 10.1074/jbc.M210199200
    • ANGEVINE, C. M. & FILLINGAME, R. H. (2003). Aqueous access channels in subunit a of rotary ATP synthase. Journal ofBiological Chemistry 278, 6066-6074. (Pubitemid 36800858)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.8 , pp. 6066-6074
    • Angevine, C.M.1    Fillingame, R.H.2
  • 5
    • 34247877574 scopus 로고    scopus 로고
    • Aqueous access pathways in ATP synthase subunit a: Reactivity of cysteine substituted into transmembrane helices 1, 3, and 5
    • DOI 10.1074/jbc.M610848200
    • ANGEVINE, C. M., HEROLD, K. A. G., VINCENT, O. D. & FILLINGAME, R. H. (2007). Aqueous access pathways in ATP synthase subunit a - Reactivity of cysteine substituted into transmembrane helices 1, 3, and 5. Journal of Biological Chemistry 282, 9001-9007. (Pubitemid 47093514)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.12 , pp. 9001-9007
    • Angevine, C.M.1    Herold, K.A.G.2    Vincent, O.D.3    Fillingame, R.H.4
  • 6
    • 0023930674 scopus 로고
    • Topography and subunit stoichiometry of the coated vesicle proton pump
    • ARAI, A., TERRES, G., PINK, S. & FORGAC, M. (1988). Topography and subunit stoichiometry of the coated vesicle proton pump. Journal of Biological Chemistry 263, 8796-8802.
    • (1988) Journal of Biological Chemistry , vol.263 , pp. 8796-8802
    • Arai, A.1    Terres, G.2    Pink, S.3    Forgac, M.4
  • 7
    • 0036479217 scopus 로고    scopus 로고
    • +-ATPase
    • DOI 10.1074/jbc.M109967200
    • ARATA, Y., BALEJA, J. D. & FORGAC, M. (2002). Cysteine-directed cross-linking to subunit B suggests that subunit E forms part of the peripheral stalk of the vacuolar H -ATPase. Journal of Biological Chemistry 277, 3357-3363. (Pubitemid 34953203)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.5 , pp. 3357-3363
    • Arata, Y.1    Baleja, J.D.2    Forgac, M.3
  • 8
    • 34548503612 scopus 로고    scopus 로고
    • 1-ATPase rotates by an asymmetric, sequential mechanism using all three catalytic subunits
    • DOI 10.1038/nsmb1296, PII NSMB1296
    • ARIGA, T., MUNEYUKI, E. & YOSHIDA, M. (2007). F1-ATPase rotates by an asymmetric, sequential mechanism using all three catalytic subunits. Nature Structural and Molecular Biology 14, 841-846. (Pubitemid 47373838)
    • (2007) Nature Structural and Molecular Biology , vol.14 , Issue.9 , pp. 841-846
    • Ariga, T.1    Muneyuki, E.2    Yoshida, M.3
  • 9
    • 0032534790 scopus 로고    scopus 로고
    • 0-ATP synthase exists as a dimer: Identification of three dimer-specific subunits
    • DOI 10.1093/emboj/17.24.7170
    • ARNOLD, I., PFEIFFER, K., NEUPERT, W., STUART, R. A. & SCHAGGER, H. (1998). Yeast mitochondrial F1F0-ATP synthase exists as a dimer: identification of three dimer-specific subunits. EMBO Journal 17, 7170-7178. (Pubitemid 29002686)
    • (1998) EMBO Journal , vol.17 , Issue.24 , pp. 7170-7178
    • Arnold, I.1    Pfeiffer, K.2    Neupert, W.3    Stuart, R.A.4    Schagger, H.5
  • 10
    • 0038070570 scopus 로고    scopus 로고
    • The GxxxG motif of the transmembrane domain of subunit e is involved in the dimerization/oligomerization of the yeast ATP synthase complex in the mitochondrial membrane
    • DOI 10.1046/j.1432-1033.2003.03557.x
    • ARSELIN, G., GIRAUD, M. F., DAUTANT, A., VAILLIER, J., BRETHES, D., COULARY-SALIN, B., SCHAEFFER, J. & VELOURS, J. (2003). The GxxxG motif of the transmembrane domain of subunit e is involved in the di-merization/ oligomerization of the yeast ATP synthase complex in the mitochondrial membrane. European Journal of Biochemisty 270, 1875-1884. (Pubitemid 36532545)
    • (2003) European Journal of Biochemistry , vol.270 , Issue.8 , pp. 1875-1884
    • Arselin, G.1    Giraud, M.-F.2    Dautant, A.3    Vaillier, J.4    Brethes, D.5    Coulary-Salin, B.6    Schaeffer, J.7    Velours, J.8
  • 11
    • 42649144152 scopus 로고    scopus 로고
    • Angle determination for side views in single particle electron mi-croscopy
    • BAKER, L. A. & RUBINSTEIN, J. L. (2008). Angle determination for side views in single particle electron mi-croscopy. Journal of Structural Biology. 162, 468-477.
    • (2008) Journal of Structural Biology , vol.162 , pp. 468-477
    • Baker, L.A.1    Rubinstein, J.L.2
  • 12
    • 64049091511 scopus 로고    scopus 로고
    • Constant c(10) ring stoichiometry in the Escherichia coli ATP synthase analyzed by cross-linking
    • BALLHAUSEN, B., ALTENDORF, K. & DECKERS-HEBESTREIT, G. (2009). Constant c(10) ring stoichiometry in the Escherichia coli ATP synthase analyzed by cross-linking. Journal of Bacteriology 191, 2400-2404.
    • (2009) Journal of Bacteriology , vol.191 , pp. 2400-2404
    • Ballhausen, B.1    Altendorf, K.2    Deckers-Hebestreit, G.3
  • 13
    • 1542297711 scopus 로고    scopus 로고
    • The ionic track in the F1-ATPase from the thermophilic bacillus PS3
    • DOI 10.1021/bi036058i
    • BANDYOPADHYAY, S. & ALLISON, W. S. (2004). The ionic track in the F1-ATPase from the thermophilic bacillus PS3. Biochemistry 43, 2533-2540. (Pubitemid 38327848)
    • (2004) Biochemistry , vol.43 , Issue.9 , pp. 2533-2540
    • Bandyopadhyay, S.1    Allison, W.S.2
  • 14
    • 0027319652 scopus 로고
    • +-ATPase membrane sector
    • BAUERLE, C., HO, M. N., LINDORFER, M.A. & STEVENS, T. H. (1993). The Saccharomyces cerevisiae VMA6 gene encodes the 36-kDa subunit of the vacuolar H(+)-ATPase membrane sector. Journal of Biological Chemistry 268, 12749-12757. (Pubitemid 23182443)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.17 , pp. 12749-12757
    • Bauerle, C.1    Ho, M.N.2    Lindorfer, M.A.3    Stevens, T.H.4
  • 15
    • 0029786323 scopus 로고    scopus 로고
    • Membrane topography and near-neighbor relationships of the mitochondrial ATP synthase subunits e, f, and g
    • DOI 10.1074/jbc.271.34.20340
    • BELOGRUDOV, G. I., TOMICH, J. M. & HATEFI, Y. (1996). Membrane topography and near-neighbor relationships of the mitochondrial ATP synthase subunits e, f, and g. Journal of Biological Chemistry 271, 20340-20345. (Pubitemid 26281800)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.34 , pp. 20340-20345
    • Belogrudov, G.I.1    Tomich, J.M.2    Hatefi, Y.3
  • 16
    • 0026768406 scopus 로고
    • The membrane sector of vacuolar H(+)-ATPase by itself is impermeable to protons
    • BÉLTRAN, C. & NELSON, N. (1992). The membrane sector of vacuolar H(+)-ATPase by itself is impermeable to protons. Acta Physiologica Scandinavica 607, 41-47.
    • (1992) Acta Physiologica Scandinavica , vol.607 , pp. 41-47
    • Béltran, C.1    Nelson, N.2
  • 17
    • 4644290116 scopus 로고    scopus 로고
    • +-ATPase/synthase by electron microscopy
    • DOI 10.1016/j.str.2004.07.017, PII S0969212604002862
    • BERNAL, R. A. & STOCK, D. (2004). Three-dimensional structure of the intact Thermus thermophilus H+-ATPase/synthase by electron microscopy. Structure 12, 1789-1798. (Pubitemid 39298963)
    • (2004) Structure , vol.12 , Issue.10 , pp. 1789-1798
    • Bernal, R.A.1    Stock, D.2
  • 18
    • 0028659872 scopus 로고
    • Analysis of transient structures by cryo-microscopy combined with rapid mixing of spray droplets
    • DOI 10.1016/0304-3991(94)90012-4
    • BERRIMAN, J. & UNWIN, N. (1994). Analysis of transient structures by cryo-microscopy combined with rapid mixing of spray droplets. Ultramicroscopy 56, 241-252. (Pubitemid 24377118)
    • (1994) Ultramicroscopy , vol.56 , Issue.4 , pp. 241-252
    • Berriman, J.1    Unwin, N.2
  • 20
    • 33847620721 scopus 로고    scopus 로고
    • 0 ATP synthase from Methanocaldococcus jannaschii and its binding to the catalytic A subunit
    • DOI 10.1021/bi062123n
    • BIUKOVIC, G., ROSSLE, M., GAYEN, S., MU, Y. & GRÜBER, G. (2007). Small-angle X-ray scattering reveals the solution structure of the peripheral stalk subunit H of the A1A0 ATP synthase from Methanocaldococcus jannaschii and its binding to the catalytic A subunit. Biochemistry 46, 2070-2078. (Pubitemid 46355318)
    • (2007) Biochemistry , vol.46 , Issue.8 , pp. 2070-2078
    • Biukovic, G.1    Rossle, M.2    Gayen, S.3    Mu, Y.4    Gruber, G.5
  • 21
    • 0024461376 scopus 로고
    • Osteoclastic bone resorption by a polarized vacuolar proton pump
    • BLAIR, H. C., TEITELBAUM, S. L., GHISELLI, R. & GLUCK, S. (1989). Osteoclastic bone resorption by a polarized vacuolar proton pump. Science 245, 855-857. (Pubitemid 19223662)
    • (1989) Science , vol.245 , Issue.4920 , pp. 855-857
    • Blair, H.C.1    Teitelbaum, S.L.2    Ghiselli, R.3    Gluck, S.4
  • 24
    • 61349192268 scopus 로고    scopus 로고
    • The Ras/cAMP/protein kinase A pathway regulates glucose-dependent assembly of the vacuolar (H+)-ATPase in yeast
    • BOND, A. & FORGAC, M. (2008). The Ras/cAMP/protein kinase A pathway regulates glucose-dependent assembly of the vacuolar (H+)-ATPase in yeast. Journal of Biological Chemistry 283, 36513-36521.
    • (2008) Journal of Biological Chemistry , vol.283 , pp. 36513-36521
    • Bond, A.1    Forgac, M.2
  • 25
    • 0034681280 scopus 로고    scopus 로고
    • Direct visualisation of conformational changes in EFQF! by electron microscopy
    • BOTTCHER, B., BERTSCHE, I., REUTER, R. & GRABER, P. (2000). Direct visualisation of conformational changes in EFQF! by electron microscopy. Journal of Molecular Biology 296, 449-457.
    • (2000) Journal of Molecular Biology , vol.296 , pp. 449-457
    • Bottcher, B.1    Bertsche, I.2    Reuter, R.3    Graber, P.4
  • 26
    • 0034738114 scopus 로고    scopus 로고
    • +-ATP synthase from chloroplasts and its subcomplexes as revealed by electron microscopy
    • DOI 10.1016/S0005-2728(00)00090-6, PII S0005272800000906
    • BOTTCHER, B. & GRABER, P. (2000). The structure of the H+ -ATP synthase from chloroplasts and its sub-complexes as revealed by electron microscopy. Biochimica et Biophysica Acta - Bioenergetics 1458, 404-416. (Pubitemid 30320721)
    • (2000) Biochimica et Biophysica Acta - Bioenergetics , vol.1458 , Issue.2-3 , pp. 404-416
    • Bottcher, B.1    Graber, P.2
  • 27
    • 0032483462 scopus 로고    scopus 로고
    • 1
    • DOI 10.1006/jmbi.1998.1957
    • BOTTCHER, B., SCHWARZ, L. & GRABER, P. (1998). Direct indication for the existence of a double stalk in CFF. Journal of Molecular Biology 281, 757-762. (Pubitemid 28408426)
    • (1998) Journal of Molecular Biology , vol.281 , Issue.5 , pp. 757-762
    • Bottcher, B.1    Schwarz, L.2    Graber, P.3
  • 29
    • 34347226731 scopus 로고    scopus 로고
    • 1-ATPase from bovine heart mitochondria at 1.9 Å resolution
    • DOI 10.1074/jbc.M700203200
    • BOWLER, M. W., MONTGOMERY, M. G., LESLIE, A. G. & WALKER, J. E. (2007). Ground state structure of Fr ATPase from bovine heart mitochondria at 1-9 A resolution. Journal of Biological Chemistry 282, 14238-14242. (Pubitemid 47100445)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.19 , pp. 14238-14242
    • Bowler, M.W.1    Montgomery, M.G.2    Leslie, A.G.W.3    Walker, J.E.4
  • 30
    • 0037040244 scopus 로고    scopus 로고
    • Mutations in subunit c of the vacuolar ATPase confer resistance to bafilomycin and identify a conserved antibiotic binding site
    • DOI 10.1074/jbc.M109756200
    • BOWMAN, B.J. & BOWMAN, E.J. (2002). Mutations in sub-unit c of the vacuolar ATPase confer resistance to bafi-lomycin and identify a conserved antibiotic binding site. Journal of Biological Chemistry 277, 3965-3972. (Pubitemid 34968650)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.6 , pp. 3965-3972
    • Bowman, B.J.1    Bowman, E.J.2
  • 32
    • 0031008228 scopus 로고    scopus 로고
    • The ATP synthase - A splendid molecular machine
    • DOI 10.1146/annurev.biochem.66.1.717
    • BOYER, P. D. (1997). The ATP synthase - a splendid molecular machine. Annual Review of Biochemistry. 66, 717-749. (Pubitemid 27274672)
    • (1997) Annual Review of Biochemistry , vol.66 , pp. 717-749
    • Boyer, P.D.1
  • 33
    • 0029898733 scopus 로고    scopus 로고
    • Acidification of the male reproductive tract by a proton pumping (H +)-ATPase
    • BRETON, S., SMITH, P.J. S., LUI, B. & BROWN, D. (1996). Acidification of the male reproductive tract by a proton pumping (H +)-ATPase. Nature Medicine 2, 470-472.
    • (1996) Nature Medicine , vol.2 , pp. 470-472
    • Breton, S.1    Smith, P.J.S.2    Lui, B.3    Brown, D.4
  • 34
    • 0023571839 scopus 로고
    • +ATPase
    • BROWN, D., GLUCK, S. & HARTWIG, J. (1987). Structure of the novel membrane-coating material in proton-secreting epithelial cells and identification as an H+ATPase. Journal of Cell Biology 105, 1637-1648. (Pubitemid 18023378)
    • (1987) Journal of Cell Biology , vol.105 , Issue.4 , pp. 1637-1648
    • Brown, D.1    Gluck, S.2    Hartwig, J.3
  • 35
    • 66449088593 scopus 로고    scopus 로고
    • Regulation of the V-ATPase in kidney epithelial cells: Dual role in acid-base homeostasis and vesicle trafficking
    • BROWN, D., PAUNESCU, T. G., BRETON, S. & MARSHANSKY, V. (2009). Regulation of the V-ATPase in kidney epithelial cells: dual role in acid-base homeostasis and vesicle trafficking. Journal of Experimental Biology 212, 1762-1772.
    • (2009) Journal of Experimental Biology , vol.212 , pp. 1762-1772
    • Brown, D.1    Paunescu, T.G.2    Breton, S.3    Marshansky, V.4
  • 36
    • 4143130167 scopus 로고    scopus 로고
    • Rotor/stator interactions of the ε subunit in Escherichia coli ATP synthase and implications for enzyme regulation
    • DOI 10.1074/jbc.M405012200
    • BULYGIN, V. V., DUNCAN, T. M. & CROSS, R L. (2004). Rotor/stator interactions of the epsilon subunit in Escherichia coli ATP synthase and implications for enzyme regulation. Journal of Biological Chemistry 279, 35616-35621. (Pubitemid 39100563)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.34 , pp. 35616-35621
    • Bulygin, V.V.1    Duncan, T.M.2    Cross, R.L.3
  • 37
    • 23844521281 scopus 로고    scopus 로고
    • The modification of the conserved GXXXG motif of the membrane-spanning segment of subunit g destabilizes the supramolecular species of yeast ATP synthase
    • DOI 10.1074/jbc.M502140200
    • BUSTOS, D. M. & VELOURS, J. (2005). The modification of the conserved GXXXG motif of the membrane-spanning segment of subunit g destabilizes the supra-molecular species of yeast ATP synthase. Journal of Biological Chemistry 280, 29004-29010. (Pubitemid 41161348)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.32 , pp. 29004-29010
    • Bustos, D.M.1    Velours, J.2
  • 39
    • 0034353297 scopus 로고    scopus 로고
    • 0 stator subunits
    • DOI 10.1023/A:1005575919638
    • CAIN, B. D. (2000). Mutagenic analysis of the F0 stator subunits. Journal of Bioenergetics and Biomembranes 32, 365-371. (Pubitemid 32001400)
    • (2000) Journal of Bioenergetics and Biomembranes , vol.32 , Issue.4 , pp. 365-371
    • Cain, B.D.1
  • 40
    • 0024977998 scopus 로고
    • 0ATPase of Escherichia coli. Mutagenic analysis of the a subunit
    • CAIN, B. D. & SIMONI, R. D. (1989). Proton translocation by the F1F0ATPase of Escherichia coli. Mutagenic analysis of the a subunit. Journal of Biological Chemistry 264, 3292-3300.
    • (1989) Journal of Biological Chemistry , vol.264 , pp. 3292-3300
    • Cain, B.D.1    Simoni, R.D.2
  • 42
    • 0036496185 scopus 로고    scopus 로고
    • 0-type ATP synthase, a biological rotary motor
    • DOI 10.1016/S0968-0004(01)02051-5, PII S0968000401020515
    • CAPALDI, R. A. & AGGELER, R. (2002). Mechanism of the F1F0-type ATP synthase, a biological rotary motor. Trends in Biochemical Science 27, 154-160. (Pubitemid 34219326)
    • (2002) Trends in Biochemical Sciences , vol.27 , Issue.3 , pp. 154-160
    • Capaldi, R.A.1    Aggeler, R.2
  • 43
    • 0033971704 scopus 로고    scopus 로고
    • Cross-linking and electron microscopy studies of the structure and functioning of the Escherichia coli ATP synthase
    • CAPALDI, R.A., SCHULENBERG, B., MURRAY, J. & AGGELER, R. (2000). Cross-linking and electron microscopy studies of the structure and functioning of the Escherichia coli ATP synthase. Journal of Experimental Biology 203, 29-33. (Pubitemid 30079066)
    • (2000) Journal of Experimental Biology , vol.203 , Issue.1 , pp. 29-33
    • Capaldi, R.A.1    Schulenberg, B.2    Murray, J.3    Aggeler, R.4
  • 44
    • 33947585115 scopus 로고    scopus 로고
    • o-ATP Synthase Interacts with the N-terminal Region of an Alpha Subunit
    • DOI 10.1016/j.jmb.2007.02.059, PII S0022283607002409
    • CARBAJO, R. J., KELLAS, F. A., YANG, J. C., RUNSWICK, M. J., MONTGOMERY, M.G., WALKER, J.E. & NEUHAUS, D. (2007). How the N-terminal domain of the OSCP sub-unit of bovine F1F0-ATP synthase interacts with the N-terminal region of an a subunit. Journal of Molecular Biology 368, 310-318. (Pubitemid 46483497)
    • (2007) Journal of Molecular Biology , vol.368 , Issue.2 , pp. 310-318
    • Carbajo, R.J.1    Kellas, F.A.2    Yang, J.-C.3    Runswick, M.J.4    Montgomery, M.G.5    Walker, J.E.6    Neuhaus, D.7
  • 45
    • 0014782571 scopus 로고
    • Biochemical and ultrastructural properties of a mi-tochondrial inner membrane fraction deficient in outer membrane and matrix activities
    • CHAN, T. L., GREENAWALT, J. W. & PEDERSEN, P. L. (1970). Biochemical and ultrastructural properties of a mi-tochondrial inner membrane fraction deficient in outer membrane and matrix activities. Journal of Cell Biology 45, 291-305.
    • (1970) Journal of Cell Biology , vol.45 , pp. 291-305
    • Chan, T.L.1    Greenawalt, J.W.2    Pedersen, P.L.3
  • 46
    • 0034711281 scopus 로고    scopus 로고
    • +-ATPase
    • DOI 10.1074/jbc.M006640200
    • CHARSKY, C.M.H., SCHUMANN, N.J. & KANE, P.M. (2000). Mutational analysis of subunit G (Vma10p) of the yeast vacuolar H+-ATPase. Journal of Biological Chemistry 275, 37232-37239. (Pubitemid 32002144)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.47 , pp. 37232-37239
    • Charsky, C.M.H.1    Schumann, N.J.2    Kane, P.M.3
  • 47
    • 0032947857 scopus 로고    scopus 로고
    • Transient accumulation of elastic energy in proton translocating ATP synthase
    • DOI 10.1016/S0014-5793(99)00386-5, PII S0014579399003865
    • CHEREPANOV, D. A., MULKIDJANIAN, A. Y. & JUNGE, W. (1999). Transient accumulation of elastic energy in proton translocating ATP synthase. FEBS Letters 449, 1-6. (Pubitemid 29182659)
    • (1999) FEBS Letters , vol.449 , Issue.1 , pp. 1-6
    • Cherepanov, D.A.1    Mulkidjanian, A.Y.2    Junge, W.3
  • 48
    • 33745867962 scopus 로고    scopus 로고
    • An expanded and flexible form of the vacuolar ATPase membrane sector
    • DOI 10.1016/j.str.2006.05.014, PII S096921260600253X
    • CLARE, D. K., ORLOVA, E. V., FINBOW, M. E., HARRISON, M. A., FINDLAY, J. B. C. & SAIBIL, H. R. (2006). An expanded and flexible form of the vacuolar ATPase membrane sector. Structure 14, 1149-1156. (Pubitemid 44037422)
    • (2006) Structure , vol.14 , Issue.7 , pp. 1149-1156
    • Clare, D.K.1    Orlova, E.V.2    Finbow, M.A.3    Harrison, M.A.4    Findlay, J.B.C.5    Saibil, H.R.6
  • 49
    • 4644343538 scopus 로고    scopus 로고
    • Structure and subunit arrangement of the A-type ATP synthase complex from the archaeon Methanococcus jannaschii visualized by electron microscopy
    • DOI 10.1074/jbc.M406196200
    • C̈OSKUN, U., CHABAN, Y.L., LINGL, A., MÜLLER, V., KEEGSTRA, W., BOEKEMA, E. J. & GRÜBER, G. (2004). Structure and subunit arrangement of the A-type ATP synthase complex from the archaeon Methanococcus jan-naschii visualized by electron microscopy. Journal of Biological Chemistry 279, 38644-38648. (Pubitemid 39296020)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.37 , pp. 38644-38648
    • Coskun, U.1    Chaban, Y.L.2    Lingl, A.3    Muller, V.4    Keegstra, W.5    Boekema, E.J.6    Gruber, G.7
  • 53
    • 1042278165 scopus 로고    scopus 로고
    • Genome-wide Analysis of Iron-dependent Growth Reveals a Novel Yeast Gene Required for Vacuolar Acidification
    • DOI 10.1074/jbc.M310680200
    • DAVIS-KAPLAN, S. R., MCVEY WARD, D., SHIFLETT, S. L. & KAPLAN, J. (2004). Genome-wide analysis of iron-dependent drowth reveals a novel yeast gene required for vacuolar acidification. Journal of Biological Chemistry 279, 4322-4329. (Pubitemid 38199020)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.6 , pp. 4322-4329
    • Davis-Kaplan, S.R.1    McVey Ward, D.2    Shiflett, S.L.3    Kaplan, J.4
  • 56
    • 33745548556 scopus 로고    scopus 로고
    • On the structure of the stator of the mitochondrial ATP synthase
    • DOI 10.1038/sj.emboj.7601177, PII 7601177
    • DICKSON, V.K., SILVESTER, J.A., FEARNLEY, I.M., LESLIE, A. G. & WALKER, J. E. (2006). On the structure of the stator of the mitochondrial ATP synthase. EMBO Journal 25, 2911-2918. (Pubitemid 43980397)
    • (2006) EMBO Journal , vol.25 , Issue.12 , pp. 2911-2918
    • Dickson, V.K.1    Silvester, J.A.2    Fearnley, I.M.3    Leslie, A.G.W.4    Walker, J.E.5
  • 57
    • 53849140811 scopus 로고    scopus 로고
    • Structural organization of the V-ATPase and its implications for regulatory assembly and disassembly
    • DIEPHOLZ, M., BÖRSCH, M. & BÖTTCHER, B. (2008a). Structural organization of the V-ATPase and its implications for regulatory assembly and disassembly. Biochemical Society Transactions 36, 1027-1031.
    • (2008) Biochemical Society Transactions , vol.36 , pp. 1027-1031
    • Diepholz, M.1    Börsch, M.2    Böttcher, B.3
  • 58
    • 57149127160 scopus 로고    scopus 로고
    • A different conformation for EGC stator subcomplex in solution and in the assembled yeast V-ATPase: Possible implications for regulatory disassembly
    • DIEPHOLZ, M., VENZKE, D., PRINZ, S., BATISSE, C., FLÖRCHINGER, B., RÖSSLE, M., SVERGUN, D.I., BÖTTCHER, B. & FÉTHIÈRE, J. (2008b). A different conformation for EGC stator subcomplex in solution and in the assembled yeast V-ATPase: possible implications for regulatory disassembly. Structure 16, 1789-1798.
    • (2008) Structure , vol.16 , pp. 1789-1798
    • Diepholz, M.1    Venzke, D.2    Prinz, S.3    Batisse, C.4    Flörchinger, B.5    Rössle, M.6    Svergun, D.I.7    Böttcher, B.8    Féthière, J.9
  • 60
    • 33645796449 scopus 로고    scopus 로고
    • Catalytic and mechanical cycles in F-ATP synthases: Fourth in the cycles review series
    • DIMROTH, P., VON BALLMOOS, C. & MEIER, T. (2006). Catalytic and mechanical cycles in F-ATP synthases: fourth in the cycles review series. EMBO Reports 7, 276-282.
    • (2006) EMBO Reports , vol.7 , pp. 276-282
    • Dimroth, P.1    Von Ballmoos, C.2    Meier, T.3
  • 62
    • 4644240260 scopus 로고    scopus 로고
    • Spin-labelled vacuolar-ATPase inhibitors in lipid membranes
    • DOI 10.1016/j.bbamem.2004.08.001, PII S0005273604001841
    • DIXON, N., PALI, T., KEE, T. P. & MARSH, D. (2004). Spin-labelled vacuolar-ATPase inhibitors in lipid membranes. Biochimica et Biophysica Acta 1665, 177-183. (Pubitemid 39303582)
    • (2004) Biochimica et Biophysica Acta - Biomembranes , vol.1665 , Issue.1-2 , pp. 177-183
    • Dixon, N.1    Pali, T.2    Kee, T.P.3    Marsh, D.4
  • 63
    • 0037066762 scopus 로고    scopus 로고
    • Three-dimensional map of a plant V-ATPase based on electron microscopy
    • DOI 10.1074/jbc.M112011200
    • DOMGALL, I., VENZKE, D., LUTTGE, U., RATAJCZAK, R. & BÖTTCHER, B. (2002). Three-dimensional map of a plant V-ATPase based on electron microscopy. Journal of Biological Chemistry 277, 13115-13121. (Pubitemid 34952682)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.15 , pp. 13115-13121
    • Domgall, I.1    Venzke, D.2    Luttge, U.3    Ratajczak, R.4    Bottcher, B.5
  • 64
    • 12144279605 scopus 로고    scopus 로고
    • Crystal structure of yeast V-ATPase subunit C reveals its stator function
    • DOI 10.1038/sj.embor.7400294
    • DRORY, O., FROLOW, F. & NELSON, N. (2004). Crystal structure of yeast V-ATPase subunit C reveals its stator function. EMBO Reports 5, 1148-1152. (Pubitemid 40103608)
    • (2004) EMBO Reports , vol.5 , Issue.12 , pp. 1148-1152
    • Drory, O.1    Frolow, F.2    Nelson, N.3
  • 67
    • 41649087227 scopus 로고    scopus 로고
    • Detection and separation of heterogeneity in molecular complexes by statistical analysis of their two-dimensional projections
    • ELAD, N., CLARE, D. K., SAIBIL, H. R. & ORLOVA, E. V. (2008). Detection and separation of heterogeneity in molecular complexes by statistical analysis of their two-dimensional projections. Journal of Structural Biology 162, 108-120.
    • (2008) Journal of Structural Biology , vol.162 , pp. 108-120
    • Elad, N.1    Clare, D.K.2    Saibil, H.R.3    Orlova, E.V.4
  • 68
    • 0032576724 scopus 로고    scopus 로고
    • Energy trans-duction in ATP synthase
    • ELSTON, T., WANG, H. & OSTER, G. (1998). Energy trans-duction in ATP synthase. Nature 391, 510-513.
    • (1998) Nature , vol.391 , pp. 510-513
    • Elston, T.1    Wang, H.2    Oster, G.3
  • 71
    • 76249120489 scopus 로고    scopus 로고
    • Conformational transitions of sub-unit e in ATP synthase from thermophilic Bacillus PS3
    • FENIOUK, B.A., KATO-YAMADA, Y., YOSHIDA, M. & SUZUKI, T. (2010). Conformational transitions of sub-unit e in ATP synthase from thermophilic Bacillus PS3. Biophysical Journal 98, 434-442.
    • (2010) Biophysical Journal , vol.98 , pp. 434-442
    • Feniouk, B.A.1    Kato-Yamada, Y.2    Yoshida, M.3    Suzuki, T.4
  • 72
  • 73
    • 28544445574 scopus 로고    scopus 로고
    • Peripheral stator of the yeast V-ATPase: Stoichiometry and specificity of interaction between the EG complex and subunits C and H
    • DOI 10.1021/bi051762f
    • FÉTHIÈRE, J., VENZKE, D., MADDEN, D. R. & BÖTTCHER, B. (2005). Peripheral stator of the yeast V-ATPase: stoi-chiometry and specificity of interaction between the EG complex and subunits C and H. Biochemistry 44, 15906-15914. (Pubitemid 41746921)
    • (2005) Biochemistry , vol.44 , Issue.48 , pp. 15906-15914
    • Fethiere, J.1    Venzke, D.2    Madden, D.R.3    Bottcher, B.4
  • 74
    • 0037055972 scopus 로고    scopus 로고
    • o ATP synthase: Aqueous access channels and helix rotations at the a-c interface
    • DOI 10.1016/S0005-2728(02)00250-5, PII S0005272802002505
    • FILLINGAME, R. H., ANGEVINE, C. M. & DMITRIEV, O. Y. (2002). Coupling proton movements to c-ring rotation in F1F0 ATP synthase: aqueous access channels and helix rotations at the a-c interface. Biochimica et Biophysica Acta 1555, 29-36. (Pubitemid 35246001)
    • (2002) Biochimica et Biophysica Acta - Bioenergetics , vol.1555 , Issue.1-3 , pp. 29-36
    • Fillingame, R.H.1    Angevine, C.M.2    Dmitriev, O.Y.3
  • 75
    • 35448946098 scopus 로고    scopus 로고
    • Vacuolar ATPases: Rotary proton pumps in physiology and pathophysiology
    • DOI 10.1038/nrm2272, PII NRM2272
    • FORGAC, M. (2007). Vacuolar ATPases: rotary proton pumps in physiology and pathophysiology. Nature Reviews Molecular and Cellular Biology 8, 917-929. (Pubitemid 47622561)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.11 , pp. 917-929
    • Forgac, M.1
  • 79
    • 0034738058 scopus 로고    scopus 로고
    • + ATPase): Coupling between catalysis, mechanical work, and proton translocation
    • DOI 10.1016/S0005-2728(00)00080-3, PII S0005272800000803
    • FUTAI, M., OMOTE, H., SAMBONGI, Y. & WADA, Y (2000). Synthase (H+ ATPase): coupling between catalysis, mechanical work, and proton translocation. Biochimica et Biophysica Acta - Bioenergetics 1458, 276-288. (Pubitemid 30320711)
    • (2000) Biochimica et Biophysica Acta - Bioenergetics , vol.1458 , Issue.2-3 , pp. 276-288
    • Futai, M.1    Omote, H.2    Sambongi, Y.3    Wada, Y.4
  • 83
    • 34248585138 scopus 로고    scopus 로고
    • Three-dimensional reconstruction of bovine brain V-ATPase by cryo-electron microscopy and single particle analysis
    • DOI 10.1016/j.jsb.2007.01.002, PII S1047847707000214
    • GREGORINI, M., WANG, J., XIE, X. S., MILLIGAN, R. A. & ENGEL, A. (2007). Three-dimensional reconstruction of bovine brain V-ATPase by cryo-electron microscopy and single particle analysis. Journal of Structural Biology 158, 445-454. (Pubitemid 46764572)
    • (2007) Journal of Structural Biology , vol.158 , Issue.3 , pp. 445-454
    • Gregorini, M.1    Wang, J.2    Xie, X.-S.3    Milligan, R.A.4    Engel, A.5
  • 85
    • 0035916075 scopus 로고    scopus 로고
    • 1 ATPase from the archaeon, Methanosarcina mazei Gö1
    • DOI 10.1021/bi002195t
    • GRUBER, G., SVERGUN, D. I., COSKUN, U., LEMKER, T., KOCH, M. H.J., SCHAGGER, H. & MULLER, V (2001a). Structural insights into the A1 ATPase from the ar-chaeon, Methanosarcina mazei Gö1. Biochemistry 40, 1890-1896. (Pubitemid 32165656)
    • (2001) Biochemistry , vol.40 , Issue.7 , pp. 1890-1896
    • Gruber, G.1    Svergun, D.I.2    Coskun, U.3    Lemker, T.4    Koch, M.H.J.5    Schagger, H.6    Muller, V.7
  • 86
  • 89
    • 0142057283 scopus 로고    scopus 로고
    • Structure and function of the vacuolar H+-ATPase: Moving from low resolution models to high resolution structures
    • DOI 10.1023/A:1025728915565
    • HARRISON, M. A., DUROSE, L., SONG, C. F., BARRATT, E., TRINICK, J., JONES, R. & FINDLAY, J.B.C. (2003). Structure and function of the vacuolar H+-ATPase: moving from low resolution models to high resolution structures. Journal of Bioenergetics and Biomembranes 35, 337-345. (Pubitemid 37288700)
    • (2003) Journal of Bioenergetics and Biomembranes , vol.35 , Issue.4 , pp. 337-345
    • Harrison, M.1    Durose, L.2    Song, C.F.3    Barratt, E.4    Trinick, J.5    Jones, R.6    Findlay, J.B.C.7
  • 90
    • 0038584352 scopus 로고    scopus 로고
    • 3 as determined by fluorescence correlation spectroscopy
    • HÄSLER, K., PÄNKE, O. & JUNGE, W. (1999). On the stator of rotary ATP synthase: the binding strength of subunit d to (ab)3 as determined by fluorescence correlation spectroscopy. Biochemistry 38, 13759-13765.
    • (1999) Biochemistry , vol.38 , pp. 13759-13765
    • Häsler, K.1    Pänke, O.2    Junge, W.3
  • 92
    • 3142655417 scopus 로고    scopus 로고
    • Realizing the potential of electron cryo-microscopy
    • DOI 10.1017/S0033583504003920
    • HENDERSON, R. (2004). Realizing the potential of electron cryo-microscopy. Quarterly Reviews of Biophysics 37, 3-13. (Pubitemid 38902192)
    • (2004) Quarterly Reviews of Biophysics , vol.37 , Issue.1 , pp. 3-13
    • Henderson, R.1
  • 93
    • 0031864850 scopus 로고    scopus 로고
    • The prokaryote-to-eukaryote transition reflected in the evolution of the V/F/A-ATPase catalytic and proteolipid subunits
    • DOI 10.1007/PL00006351
    • HILARIO, E. & GOGARTEN, J. P. (1998). The prokaryote-to-eukaryote transition reflected in the evolution of the V/F/A-ATPase catalytic and proteolipid subunits. Journal of Molecular Evolution 46, 703-715. (Pubitemid 28270228)
    • (1998) Journal of Molecular Evolution , vol.46 , Issue.6 , pp. 703-715
    • Hilario, E.1    Gogarten, J.P.2
  • 95
    • 0038606551 scopus 로고    scopus 로고
    • Subunit rotation of vacuolar-type proton pumping ATPase. Relative rotation of the G and c subunits
    • DOI 10.1074/jbc.M302756200
    • HIRATA, T., IWAMOTO-KIHARA, A., SUN-WADA, G.H., OKAJIMA, T., WADA, Y. & FUTAI, M. (2003). Subunit rotation of vacuolar-type proton pumping ATPase: relative rotation of the G and c subunits. Journal of Biological Chemistry 278, 23714-23719. (Pubitemid 36830195)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.26 , pp. 23714-23719
    • Hirata, T.1    Iwamoto-Kihara, A.2    Sun-Wada, G.-H.3    Okajima, T.4    Wada, Y.5    Futai, M.6
  • 97
    • 0026684630 scopus 로고
    • Purification and properties of an ATPase from Sulfolobus solfataricus
    • HOCHSTEIN, L. I. & STAN-LOTTER, H. (1992). Purification and properties of an ATPase from Sulfolobus solfataricus. Archives of Biochemistry and Biophysics 295, 153-160.
    • (1992) Archives of Biochemistry and Biophysics , vol.295 , pp. 153-160
    • Hochstein, L.I.1    Stan-Lotter, H.2
  • 98
    • 0000207681 scopus 로고
    • TMbase - A database of membrane spanning proteins segments
    • HOFMANN, K. & STOFFEL, W. (1993). TMbase - a database of membrane spanning proteins segments. Biological Chemistry Hoppe-Seyler 374, 166-173.
    • (1993) Biological Chemistry Hoppe-Seyler , vol.374 , pp. 166-173
    • Hofmann, K.1    Stoffel, W.2
  • 99
    • 31444437369 scopus 로고    scopus 로고
    • A WNK kinase binds and phosphorylates V-ATPase subunit C
    • DOI 10.1016/j.febslet.2006.01.018, PII S0014579306000500
    • HONG-HERMESDORF, A., BRUX, A., GRÜBER, A., GRÜBER, G. & SCHUMACHER, K. (2006). A WNK kinase binds and phosphorylates V-ATPase subunit C. FEBS Letters 580, 932-939. (Pubitemid 43152317)
    • (2006) FEBS Letters , vol.580 , Issue.3 , pp. 932-939
    • Hong-Hermesdorf, A.1    Brux, A.2    Gruber, A.3    Gruber, G.4    Schumacher, K.5
  • 100
    • 0031433216 scopus 로고    scopus 로고
    • The intriguing evolution of the 'b' and 'G' subunits in F-type and V- type ATPases: Isolation of the vma-10 gene from Neurospora crassa
    • DOI 10.1023/A:1022474816665
    • HUNT, I. E. & BOWMAN, B. J. (1997). The intriguing evolution of the b and G subunits in F-type and V-type ATPases: isolation of the vma-10 gene from Neurospora crassa. Journal of Bioenergetics and Biomembranes 29, 533-540. (Pubitemid 28164858)
    • (1997) Journal of Bioenergetics and Biomembranes , vol.29 , Issue.6 , pp. 533-540
    • Hunt, I.E.1    Bowman, B.J.2
  • 102
    • 36549034305 scopus 로고    scopus 로고
    • O complexes
    • DOI 10.1016/j.febslet.2007.11.004, PII S0014579307011337
    • HUSS, M. & WIECZOREK, H. (2007). Influence of ATP and ADP on dissociation of the V-ATPase into its V1 and V0 complexes. FEBS Letters 581, 5566-5572. (Pubitemid 350179763)
    • (2007) FEBS Letters , vol.581 , Issue.29 , pp. 5566-5572
    • Huss, M.1    Wieczorek, H.2
  • 104
    • 2342439140 scopus 로고    scopus 로고
    • 1-ATPase Promotes ATPase Activity but Is Not Necessary for Rotation
    • DOI 10.1074/jbc.M314204200
    • IMAMURA, H., IKEDA, C., YOSHIDA, M. & YOKOYAMA, K. (2004). The F subunit of Thermus thermophilus V1-ATPase promotes ATPase activity but is not necessary for rotation. Journal of Biological Chemistry 279, 18085-18090. (Pubitemid 38560578)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.17 , pp. 18085-18090
    • Imamura, H.1    Ikeda, C.2    Yoshida, M.3    Yokoyama, K.4
  • 107
    • 0022501645 scopus 로고
    • Characterization and purification of the membrane-bound ATPase of the archaebacterium Methanosarcina barkeri
    • INATOMI, K. (1986). Characterization and purification of the membrane-bound ATPase of the archaebacterium Methanosarcina barkeri. Journal of Bacteriology 167, 837-841. (Pubitemid 16045015)
    • (1986) Journal of Bacteriology , vol.167 , Issue.3 , pp. 837-841
    • Inatomi, K.I.1
  • 108
    • 23044497763 scopus 로고    scopus 로고
    • 0 domain
    • DOI 10.1074/jbc.M504890200
    • INOUE, T. & FORGAC, M. (2005). Cysteine-mediated cross-linking indicates that subunit C of the V-ATPase is in close proximity to subunits E and G of the V1 domain and subunit a of the V0 Domain. Journal of Biological Chemistry 280, 27896-27903. (Pubitemid 41076907)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.30 , pp. 27896-27903
    • Inoue, T.1    Forgac, M.2
  • 110
    • 41949126316 scopus 로고    scopus 로고
    • 1 domain by interaction with the rotary subunit F
    • JEFFERIES, K. C. & FORGAC, M. (2008). Subunit H of the vacuolar (H+) ATPase inhibits ATP hydrolysis by the free V1 domain by interaction with the rotary subunit F. Journal of Biological Chemistry 283, 4512-4519.
    • (2008) Journal of Biological Chemistry , vol.283 , pp. 4512-4519
    • Jefferies, K.C.1    Forgac, M.2
  • 112
  • 113
    • 0032491417 scopus 로고    scopus 로고
    • +-transporting ATP synthase
    • JONES, P. C. & FILLINGAME, R. H. (1998). Genetic fusions of subunit c in the F0 sector of H+-transporting ATP synthase. Journal of Biological Chemistry 273, 29701-29705.
    • (1998) Journal of Biological Chemistry , vol.273 , pp. 29701-29705
    • Jones, P.C.1    Fillingame, R.H.2
  • 114
    • 0034613389 scopus 로고    scopus 로고
    • 1 ATP synthase from the cross-linking of subunits b and c in the Escherichia coli enzyme
    • JONES, P. C., HERMOLIN, J., JIANG, W. & FILLINGAME, R. H. (2000). Insights into the rotary catalytic mechanism of F0F1 ATP synthase from the cross-linking of subunits b and c in the Escherichia coli enzyme. Journal of Biological Chemistry 275, 31340-31346.
    • (2000) Journal of Biological Chemistry , vol.275 , pp. 31340-31346
    • Jones, P.C.1    Hermolin, J.2    Jiang, W.3    Fillingame, R.H.4
  • 115
    • 14844349013 scopus 로고    scopus 로고
    • +-ATPase
    • DOI 10.1021/bi048402x
    • JONES, R.P.O., DUROSE, L.J., FINDLAY, J.B.C. & HARRISON, M. A. (2005). Defined sites of interaction between subunits E (Vma4p), C (Vma5p), and G (Vma10p) within the stator structure of the vacuolar H+-ATPase. Biochemistry 44, 3933-3941. (Pubitemid 40358045)
    • (2005) Biochemistry , vol.44 , Issue.10 , pp. 3933-3941
    • Jones, R.P.O.1    Durose, L.J.2    Findlay, J.B.C.3    Harrison, M.A.4
  • 116
    • 77954497964 scopus 로고    scopus 로고
    • A site-directed cross-linking approach to the characterization of subunit E-subunit G contacts in the vacuolar H+-ATPase stator
    • JONES, R. P. O., DUROSE, L. J., PHILLIPS, C., KEEN, J. N., FINDLAY, J. B. C. & HARRISON, M. A. (2010). A site-directed cross-linking approach to the characterization of subunit E-subunit G contacts in the vacuolar H+-ATPase stator. Molecular Membrane Biology 27, 147-159.
    • (2010) Molecular Membrane Biology , vol.27 , pp. 147-159
    • Jones, R.P.O.1    Durose, L.J.2    Phillips, C.3    Keen, J.N.4    Findlay, J.B.C.5    Harrison, M.A.6
  • 117
    • 3042728346 scopus 로고    scopus 로고
    • Protons, proteins and ATP
    • DOI 10.1023/B:PRES.0000030677.98474.74
    • JUNGE, W. (2004). Protons, proteins and ATP. Photosynthesis Research 80, 197-221. (Pubitemid 38889628)
    • (2004) Photosynthesis Research , vol.80 , Issue.1-3 , pp. 197-221
    • Junge, W.1
  • 118
    • 0030715561 scopus 로고    scopus 로고
    • ATP synthase: An electrochemical transducer with rotatory mechanics
    • DOI 10.1016/S0968-0004(97)01129-8, PII S0968000497011298
    • JUNGE, W., LILL, H. & ENGELBRECHT, S. (1997). ATP syn-thase: an electrochemical transducer with rotatory mechanics. Trends in Biochemical Science 22, 420-423. (Pubitemid 27508785)
    • (1997) Trends in Biochemical Sciences , vol.22 , Issue.11 , pp. 420-423
    • Junge, W.1    Lill, H.2    Engelbrecht, S.3
  • 119
    • 66249132322 scopus 로고    scopus 로고
    • 1 -ATPase
    • JUNGE, W., SIELAFF, H. & ENGELBRECHT, S. (2009). Torque generation and elastic power transmission in the rotary F0F1-ATPase. Nature 459, 364-370.
    • (2009) Nature , vol.459 , pp. 364-370
    • Junge, W.1    Sielaff, H.2    Engelbrecht, S.3
  • 120
    • 33751086144 scopus 로고    scopus 로고
    • 1 ATPase
    • DOI 10.1038/sj.emboj.7601410, PII 7601410
    • KABALEESWARAN, V., PURI, N., WALKER, J.E., LESLIE, A. G. W. & MUELLER, D. M. (2006). Novel features of the rotary catalytic mechanism revealed in the structure of yeast F-1 ATPase. EMBO Journal 25, 5433-5442. (Pubitemid 44764152)
    • (2006) EMBO Journal , vol.25 , Issue.22 , pp. 5433-5442
    • Kabaleeswaran, V.1    Puri, N.2    Walker, J.E.3    Leslie, A.G.W.4    Mueller, D.M.5
  • 121
    • 0032932118 scopus 로고    scopus 로고
    • +-translocating ATPase in Enterococcus hirae
    • DOI 10.1023/A:1005499126939
    • KAKINUMA, Y., YAMATO, I. & MURATA, T. (1999). Structure and function of vacuolar Na+-translocating ATPase in Enterococcus hirae. Journal of Bioenergetics and Biomembranes 31, 7-14. (Pubitemid 29203373)
    • (1999) Journal of Bioenergetics and Biomembranes , vol.31 , Issue.1 , pp. 7-14
    • Kakinuma, Y.1    Yamato, I.2    Murata, T.3
  • 122
    • 0029063512 scopus 로고
    • Disassembly and reassembly of the yeast vacuolar H(+)-ATPase in vivo
    • KANE, P. M. (1995). Disassembly and reassembly of the yeast vacuolar H(+)-ATPase in vivo. Journal of Biological Chemistry 270, 17025-17032.
    • (1995) Journal of Biological Chemistry , vol.270 , pp. 17025-17032
    • Kane, P.M.1
  • 123
    • 0033538506 scopus 로고    scopus 로고
    • Novel features in the structure of bovine ATP synthase
    • DOI 10.1006/jmbi.1999.2897
    • KARRASCH, S. & WALKER, J. E. (1999). Novel features in the structure of bovine ATP synthase. Journal of Molecular Biology 290, 379-384. (Pubitemid 29324824)
    • (1999) Journal of Molecular Biology , vol.290 , Issue.2 , pp. 379-384
    • Karrasch, S.1    Walker, J.E.2
  • 125
    • 0141815743 scopus 로고    scopus 로고
    • 1-ATPase binds ATP
    • DOI 10.1074/jbc.M306140200
    • KATO-YAMADA, Y. & YOSHIDA, M. (2003). Isolated e sub-unit of thermophilic F1-ATPase binds ATP. Journal of Biological Chemistry 278, 36013-36016. (Pubitemid 37139920)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.38 , pp. 36013-36016
    • Kato-Yamada, Y.1    Yoshida, M.2
  • 128
    • 0032478354 scopus 로고    scopus 로고
    • 1-ATPase: A rotary motor made of a single molecule
    • DOI 10.1016/S0092-8674(00)81142-3
    • KINOSITA, K., YASUDA, R., NOJI, H., ISHIWATA, S. & YOSHIDA, M. (1998). F1-ATPase: a rotary motor made of a single molecule. Cell 93, 21-24. (Pubitemid 28173548)
    • (1998) Cell , vol.93 , Issue.1 , pp. 21-24
    • Kinosita Jr., K.1    Yasuda, R.2    Noji, H.3    Ishiwata, S.4    Yoshida, M.5
  • 129
    • 37349093687 scopus 로고    scopus 로고
    • 0-ATP synthase-structural characterization of the E and H subunits
    • DOI 10.1016/j.jmb.2007.10.063, PII S0022283607014222
    • KISH-TRIER, E., BRIERE, L. A., DUNN, S. D. & WILKENS, S. (2008). The stator complex of the A1A0-ATP synthase-structural characterization of the E and H subunits. Journal of Molecular Biology 375, 673-685. (Pubitemid 350297285)
    • (2008) Journal of Molecular Biology , vol.375 , Issue.3 , pp. 673-685
    • Kish-Trier, E.1    Briere, L.-A.K.2    Dunn, S.D.3    Wilkens, S.4
  • 130
    • 66449094132 scopus 로고    scopus 로고
    • 0-ATP synthase from Thermoplasma acidophilum
    • KISH-TRIER, E. & WILKENS, S. (2009a). Domain architecture of the stator complex of the A1A0-ATP synthase from Thermoplasma acidophilum. Journal of Biological Chemistry 284, 12031-12040.
    • (2009) Journal of Biological Chemistry , vol.284 , pp. 12031-12040
    • Kish-Trier, E.1    Wilkens, S.2
  • 131
    • 70349446454 scopus 로고    scopus 로고
    • 0 -ATP synthase peripheral stalk with the catalytic domain
    • KISH-TRIER, E. & WILKENS, S. (2009b). Interaction of the Thermoplasma acidophilum A1A0-ATP synthase peripheral stalk with the catalytic domain. FEBS Letters 583, 3121-3126.
    • (2009) FEBS Letters , vol.583 , pp. 3121-3126
    • Kish-Trier, E.1    Wilkens, S.2
  • 132
    • 41249097135 scopus 로고    scopus 로고
    • 1-ATPase determined by mass spectrometry
    • KITAGAWA, N., MAZON, H., HECK, A. J. R. & WILKENS, S. (2008). Stoichiometry of the peripheral stalk subunits E and G of yeast V1-ATPase determined by mass spec-trometry. Journal of Biological Chemistry 283, 3329-3337.
    • (2008) Journal of Biological Chemistry , vol.283 , pp. 3329-3337
    • Kitagawa, N.1    Mazon, H.2    Heck, A.J.R.3    Wilkens, S.4
  • 133
    • 0034685544 scopus 로고    scopus 로고
    • 1 sector
    • DOI 10.1074/jbc.M000207200
    • LANDOLT-MARTICORENA, C., WILLIAMS, K. M., CORREA, J., CHEN, W. & MANOLSON, M. F. (2000). Evidence that the NH2 terminus of Vph1p, an integral subunit of the V0 sector of the yeast V-ATPase, interacts directly with the Vma1p and Vma13p subunits of the V1 sector. Journal of Biological Chemistry 275, 15449-15457. (Pubitemid 30337276)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.20 , pp. 15449-15457
    • Landolt-Marticorena, C.1    Williams, K.M.2    Correa, J.3    Chen, W.4    Manolson, M.F.5
  • 134
    • 34447260787 scopus 로고    scopus 로고
    • 1 ATP synthase. Effect of repositioning within Helix 4 of subunit a and Helix 2 of subunit c
    • DOI 10.1016/j.bbabio.2007.05.007, PII S0005272807001120
    • LANGEMEYER, L. & ENGELBRECHT, S. (2007). Essential ar-ginine in subunit a and aspartate in subunit c of F0F1 ATP synthase: effect of repositioning within Helix 4 of subunit a and Helix 2 of subunit c. Biochimica et Biophysica Acta 1767, 998-1005. (Pubitemid 47039236)
    • (2007) Biochimica et Biophysica Acta - Bioenergetics , vol.1767 , Issue.7 , pp. 998-1005
    • Langemeyer, L.1    Engelbrecht, S.2
  • 137
    • 0025363109 scopus 로고
    • 0 of Propionigenium modestum is a functional sodium ion pump
    • DOI 10.1021/bi00475a008
    • LAUBINGER, G., DECKERS-HEBESTREIT, G., ALTENDORF, K. & DIMROTH, P. (1990). A hybrid adenosine tripho-sphatase composed of F1 of Escherichia coli and F0 of Propionigenium modestum is a functional sodium ion pump. Biochemistry 29, 5458-5463. (Pubitemid 20202269)
    • (1990) Biochemistry , vol.29 , Issue.23 , pp. 5458-5463
    • Laubinger, W.1    Deckers-Hebestreit, G.2    Altendorf, K.3    Dimroth, P.4
  • 139
    • 77955552311 scopus 로고    scopus 로고
    • Vacuolar (H+)-ATPases in Caenorhabditis elegans: What can we learn about giant H pumps from tiny worms?
    • LEE, S. K., LI, W., RYU, S. E., RHIM, T. & AHNN, J. (2010b). Vacuolar (H+)-ATPases in Caenorhabditis elegans: what can we learn about giant H pumps from tiny worms ? Biochimica et Biophysica Acta 1797, 1687-1695.
    • (2010) Biochimica et Biophysica Acta , vol.1797 , pp. 1687-1695
    • Lee, S.K.1    L, I.W.2    Ryu, S.E.3    Rhim, T.4    Ahnn, J.5
  • 140
    • 0032549629 scopus 로고    scopus 로고
    • Function of the COOH-terminal domain of Vph1p in activity and assembly of the yeast V-ATPase
    • DOI 10.1074/jbc.273.12.6717
    • LENG, X. H., MANOLSON, M. F. & FORGAC, M. (1998). Function of the COOH-terminal domain of Vph1p in activity and assembly of the yeast V-ATPase. Journal of Biological Chemistry 273, 6717-6723. (Pubitemid 28160331)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.12 , pp. 6717-6723
    • Leng, X.-H.1    Manolson, M.F.2    Forgac, M.3
  • 141
    • 0029831620 scopus 로고    scopus 로고
    • +)-ATPase
    • DOI 10.1074/jbc.271.37.22487
    • LENG, X. H., MANOLSON, M. F., LIU, Q. & FORGAC, M. (1996). Site-directed mutagenesis of the 100-kda subunit (Vph1p) of the yeast vacuolar (H +)-ATPase. Journal of Biological Chemistry 271, 22487-22493. (Pubitemid 26304685)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.37 , pp. 22487-22493
    • Leng, X.-H.1    Manolson, M.F.2    Liu, Q.3    Forgac, M.4
  • 142
    • 0033591450 scopus 로고    scopus 로고
    • Transmembrane topography of the 100-kda a subunit (Vph1p) of the yeast vacuolar proton translocating ATPase
    • LENG, X. H., NISHI, T. & FORGAC, M. (1999). Transmembrane topography of the 100-kda a subunit (Vph1p) of the yeast vacuolar proton translocating ATPase. Journal of Biological Chemistry 274, 14655-14661.
    • (1999) Journal of Biological Chemistry , vol.274 , pp. 14655-14661
    • Leng, X.H.1    Nishi, T.2    Forgac, M.3
  • 143
    • 0032748995 scopus 로고    scopus 로고
    • Atp6i-deficient mice exhibit severe osteopetrosis due to loss of osteoclast-mediated extracellular acidification
    • LI, Y. P., CHEN, W., LIANG, Y. Q., LI, E. & STASHENKO, P. (1999). Atp6i-deficient mice exhibit severe osteopetrosis due to loss of osteoclast-mediated extracellular acidification. Nature Genetics 23, 447-451.
    • (1999) Nature Genetics , vol.23 , pp. 447-451
    • I, Y.P.L.1    Chen, W.2    Liang, Y.Q.3    L, I.E.4    Stashenko, P.5
  • 144
    • 0242280092 scopus 로고    scopus 로고
    • O ATP synthase comprising nine subunits from the hyperthermophile Methanococcus jannaschii
    • DOI 10.1007/s00792-003-0318-7
    • LINGL, A., HUBER, H., STETTER, K. O., MAYER, F., KELLERMANN, J. & MULLER, V. (2003). Isolation of a complete A1A0 ATP synthase comprising nine subunits from the hyperthermophile Methanococcus jannaschii Extremophiles 7, 249-257. (Pubitemid 40876351)
    • (2003) Extremophiles , vol.7 , Issue.3 , pp. 249-257
    • Lingl, A.1    Huber, H.2    Stetter, K.O.3    Mayer, F.4    Kellermann, J.5    Muller, V.6
  • 146
    • 0037064113 scopus 로고    scopus 로고
    • +-ATPase (V-ATPase) interacts with the H subunit and is required for V-ATPase function
    • DOI 10.1074/jbc.M203521200
    • LU, M., VERGARA, S., ZHANG, L., HOLLIDAY, L. S., ARIS, J. & GLUCK, S. L. (2002). The amino-terminal domain of the E subunit of vacuolar H + -ATPase (V-ATPase) interacts with the H subunit and is required for V-ATPase function. Journal of Biological Chemistry 277, 38409-38415. (Pubitemid 35154697)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.41 , pp. 38409-38415
    • Lu, M.1    Vergara, S.2    Zhang, L.3    Shannon Holliday, L.4    Aris, J.5    Gluck, S.L.6
  • 147
    • 0025376430 scopus 로고
    • Structure of the ATP synthase complex (ECF1F0) of Escherichia coli from cryoelectron microscopy
    • LUCKEN, U., GOGOL, E. P. & CAPALDI, R. A. (1990). Structure of the ATP synthase complex (ECF1F0) of Escherichia coli from cryoelectron microscopy. Biochemistry 29, 5339-5343.
    • (1990) Biochemistry , vol.29 , pp. 5339-5343
    • Lucken, U.1    Gogol, E.P.2    Capaldi, R.A.3
  • 148
    • 0032079560 scopus 로고    scopus 로고
    • Identification and characterization of a novel 9.2-kDa membrane sector- associated protein of vacuolar proton-ATPase from chromaffin granules
    • DOI 10.1074/jbc.273.18.10939
    • LUDWIG, J., KERSCHER, S., BRANDT, U., PFEIFFER, K., GETLAWI, F., APPS, D. K. & SCHAGGER, H. (1998). Identification and characterisation of a novel 9-2-kDa membrane sector-associated protein of vacuolar proton ATPase form chromaffin granules. Journal of Biological Chemistry 273, 10939-10947. (Pubitemid 28204933)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.18 , pp. 10939-10947
    • Ludwig, J.1    Kerscher, S.2    Brandt, U.3    Pfeiffer, K.4    Getlawi, F.5    Apps, D.K.6    Schagger, H.7
  • 149
    • 0036073866 scopus 로고    scopus 로고
    • 1-ATPase
    • DOI 10.1016/S0969-2126(02)00789-X, PII S096921260200789X
    • MA, J., FLYNN, T. C, CUI, Q., LESLIE, A. G. W., WALKER, J. E. & KARPLUS, M. (2002). A dynamic analysis of the rotation mechanism for conformational change in F1-ATPase. Structure 10, 921-931. (Pubitemid 34786737)
    • (2002) Structure , vol.10 , Issue.7 , pp. 921-931
    • Ma, J.1    Flynn, T.C.2    Cui, Q.3    Leslie, A.G.W.4    Walker, J.E.5    Karplus, M.6
  • 150
    • 33646541995 scopus 로고    scopus 로고
    • Structure of the catalytic nucleotide-binding subunit A of A-type ATP synthase from Pyrococcus horikoshii reveals a novel domain related to the peripheral stalk
    • MAEGAWA, Y., MORITA, H., IYAGUCHI, D., YAO, M., WATANABE, N. & TANAKA, I. (2006). Structure of the catalytic nucleotide-binding subunit A of A-type ATP synthase from Pyrococcus horikoshii reveals a novel domain related to the peripheral stalk. Acta Crystallographica D 62, 483-488.
    • (2006) Acta Crystallographica D , vol.62 , pp. 483-488
    • Maegawa, Y.1    Morita, H.2    Iyaguchi, D.3    Yao, M.4    Watanabe, N.5    Tanaka, I.6
  • 154
    • 47349120492 scopus 로고    scopus 로고
    • + -ATPase in vesicular trafficking: Targeting, regulation and function
    • MARSHANSKY, V. & FUTAI, M. (2008). The V-type H+-ATPase in vesicular trafficking: targeting, regulation and function. Current Opinion in Cell Biology 20, 415-426.
    • (2008) Current Opinion in Cell Biology , vol.20 , pp. 415-426
    • Marshansky, V.1    Futai, M.2
  • 156
    • 0032511038 scopus 로고    scopus 로고
    • The b and δ subunits of the Escherichia coli ATP synthase interact via residues in their C-terminal regions
    • DOI 10.1074/jbc.273.24.15162
    • MCLACHLIN, D. T., BESTARD, J. A. & DUNN, S. D. (1998). The b and d subunits of the Escherichia coliATP synthase interact via residues in their C-terminal regions. Journal of Biological Chemistry 273, 15162-15168. (Pubitemid 28272815)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.24 , pp. 15162-15168
    • McLachlin, D.T.1    Bestard, J.A.2    Dunn, S.D.3
  • 157
    • 0034625459 scopus 로고    scopus 로고
    • Site-directed cross-linking of b to the α, β, and a subunits of the Escherichia coli ATP synthase
    • DOI 10.1074/jbc.M000375200
    • MCLACHLIN, D. T., COVENY, A. M., CLARK, S. M. & DUNN, S. D. (2000). Site-directed cross-linking of b to the a, b, and a subunits of the Escherichia coli ATP synthase. Journal of Biological Chemistry 275, 17571-17577. (Pubitemid 30430801)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.23 , pp. 17571-17577
    • McLachlin, D.T.1    Coveny, A.M.2    Clark, S.M.3    Dunn, S.D.4
  • 158
    • 33751091503 scopus 로고    scopus 로고
    • Structural investigations of the membrane-embedded rotor ring of the F-ATPase from Clostridium paradoxum
    • DOI 10.1128/JB.00934-06
    • MEIER, T., FERGUSON, S. A., COOK, G. M., DIMROTH, P. & VONCK, J. (2006). Structural investigations of the membrane-embedded rotor ring of the F-ATPase from Clostridium paradoxum. Journal of Bacteriology 188, 7759-7764. (Pubitemid 44764512)
    • (2006) Journal of Bacteriology , vol.188 , Issue.22 , pp. 7759-7764
    • Meier, T.1    Ferguson, S.A.2    Cook, G.M.3    Dimroth, P.4    Vonck, J.5
  • 159
    • 17844367330 scopus 로고    scopus 로고
    • +-ATPase from Ilyobacter tartaricus
    • DOI 10.1126/science.1111199
    • MEIER, T., POLZER, P., DIEDERICHS, K., WELTE, W. & DIMROTH, P. (2005a). Structure of the rotor ring of F-type Na -ATPase from Ilyobacter tartaricus. Science 308, 659-662. (Pubitemid 40594380)
    • (2005) Science , vol.308 , Issue.5722 , pp. 659-662
    • Meier, T.1    Polzer, P.2    Diederichs, K.3    Welte, W.4    Dimroth, P.5
  • 160
    • 27644486110 scopus 로고    scopus 로고
    • 11 ring stoichiometry in the sodium F-ATP synthase
    • DOI 10.1111/j.1742-4658.2005.04940.x
    • MEIER, T., YU, J., RASCHLE, T., HENZEN, F., DIMROTH, P. & MULLER, D.J. (2005b). Structural evidence for a constant c11 ring stoichiometry in the sodium F-ATP synthase. FEBSJournal 272, 5474-5483. (Pubitemid 41579409)
    • (2005) FEBS Journal , vol.272 , Issue.21 , pp. 5474-5483
    • Meier, T.1    Yu, J.2    Raschle, T.3    Henzen, F.4    Dimroth, P.5    Muller, D.J.6
  • 161
    • 0035838982 scopus 로고    scopus 로고
    • 1-ATPase with nucleotide bound to all three catalytic sites: Implications for the mechanism of rotary catalysis
    • DOI 10.1016/S0092-8674(01)00452-4
    • MENZ, R. I., WALKER, J. E. & LESLIE, A. G. W. (2001). Structure of bovine mitochondrial F-ATPase with nucleotide bound to all three catalytic sites: implications for the mechanism of rotary catalysis. Cell106, 331-341. (Pubitemid 32772617)
    • (2001) Cell , vol.106 , Issue.3 , pp. 331-341
    • Menz R.Ian1    Walker, J.E.2    Leslie, A.G.W.3
  • 162
    • 77957307407 scopus 로고    scopus 로고
    • N-terminal domain of V-ATPase a2-subunit displays integral membrane protein properties
    • MERKULOVA, M., MCKEE, M., DIP, P. V., GRUBER, G. & MARSHANSKY, V. (2010). N-terminal domain of V-ATPase a2-subunit displays integral membrane protein properties. Protein Science 19, 1850-1862.
    • (2010) Protein Science , vol.19 , pp. 1850-1862
    • Merkulova, M.1    McKee, M.2    Dip, P.V.3    Gruber, G.4    Marshansky, V.5
  • 164
    • 0034714282 scopus 로고    scopus 로고
    • The multigene family of the tobacco hornworm V-ATPase: Novel subunits a, C, D, H, and putative isoforms
    • DOI 10.1016/S0005-2736(00)00233-9, PII S0005273600002339
    • MERZENDORFER, H., REINEKE, S., ZHAO, X.-F., JACOBMEIER, B., HARVEY, W. R. & WIECZOREK, H. (2000). The mul-tigene family of the tobacco hornworm V-ATPase: novel subunits a, C, D, H and putative isoforms. Biochimica et Biophysica Acta 1467, 369-379. (Pubitemid 30665590)
    • (2000) Biochimica et Biophysica Acta - Biomembranes , vol.1467 , Issue.2 , pp. 369-379
    • Merzendorfer, H.1    Reineke, S.2    Zhao, X.-F.3    Jacobmeier, B.4    Harvey, W.R.5    Wieczorek, H.6
  • 167
    • 36949083936 scopus 로고
    • Coupling of phosphorylation to electron and hydrogen transfer by a chemi-osmotic type of mechanism
    • MITCHELL, P. (1961). Coupling of phosphorylation to electron and hydrogen transfer by a chemi-osmotic type of mechanism. Nature 191, 144-148.
    • (1961) Nature , vol.191 , pp. 144-148
    • Mitchell, P.1
  • 168
    • 57649119786 scopus 로고    scopus 로고
    • Structural interactions between transmembrane helices 4 and 5 of subunit a and the subunit c ring of Escherichia coli ATP synthase
    • MOORE, K. J. & FILLINGAME, R. H. (2008). Structural interactions between transmembrane helices 4 and 5 of subunit a and the subunit c ring of Escherichia coli ATP synthase. Journal of Biological Chemistry 283, 31726-31735.
    • (2008) Journal of Biological Chemistry , vol.283 , pp. 31726-31735
    • Moore, K.J.1    Fillingame, R.H.2
  • 169
    • 0344444207 scopus 로고    scopus 로고
    • +ATPase
    • DOI 10.1016/S0248-4900(03)00075-3
    • MOREL, N. (2003). Neurotransmitter release: the dark side of the vacuolar-H+-ATPase. Biology of the Cell 95, 453-457. (Pubitemid 37441636)
    • (2003) Biology of the Cell , vol.95 , Issue.7 , pp. 453-457
    • Morel, N.1
  • 172
    • 35348829149 scopus 로고    scopus 로고
    • Inventing the dynamo machine: The evolution of the F-type and V-type ATPases
    • DOI 10.1038/nrmicro1767, PII NRMICRO1767
    • MULKIDJANIAN, A. Y., MAKAROVA, K. S., GALPERIN, M. Y. & KOONIN, E. V. (2007). Inventing the dynamo machine: the evolution of the F-type and V-type ATPases. Nature Reviews Microbiology 5, 892-899. (Pubitemid 47578390)
    • (2007) Nature Reviews Microbiology , vol.5 , Issue.11 , pp. 892-899
    • Mulkidjanian, A.Y.1    Makarova, K.S.2    Galperin, M.Y.3    Koonin, E.V.4
  • 173
    • 0037188741 scopus 로고    scopus 로고
    • 1-ATPase, the C-terminal end of subunit γ is not required for ATP hydrolysis-driven rotation
    • DOI 10.1074/jbc.M201998200
    • MÜLLER, M., PÄNKE, O., JUNGE, W. & ENGELBRECHT, S. (2002). F1-ATPase, the C-terminal end of subunit c is not required for ATP hydrolysis-driven rotation. Journal of Biological Chemistry 277, 23308-23313. (Pubitemid 34952160)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.26 , pp. 23308-23313
    • Muller, M.1    Panke, O.2    Junge, W.3    Engelbrecht, S.4
  • 174
    • 0037955289 scopus 로고    scopus 로고
    • ATP synthases: Structure, function and evolution of unique energy converters
    • DOI 10.1007/s000180300040
    • MÜLLER, V. & GRÜBER, G. (2003). ATP synthases: structure, function and evolution of unique energy converters. Cellular and Molecular Life Sciences 60, 474-494. (Pubitemid 36459527)
    • (2003) Cellular and Molecular Life Sciences , vol.60 , Issue.3 , pp. 474-494
    • Muller, V.1    Gruber, G.2
  • 175
    • 33646553630 scopus 로고    scopus 로고
    • ATP synthases with novel rotor subunits: New insights into structure, function and evolution of ATPases
    • DOI 10.1007/s10863-005-9491-y
    • MÜLLER, V., LINGL, A., LEWALTER, K. & FRITZ, M. (2005). ATP synthases with novel rotor subunits: new insights into structure, function and evolution of ATPases. Journal of Bioenergetics and Biomembranes 37, 455-460. (Pubitemid 43725176)
    • (2005) Journal of Bioenergetics and Biomembranes , vol.37 , Issue.6 , pp. 455-460
    • Muller, V.1    Lingl, A.2    Lewalter, K.3    Fritz, M.4
  • 176
    • 0032586729 scopus 로고    scopus 로고
    • 0-ATPases from methanogenic archaea
    • DOI 10.1023/A:1005451311009
    • MÜLLER, V., RUPPERT, C. & LEMKER, T. (1999). Structure and function of the A(1)A(0)-ATPases from methano-genic archaea. Journal of Bioenergetics and Biomembranes 31, 15-27. (Pubitemid 29203374)
    • (1999) Journal of Bioenergetics and Biomembranes , vol.31 , Issue.1 , pp. 15-27
    • Muller, V.1    Ruppert, C.2    Lemker, T.3
  • 178
    • 17844369968 scopus 로고    scopus 로고
    • +-ATPase from Enterococcus hirae
    • DOI 10.1126/science.1110064
    • MURATA, T., YAMATO, I., KAKINUMA, Y., LESLIE, A. G. W. & WALKER, J. E. (2005). Structure of the rotor of the V-type Na+-ATPase from Enterococcus hirae. Science 308, 654-659. (Pubitemid 40594379)
    • (2005) Science , vol.308 , Issue.5722 , pp. 654-659
    • Murata, T.1    Yamato, I.2    Kakinuma, Y.3    Leslie, A.G.W.4    Walker, J.E.5
  • 183
    • 34347238974 scopus 로고    scopus 로고
    • +-ATPase are linked by an interaction between the G and a subunits
    • DOI 10.1074/jbc.M701226200
    • NORGETT, E. E., BORTHWICK, K. J., AL LAMKI, R. S., SU, Y., SMITH, A. N. & KARET, F. E. (2007). V1 and V0 domains of the human H+-ATPase are linked by an interaction between the G and a subunits. Journal of Biological Chemistry 282, 14421-14427. (Pubitemid 47100461)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.19 , pp. 14421-14427
    • Norgett, E.E.1    Borthwick, K.J.2    Al-Lamki, R.S.3    Su, Y.4    Smith, A.N.5    Karet, F.E.6
  • 184
    • 70449115562 scopus 로고    scopus 로고
    • 1 -ATPase
    • NUMOTO, N., HASEGAWA, Y., TAKEDA, K. & MIKI, K. (2009). Inter-subunit interaction and quaternary rearrangement defined by the central stalk of prokaryotic V1-ATPase. EMBO Reports 10, 1228-1234.
    • (2009) EMBO Reports , vol.10 , pp. 1228-1234
    • Numoto, N.1    Hasegawa, Y.2    Takeda, K.3    Miki, K.4
  • 185
    • 0030959251 scopus 로고    scopus 로고
    • 0 parts of the Escherichia coli ATP synthase
    • DOI 10.1074/jbc.272.26.16652
    • OGILVIE, I., AGGELER, R. & CAPALDI, R. A. (1997). Cross-linking of the d subunit to one of the three a subunits has no effect on functioning, as expected if d is a part of the stator that links the F1 and F0 parts of the Escherichia coli ATP synthase. Journal of Biological Chemistry 272, 16652-16656. (Pubitemid 27276498)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.26 , pp. 16652-16656
    • Ogilvie, I.1    Aggeler, R.2    Capaldi, R.A.3
  • 187
    • 77955298786 scopus 로고    scopus 로고
    • Domain characterization and interaction of the yeast vacuolar ATPase subunit C with the peripheral stator stalk subunits e and G
    • OOT, R. A. & WILKENS, S. (2010). Domain characterization and interaction of the yeast vacuolar ATPase subunit C with the peripheral stator stalk subunits E and G. Journal of Biological Chemistry 285, 24654-24664.
    • (2010) Journal of Biological Chemistry , vol.285 , pp. 24654-24664
    • Oot, R.A.1    Wilkens, S.2
  • 188
    • 0034738090 scopus 로고    scopus 로고
    • Reverse engineering a protein: The mechanochemistry of ATP synthase
    • DOI 10.1016/S0005-2728(00)00096-7, PII S0005272800000967
    • OSTER, G. & WANG, H. Y. (2000a). Reverse engineering a protein: the mechanochemistry of ATP synthase. Biochimica et Biophysica Acta 1458, 482-510. (Pubitemid 30320727)
    • (2000) Biochimica et Biophysica Acta - Bioenergetics , vol.1458 , Issue.2-3 , pp. 482-510
    • Oster, G.1    Wang, H.2
  • 189
  • 191
    • 2442496477 scopus 로고    scopus 로고
    • Incorporation of the V-ATPase inhibitors concanamycin and indole pentadiene in lipid membranes. Spin-label EPR studies
    • DOI 10.1016/j.bbamem.2004.03.003, PII S0005273604000811
    • PALI, T., DIXON, N., KEE, T. P. & MARSH, D. (2004). Incorporation of the V-ATPase inhibitors con-canamycin and indole pentadiene in lipid membranes. Spin-label EPR studies. Biochimica et Biophysica Acta 1663, 14-18. (Pubitemid 38625577)
    • (2004) Biochimica et Biophysica Acta - Biomembranes , vol.1663 , Issue.1-2 , pp. 14-18
    • Pali, T.1    Dixon, N.2    Kee, T.P.3    Marsh, D.4
  • 192
    • 0034866072 scopus 로고    scopus 로고
    • Viscoelastic dynamics of actin filaments coupled to rotary F-ATPase: Angular torque profile of the enzyme
    • PÄNKE, O., CHEREPANOV, D.A., GUMBIOWSKI, K., ENGELBRECHT, S. & JUNGE, W. (2001). Viscoelastic dynamics of actin filaments coupled to rotary F-ATPase: angular torque profile of the enzyme. Biophysical Journal 81, 1220-1233. (Pubitemid 32783567)
    • (2001) Biophysical Journal , vol.81 , Issue.3 , pp. 1220-1233
    • Panke, O.1    Cherepanov, D.A.2    Gumbiowski, K.3    Engelbrecht, S.4    Junge, W.5
  • 193
    • 0034647941 scopus 로고    scopus 로고
    • 1 complexes
    • DOI 10.1074/jbc.M002305200
    • PARRA, K. J., KEENAN, K. L. & KANE, P. M. (2000). The H subunit (Vma13p) of the yeast V-ATPase inhibits the ATPase activity of cytosolic V1 complexes. Journal of Biological Chemistry 275, 21761-21767. (Pubitemid 30481886)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.28 , pp. 21761-21767
    • Parra, K.J.1    Keenan, K.L.2    Kane, P.M.3
  • 194
    • 33644847296 scopus 로고    scopus 로고
    • Estimation of variance in single particle reconstruction using the bootstrap technique
    • PENCZEK, P. A., CHAO, Y., FRANK, J. & SPAHN, C. M. T. (2006). Estimation of variance in single particle reconstruction using the bootstrap technique. Journal of Structural Biology 154, 168-183.
    • (2006) Journal of Structural Biology , vol.154 , pp. 168-183
    • Penczek, P.A.1    Chao, Y.2    Frank, J.3    Spahn, C.M.T.4
  • 195
    • 34447629933 scopus 로고    scopus 로고
    • O ATP synthase from the hyperthermophilic archaeon Pyrococcus furiosus
    • DOI 10.1111/j.1742-4658.2007.05925.x
    • PISA, K. Y., HUBER, H., THOM, M. & MÜLLER, V. (2007a). A sodium ion-dependent A1A0 ATP synthase from the hyperthermophilic archaeon Pyrococcus furiosus. FEBS Journal 274, 3928-3938. (Pubitemid 47087680)
    • (2007) FEBS Journal , vol.274 , Issue.15 , pp. 3928-3938
    • Pisa, K.Y.1    Huber, H.2    Thomm, M.3    Muller, V.4
  • 196
    • 35748984933 scopus 로고    scopus 로고
    • o ATP synthase from the archaeon Methanosarcina mazei Gö1
    • DOI 10.1111/j.1574-6968.2007.00939.x
    • PISA, K. Y., WEIDNER, C., MAISCHAK, H., KAVERMANN, H. & MÜLLER, V. (2007b). The coupling ion in the metha-noarchaeal ATP synthases: H+ vs. Na+ in the A(1)A(0) ATP synthase from the archaeon Methanosarcina mazei Gö1. FEMS Microbiology Letters 277, 56-63. (Pubitemid 350045658)
    • (2007) FEMS Microbiology Letters , vol.277 , Issue.1 , pp. 56-63
    • Pisa, K.Y.1    Weidner, C.2    Maischak, H.3    Kavermann, H.4    Muller, V.5
  • 197
    • 34547732425 scopus 로고    scopus 로고
    • The oligomeric state of c rings from cyanobacterial F-ATP synthases varies from 13 to 15
    • DOI 10.1128/JB.00581-07
    • POGORYELOV, D., REICHEN, C., KLYSZEJKO, A.L., BRUNISHOLZ, R., MULLER, D. J., DIMROTH, P. & MEIER, T. (2007). The oligomeric state of c rings from cyano-bacterial F-ATP synthases varies from 13 to 15. Journal of Bacteriology 189, 5895-5902. (Pubitemid 47236142)
    • (2007) Journal of Bacteriology , vol.189 , Issue.16 , pp. 5895-5902
    • Pogoryelov, D.1    Reichen, C.2    Klyszejko, A.L.3    Brunisholz, R.4    Muller, D.J.5    Dimroth, P.6    Meier, T.7
  • 198
    • 27644566520 scopus 로고    scopus 로고
    • 0 symmetry mismatch is not obligatory
    • DOI 10.1038/sj.embor.7400517, PII 7400517
    • POGORYELOV, D., YU, J., MEIER, T., VONCK, J., DIMROTH, P. & MULLER, D. J. (2005). The c15 ring of the Spirulina platensis F-ATP synthase: F1/F0 symmetry mismatch is not obligatory. EMBO Reports 6, 1040-1044. (Pubitemid 41637648)
    • (2005) EMBO Reports , vol.6 , Issue.11 , pp. 1040-1044
    • Pogoryelov, D.1    Yu, J.2    Meier, T.3    Vonck, J.4    Dimroth, P.5    Muller, D.J.6
  • 199
    • 0034604676 scopus 로고    scopus 로고
    • +-ATPase proton pore
    • DOI 10.1074/jbc.M004440200
    • POWELL, B., GRAHAM, L. A. & STEVENS, T. H. (2000). Molecular characterization of the yeast vacuolar H+-ATPase proton pore. Journal of Biological Chemistry 275, 23654-23660. (Pubitemid 30627454)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.31 , pp. 23654-23660
    • Powell, B.1    Graham, L.A.2    Stevens, T.H.3
  • 201
    • 0000228422 scopus 로고
    • A naturally occurring inhibitor of mitochondrial adenosine tripho-sphatase
    • PULLMAN, M. E. & MONROY, G. C. (1963). A naturally occurring inhibitor of mitochondrial adenosine tripho-sphatase. Journal of Biological Chemistry 238, 3762-3769.
    • (1963) Journal of Biological Chemistry , vol.238 , pp. 3762-3769
    • Pullman, M.E.1    Monroy, G.C.2
  • 202
    • 50349103459 scopus 로고    scopus 로고
    • Function and subunit interactions of the N-terminal domain of subunit a (Vph1p) of the yeast V-ATPase
    • QI, J. & FORGAC, M. (2008). Function and subunit interactions of the N-terminal domain of subunit a (Vph1p) of the yeast V-ATPase. Journal of Biological Chemistry 283, 19274-19282.
    • (2008) Journal of Biological Chemistry , vol.283 , pp. 19274-19282
    • Q, I.J.1    Forgac, M.2
  • 204
    • 0033607683 scopus 로고    scopus 로고
    • 0-ATPase operon from Acetobacterium woodii: Operon structure and presence of multiple copies of atpE which encode proteolipids of 8- and 18-kDa
    • RAHLFS, S., AUFURTH, S. & MÜLLER, V. (1999). The Na+-F1F0-ATPase operon from Acetobacterium woodii. Operon structure and presence of multiple copies of atpE which encode proteolipids of 8- and 18-kDa. Journal of Biological Chemistry 274, 33999-34004. (Pubitemid 129511731)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.48 , pp. 33999-34004
    • Rahlfs, S.1    Aufurth, S.2    Muller, V.3
  • 205
    • 0033581879 scopus 로고    scopus 로고
    • Structural changes linked to proton translocation by subunit c of the ATP synthase
    • RASTOGI, V. K. & GIRVIN, M. E. (1999). Structural changes linked to proton translocation by subunit c in the ATP synthase. Nature 402, 263-268. (Pubitemid 129516255)
    • (1999) Nature , vol.402 , Issue.6759 , pp. 263-268
    • Rastogi, V.K.1    Girbvin, M.E.2
  • 209
    • 0032491567 scopus 로고    scopus 로고
    • 1 via an α-subunit in the Escherichia coli ATP synthase
    • DOI 10.1074/jbc.273.45.29406
    • RODGERS, A. J. W. & CAPALDI, R. A. (1998). The second stalk composed of the b- and delta-subunits connects F0 to F1 via and alpha-subunit in the Escherichia coli ATP synthase. Journal of Biological Chemistry 273, 29406-29410. (Pubitemid 28509942)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.45 , pp. 29406-29410
    • Rodgers, A.J.W.1    Capaldi, R.A.2
  • 213
    • 0142042865 scopus 로고    scopus 로고
    • Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy
    • DOI 10.1016/j.jmb.2003.07.013
    • ROSENTHAL, P. B. & HENDERSON, R. (2003). Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy. Journal of Molecular Biology 333, 721-745. (Pubitemid 37268015)
    • (2003) Journal of Molecular Biology , vol.333 , Issue.4 , pp. 721-745
    • Rosenthal, P.B.1    Henderson, R.2
  • 214
    • 0347504884 scopus 로고    scopus 로고
    • Structure of the mitochondrial ATP synthase by electron cryomicroscopy
    • DOI 10.1093/emboj/cdg608
    • RUBINSTEIN, J. L., WALKER, J. E. & HENDERSON, R. (2003). Structure of the mitochondrial ATP synthase by electron cryomicroscopy. EMBO Journal 22, 6182-6192. (Pubitemid 37522576)
    • (2003) EMBO Journal , vol.22 , Issue.23 , pp. 6182-6192
    • Rubinstein, J.L.1    Walker, J.E.2    Henderson, R.3
  • 215
    • 0029893335 scopus 로고    scopus 로고
    • Intersubunit rotation in active F-ATPase
    • DOI 10.1038/381623a0
    • SABBERT, D., ENGELBRECHT, S. & JUNGE, W. (1996). Intersubunit rotation in active F-ATPase. Nature 381, 623-625. (Pubitemid 26177481)
    • (1996) Nature , vol.381 , Issue.6583 , pp. 623-625
    • Sabbert, D.1    Engelbrecht, S.2    Junge, W.3
  • 217
    • 2342435823 scopus 로고    scopus 로고
    • The Yeast Vacuolar Proton-translocating ATPase Contains a Subunit Homologous to the Manduca sexta and Bovine e Subunits That Is Essential for Function
    • DOI 10.1074/jbc.M314104200
    • SAMBADE, M. & KANE, P. M. (2004). The yeast vacuolar proton-translocating ATPase contains a subunit homologous to the Manduca sexta and bovine e subunits that is essential for function. Journal of Biological Chemistry 279, 17361-17365. (Pubitemid 38560496)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.17 , pp. 17361-17365
    • Sambade, M.1    Kane, P.M.2
  • 220
    • 33845939047 scopus 로고    scopus 로고
    • Disentangling conformational states of macromolecules in 3D-EM through likelihood optimization
    • DOI 10.1038/nmeth992, PII NMETH992
    • SCHERES, S. H. W., GAO, H., VALLE, M., HERMAN, G. T., EGGERMONT, P. P. B., FRANK, J. & CARAZO, J.-M. (2006). Disentangling conformational states of macromolecules in 3D-EM through likelihood optimization. Nature Methods 4, 27-29. (Pubitemid 46029470)
    • (2007) Nature Methods , vol.4 , Issue.1 , pp. 27-29
    • Scheres, S.H.W.1    Gao, H.2    Valle, M.3    Herman, G.T.4    Eggermont, P.P.B.5    Frank, J.6    Carazo, J.-M.7
  • 221
    • 33845989502 scopus 로고    scopus 로고
    • Cross-linking between helices within subunit a of Escherichia coli ATP synthase defines the transmembrane packing of a four-helix bundle
    • DOI 10.1074/jbc.M607453200
    • SCHWEM, B. E. & FILLINGAME, R. H. (2006). Cross-linking between helices within subunit a of Escherichia coli ATP synthase defines the transmembrane packing of a four-helix bundle. Journal of Biological Chemistry 281, 37861-37867. (Pubitemid 46042089)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.49 , pp. 37861-37867
    • Schwem, B.E.1    Fillingame, R.H.2
  • 222
    • 0034713072 scopus 로고    scopus 로고
    • Proton-powered turbine of a plant motor
    • DOI 10.1038/35013148
    • SEELERT, H., POETSCH, A., DENCHER, N. A., ENGEL, A., STAHLBERG, H. & MÜLLER, D. J. (2000). Structural biology: proton-powered turbine of a plant motor. Nature 405, 418-419. (Pubitemid 30367410)
    • (2000) Nature , vol.405 , Issue.6785 , pp. 418-419
    • Seelert, H.1    Poetsch, A.2    Dencher, N.A.3    Engel, A.4    Stahlberg, H.5    Muller, D.J.6
  • 225
    • 10344240424 scopus 로고    scopus 로고
    • Involvement of the nonhomologous region of subunit A of the yeast V-ATPase in coupling and in vivo dissociation
    • DOI 10.1074/jbc.M408278200
    • SHAO, E. & FORGAC, M. (2004). Involvement of the non-homologous region of subunit A of the yeast V-ATPase in coupling and in vivo dissociation. Journal of Biological Chemistry 279, 48663-48670. (Pubitemid 39625742)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.47 , pp. 48663-48670
    • Shao, E.1    Forgac, M.2
  • 226
    • 0037630395 scopus 로고    scopus 로고
    • Mutational analysis of the non-homologous region of subunit A of the yeast V-ATPase
    • DOI 10.1074/jbc.M212096200
    • SHAO, E., NISHI, T., KAWASAKI-NISHI, S. & FORGAC, M. (2003). Mutational analysis of the non-homologous region of subunit A of the yeast V-ATPase. Journal of Biological Chemistry 278, 12985-12991. (Pubitemid 36800065)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.15 , pp. 12985-12991
    • Shao, E.1    Nishi, T.2    Kawasaki-Nishi, S.3    Forgac, M.4
  • 227
    • 56649096812 scopus 로고    scopus 로고
    • 1-ATPase correlated with crystal structures
    • SIELAFF, H., RENNEKAMP, H., ENGELBRECHT, S. & JUNGE, W. (2008a). Functional halt positions of rotary F0F1-ATPase correlated with crystal structures. Biophysical Journal 95, 4979-4987.
    • (2008) Biophysical Journal , vol.95 , pp. 4979-4987
    • Sielaff, H.1    Rennekamp, H.2    Engelbrecht, S.3    Junge, W.4
  • 232
    • 0032561169 scopus 로고    scopus 로고
    • 0-ATP synthase in Escherichia coli
    • DOI 10.1074/jbc.273.43.27873
    • SORGEN, P. L., CAVISTON, T. L., PERRY, R. C. & CAIN, B. D. (1998). Deletions in the second stalk of F1F0-ATP synthase in Escherichia coli. Journal of Biological Chemistry 273, 27873-27878. (Pubitemid 28496075)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.43 , pp. 27873-27878
    • Sorgen, P.L.1    Caviston, T.L.2    Perry, R.C.3    Cain, B.D.4
  • 233
    • 0037155894 scopus 로고    scopus 로고
    • In the absence of the first membrane-spanning segment of subunit 4(b), the yeast ATP synthase is functional but does not dimerize or oligomerize
    • DOI 10.1074/jbc.M111882200
    • SOUBANNIER, V., VAILLIER, J., PAUMARD, P., COULARY, B., SCHAEFFER, J. & VELOURS, J. (2002). In the absence of the first membrane-spanning segment of subunit 4(b), the yeast ATP synthase is functional but does not di-merize or oligomerize. Journal of Biological Chemistry 277, 10739-10745. (Pubitemid 34968202)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.12 , pp. 10739-10745
    • Soubannier, V.1    Vaillier, J.2    Paumard, P.3    Coulary, B.4    Schaeffer, J.5    Velours, J.6
  • 236
    • 0033607504 scopus 로고    scopus 로고
    • Molecular architecture of the rotary motor in ATP synthase
    • STOCK, D., LESLIE, A. G. W. & WALKER, J. E. (1999). Molecular architecture of the rotary motor in ATP synthase. Science 286, 1700-1705. (Pubitemid 129515869)
    • (1999) Science , vol.286 , Issue.5445 , pp. 1700-1705
    • Stock, D.1    Leslie, A.G.W.2    Walker, J.E.3
  • 237
    • 41949123425 scopus 로고    scopus 로고
    • Dimer ribbons of ATP synthase shape the inner mitochondrial membrane
    • DOI 10.1038/emboj.2008.35, PII EMBOJ200835
    • STRAUSS, M., HOFHAUS, G., SCHRÖDER, R.R. & KÜHLBRANDT, W. (2008). Dimer ribbons of ATP syn-thase shape the inner mitochondrial membrane. EMBO Journal 27, 1154-1160. (Pubitemid 351508145)
    • (2008) EMBO Journal , vol.27 , Issue.7 , pp. 1154-1160
    • Strauss, M.1    Hofhaus, G.2    Schroder, R.R.3    Kuhlbrandt, W.4
  • 238
    • 57049106773 scopus 로고    scopus 로고
    • Supercomplex organization of the oxi-dative phosphorylation enzymes in yeast mitochondria
    • STUART, R. (2008). Supercomplex organization of the oxi-dative phosphorylation enzymes in yeast mitochondria. Journal of Bioenergetics and Biomembranes 40, 411-417.
    • (2008) Journal of Bioenergetics and Biomembranes , vol.40 , pp. 411-417
    • Stuart, R.1
  • 239
    • 0038165450 scopus 로고    scopus 로고
    • +-ATPase interacts with phosphofructokinase-1 in humans
    • DOI 10.1074/jbc.M210077200
    • SU, Y., ZHOU, A., AL LAMKI, R. S. & KARET, F. E. (2003). The a-subunit of the V-type H+-ATPase interacts with phosphofructokinase-1 in humans. Journal of Biological Chemistry 278, 20013-20018. (Pubitemid 36799194)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.22 , pp. 20013-20018
    • Su, Y.1    Zhou, A.2    Al-Lamki, R.S.3    Karet, F.E.4
  • 240
    • 0026724398 scopus 로고
    • 1-ATPase β subunit was amplified from genomic DNA of Methanosarcina barkeri. Indication of an archaebacterial F-type ATPase
    • DOI 10.1016/0014-5793(92)81472-X
    • SUMI, M., SATO, M.H., DENDA, K., DATE, T. & YOSHIDA, M. (1992). A DNA fragment homologous to F1-ATPase b subunit was amplified from genomic DNA of Methanosarcina barkeri. Indication of an archae-bacterial F-type ATPase. FEBS Letters 314, 207-210. (Pubitemid 23005656)
    • (1992) FEBS Letters , vol.314 , Issue.3 , pp. 207-210
    • Sumi, M.1    Sato, M.H.2    Denda, K.3    Date, T.4    Yoshida, M.5
  • 242
    • 0347363559 scopus 로고    scopus 로고
    • 1-ATPase
    • DOI 10.1007/s00249-003-0335-6
    • SUN, S., CHANDLER, D., DINNER, A. R. & OSTER, G. (2003). Elastic energy storage in beta-sheets with application to F-1-ATPase. European Biophysics Journal 32, 676-683. (Pubitemid 38031354)
    • (2003) European Biophysics Journal , vol.32 , Issue.8 , pp. 676-683
    • Sun, S.1    Chandler, D.2    Dinner, A.R.3    Oster, G.4
  • 244
    • 0000729527 scopus 로고    scopus 로고
    • +-ATPase related to the b subunit of F-ATpases
    • SUPEKOVA, L., SBIA, M., SUPEK, F., MA, Y. M. & NELSON, N. (1996). A novel subunit of vacuolar H+-ATPase related to the b-subunit of F-ATPases. Journal of Experimental Biology 199, 1147-1156. (Pubitemid 126603379)
    • (1996) Journal of Experimental Biology , vol.199 , Issue.5 , pp. 1147-1156
    • Supekova, L.1    Sbia, M.2    Supek, F.3    Ma, Y.4    Nelson, N.5
  • 245
    • 0032558934 scopus 로고    scopus 로고
    • 1 ATPase: Significance of structural homologies and diversities
    • DOI 10.1021/bi982367a
    • SVERGUN, D. I., KONRAD, S., HUSS, M., KOCH, M. H. J., WIECZOREK, H., ALTENDORF, K., VOLKOV, V.V. & GRÜBER, G. (1998). Quaternary structure of V1 and F1 ATPase: significance of structural homologies and diversities. Biochemistry 37, 17659-17663. (Pubitemid 29023920)
    • (1998) Biochemistry , vol.37 , Issue.51 , pp. 17659-17663
    • Svergun, D.I.1    Konrad, S.2    Huss, M.3    Koch, M.-H.J.4    Wieczorek, H.5    Altendorf, K.6    Volkov, V.V.7    Gruber, G.8
  • 246
    • 0027245710 scopus 로고
    • 1-type ATPases in one bacterial cell
    • TAKASE, K., YAMATO, I. & KAKINUMA, Y. (1993). Cloning and sequencing of the genes coding for the A and B subunits of vacuolar-type Na(+)-ATPase from Enterococcus hirae. Coexistence of vacuolar- and F0F1-type ATPases in one bacterial cell. Journal of Biological Chemistry 268, 11610-11616. (Pubitemid 23168108)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.16 , pp. 11610-11616
    • Takase, K.1    Yamato, I.2    Kakinuma, Y.3
  • 247
    • 0030603142 scopus 로고    scopus 로고
    • 1-ATPase in reconstituted membranes using atomic force microscopy
    • DOI 10.1016/0014-5793(96)00796-X
    • TAKEYASU, K., OMOTE, H., NETTIKADAN, S., TOKUMASU, F., IWAMOTO-KIHARA, A. & FUTAI, M. (1996). Molecular imaging of Escherichia coli F0F1-ATPase in reconstituted membranes using atomic force microscopy. FEBS Letters 392, 110-113. (Pubitemid 26276729)
    • (1996) FEBS Letters , vol.392 , Issue.2 , pp. 110-113
    • Takeyasu, K.1    Omote, H.2    Nettikadan, S.3    Tokumasu, F.4    Iwamoto-Kihara, A.5    Futai, M.6
  • 248
    • 35648986678 scopus 로고    scopus 로고
    • The boxing glove shape of subunit d of the yeast V-ATPase in solution and the importance of disulfide formation for folding of this protein
    • DOI 10.1007/s10863-007-9089-7
    • THAKER, Y., ROESSLE, M., & GRÜBER, G. (2007). The boxing glove shape of subunit d of the yeast V-ATPase in solution and the importance of disulfide formation for folding of this protein. Journal of Bioenergetics and Biomembranes 39, 275-289. (Pubitemid 350029427)
    • (2007) Journal of Bioenergetics and Biomembranes , vol.39 , Issue.4 , pp. 275-289
    • Thaker, Y.R.1    Roessle, M.2    Gruber, G.3
  • 250
    • 77953255215 scopus 로고    scopus 로고
    • Regulation and isoform function of the V-ATPases
    • TOEI, M., SAUM, R. & FORGAC, M. (2010). Regulation and isoform function of the V-ATPases. Biochemistry 49, 4715-4723.
    • (2010) Biochemistry , vol.49 , pp. 4715-4723
    • Toei, M.1    Saum, R.2    Forgac, M.3
  • 251
    • 0034468564 scopus 로고    scopus 로고
    • Stoichiometry of energy coupling by proton-translocating ATPases: A history of variability
    • DOI 10.1023/A:1005617024904
    • TOMASHEK, J.J. & BRUSILOW, W.S.A. (2000). Stoichiometry of energy coupling by proton-translocating ATPases: a history of variability. Journal of Bioenergetics and Biomembranes 32, 493-500. (Pubitemid 32204247)
    • (2000) Journal of Bioenergetics and Biomembranes , vol.32 , Issue.5 , pp. 493-500
    • Tomashek, J.J.1    Brusilow, W.S.A.2
  • 254
    • 0030611634 scopus 로고    scopus 로고
    • Crystal structure of the ε subunit of the proton-translocating ATP synthase from Escherichia coli
    • UHLIN, U., COX, G. B. & GUSS, J. M. (1997). Crystal structure of the e subunit of the proton-translocating ATP synthase from Escherichia coli. Structure 5, 1219-1230. (Pubitemid 27416029)
    • (1997) Structure , vol.5 , Issue.9 , pp. 1219-1230
    • Uhlin, U.1    Cox, G.B.2    Guss, J.M.3
  • 256
    • 0031464314 scopus 로고    scopus 로고
    • 1-ATP synthase
    • DOI 10.1074/jbc.272.51.32635
    • VALIYAVEETIL, F. I. & FILLINGAME, R. H. (1997). On the role of Arg-210 and Glu-219 of subunit a in proton translocation by the Escherichia coli F0F1-ATP synthase. Journal of Biological Chemistry 272, 32635-32641. (Pubitemid 28011954)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.51 , pp. 32635-32641
    • Valiyaveetil, F.I.1    Fillingame, R.H.2
  • 257
    • 19444381126 scopus 로고    scopus 로고
    • Elucidation of the stator organization in the V-ATPase of Neurospora crassa
    • DOI 10.1016/j.jmb.2005.04.033, PII S0022283605004420
    • VENZKE, D., DOMGALL, I., KOCHER, T., FÉTHIÈRE, J., FISCHER, S. & BÖTTCHER, B. (2005). Elucidation of the stator organization in the V-ATPase of Neurospora crassa. Journal of Molecular Biology 349, 659-669. (Pubitemid 40724572)
    • (2005) Journal of Molecular Biology , vol.349 , Issue.3 , pp. 659-669
    • Venzke, D.1    Domgall, I.2    Kocher, T.3    Fethiere, J.4    Fischer, S.5    Bottcher, B.6
  • 258
    • 0027970177 scopus 로고
    • 0 ATP synthases suggested by double mutants of the a subunit
    • VIK, S. B. & ANTONIO, B. J. (1994). A mechanism of proton translocation by F1F0 ATP synthases suggested by double mutants of the a subunit. Journal of Biological Chemistry 269, 30364-30369. (Pubitemid 24376512)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.48 , pp. 30364-30369
    • Vik, S.B.1    Antonio, B.J.2
  • 259
    • 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
    • DOI 10.1016/S0005-2728(00)00094-3, PII S0005272800000943
    • VIK, S. B., LONG, J. C., WADA, T. & ZHANG, D. (2000). A model for the structure of subunit a of the Escherichia coli ATP synthase and its role in proton translocation. Biochimica et Biophysica Acta 1458, 457-466. (Pubitemid 30320725)
    • (2000) Biochimica et Biophysica Acta - Bioenergetics , vol.1458 , Issue.2-3 , pp. 457-466
    • Vik, S.B.1    Long, J.C.2    Wada, T.3    Zhang, D.4
  • 260
    • 0032568844 scopus 로고    scopus 로고
    • 245 and implications on gating of the proton channel
    • DOI 10.1074/jbc.273.26.16229
    • VIK, S. B., PATTERSON, A. R. & ANTONIO, B. J. (1998). Insertion scanning mutagenesis of subunit a of the F1F0 ATP synthase near His245 and implications on gating of the proton channel. Journal of Biological Chemistry 273, 16229-16234. (Pubitemid 28311398)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.26 , pp. 16229-16234
    • Vik, S.B.1    Patterson, A.R.2    Antonio, B.J.3
  • 262
    • 67650546998 scopus 로고    scopus 로고
    • Structure of the c(14) rotor ring of the proton translocating chloroplast ATP synthase
    • VOLLMAR, M., SCHLIEPER, D., WINN, M., BÜCHNER, C. & GROTH, G. (2009). Structure of the c(14) rotor ring of the proton translocating chloroplast ATP synthase. Journal of Biological Chemistry 284, 18228-18235.
    • (2009) Journal of Biological Chemistry , vol.284 , pp. 18228-18235
    • Vollmar, M.1    Schlieper, D.2    Winn, M.3    Büchner, C.4    Groth, G.5
  • 266
    • 65649105054 scopus 로고    scopus 로고
    • 0ATP synthase from the hyperthermophilic archeon Pyrococcus furiosus by electron microscopy
    • VONCK, J., PISA, K.Y., MORGNER, N., BRUTSCHY, B. & MÜLLER, V. (2009). Three-dimensional structure of A1A0ATP synthase from the hyperthermophilic archeon Pyrococcus furiosus by electron microscopy. Journal of Biological Chemistry 284, 10110-10119.
    • (2009) Journal of Biological Chemistry , vol.284 , pp. 10110-10119
    • Vonck, J.1    Pisa, K.Y.2    Morgner, N.3    Brutschy, B.4    Müller, V.5
  • 267
    • 36348958588 scopus 로고    scopus 로고
    • +-ATPase by protein kinase A
    • DOI 10.1074/jbc.M703368200
    • VOSS, M., VITAVSKA, O., WALZ, B., WIECZOREK, H. & BAUMANN, O. (2007). Stimulus-induced phosphorylation of vacuolar H+-ATPase by protein kinase A. Journal of Biological Chemistry 282, 33735-33742. (Pubitemid 350159537)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.46 , pp. 33735-33742
    • Voss, M.1    Vitavska, O.2    Walz, B.3    Wieczorek, H.4    Baumann, O.5
  • 269
    • 36349017907 scopus 로고    scopus 로고
    • Arrangement of subunits in the proteolipid ring of the V-ATPase
    • DOI 10.1074/jbc.M704331200
    • WANG, Y., CIPRIANO, D.J. & FORGAC, M. (2007). Arrangement of subunits in the proteolipid ring of the V-ATPase. Journal of Biological Chemistry 282, 34058-34065. (Pubitemid 350159463)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.47 , pp. 34058-34065
    • Wang, Y.1    Cipriano, D.J.2    Forgac, M.3
  • 270
    • 28844433952 scopus 로고    scopus 로고
    • Subunit a of the yeast V-ATPase participates in binding of bafilomycin
    • DOI 10.1074/jbc.M509106200
    • WANG, Y., INOUE, T. & FORGAC, M. (2005). Subunit a of the yeast V-ATPase participates in binding of bafilomycin. Journal of Biological Chemistry 280, 40481-40488. (Pubitemid 41780535)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.49 , pp. 40481-40488
    • Wang, Y.1    Inoue, T.2    Forgac, M.3
  • 271
    • 51049099817 scopus 로고    scopus 로고
    • Analysis of the membrane topology of transmembrane segments in the C-terminal hydrophobic domain of the yeast vacuolar ATPase subunit a (Vph1p) by chemical modification
    • WANG, Y., TOEI, M. & FORGAC, M. (2008). Analysis of the membrane topology of transmembrane segments in the C-terminal hydrophobic domain of the yeast vacuolar ATPase subunit a (Vph1p) by chemical modification. Journal of Biological Chemistry 283, 20696-20702.
    • (2008) Journal of Biological Chemistry , vol.283 , pp. 20696-20702
    • Wang, Y.1    Toei, M.2    Forgac, M.3
  • 272
    • 0029078025 scopus 로고
    • 0 part
    • WATTS, S. D., ZHANG, Y., FILLINGAME, R. H. & CAPALDI, R. A. (1995). The c subunit in the Escherichia coli ATP synthase complex (ECF1F0) extends through the stalk and contacts the c subunits of the F0 part. FEBS Letters 368, 235-238.
    • (1995) FEBS Letters , vol.368 , pp. 235-238
    • Watts, S.D.1    Zhang, Y.2    Fillingame, R.H.3    Capaldi, R.A.4
  • 273
    • 1642565143 scopus 로고    scopus 로고
    • 0-ATP Synthase
    • DOI 10.1074/jbc.M312576200
    • WEBER, J., WILKE-MOUNTS, S., NADANACIVA, S. & SENIOR, A. E. (2004). Quantitative determination of direct binding of b subunit to F1 in Escherichia coli F1F0-ATP synthase. Journal of Biological Chemistry 279, 11253-11258. (Pubitemid 38401621)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.12 , pp. 11253-11258
    • Weber, J.1    Wilke-Mounts, S.2    Nadanaciva, S.3    Senior, A.E.4
  • 274
    • 0344983330 scopus 로고    scopus 로고
    • A second generation apparatus for time-resolved electron cryo-microscopy using stepper motors and electrospray
    • DOI 10.1016/j.jsb.2003.09.027
    • WHITE, H.D., THIRUMURUGAN, K., WALKER, M.L. & TRINICK, J. (2003). A second generation apparatus for time resolved electron cryo-microscopy using stepper motors and electrospray. Journal of Structural Biology 144, 246-252. (Pubitemid 37468382)
    • (2003) Journal of Structural Biology , vol.144 , Issue.1-2 , pp. 246-252
    • White, H.D.1    Thirumurugan, K.2    Walker, M.L.3    Trinick, J.4
  • 275
    • 27744440748 scopus 로고    scopus 로고
    • +-ATPase bind with high affinity to the purified proteolipid subunit of the membrane domain
    • DOI 10.1021/bi051529h
    • WHYTESIDE, G., MEEK, P. J., BALL, S.K., DIXON, N., FINBOW, M.E., KEE, T.P., FINDLAY, J.B.C. & HARRISON, M. A. (2005). Concanamycin and indolyl pentadieneamide inhibitors of the vacuolar H+-ATPase bind with high affinity to the purified proteolipid subunit of the membrane domain. Biochemistry 44, 15024-15031. (Pubitemid 41612281)
    • (2005) Biochemistry , vol.44 , Issue.45 , pp. 15024-15031
    • Whyteside, G.1    Meek, P.J.2    Ball, S.K.3    Dixon, N.4    Finbow, M.E.5    Kee, T.P.6    Findlay, J.B.C.7    Harrison, M.A.8
  • 276
    • 0033179796 scopus 로고    scopus 로고
    • Animal plasma membrane energization by proton-motive V-ATPases
    • DOI 10.1002/(SICI)1521-1878(199908)21:8<637::AID-BIES3>3.0.CO;2-W
    • WIECZOREK, H., BROWN, D., GRINSTEIN, S., EHRENFELD, J. & HARVEY, W. R. (1999). Animal plasma membrane energization by proton-motive V-ATPases. BioEssays 21, 637-648. (Pubitemid 29384445)
    • (1999) BioEssays , vol.21 , Issue.8 , pp. 637-648
    • Wieczorek, H.1    Brown, D.2    Grinstein, S.3    Ehrenfeld, J.4    Harvey, W.R.5
  • 277
  • 278
    • 0032311089 scopus 로고    scopus 로고
    • 0 parts of the Escherichia coli ATP synthase
    • DOI 10.1016/S0005-2728(98)00048-6, PII S0005272898000486
    • WILKENS, S. & CAPALDI, R. (1998). Electron microscopic evidence of two stalks linking the F1 and F0 parts of the Escherichia coli ATP synthase. Biochimica et Biophysica Acta 1365, 93-97. (Pubitemid 29359244)
    • (1998) Biochimica et Biophysica Acta - Bioenergetics , vol.1365 , Issue.1-2 , pp. 93-97
    • Wilkens, S.1    Capaldi, R.A.2
  • 279
    • 0028052574 scopus 로고
    • Asymmetry and structural changes in ECF1 examined by cryoelectronmicroscopy
    • WILKENS, S. & CAPALDI, R. A. (1994). Asymmetry and structural-changes in EcF(1) examined by cryoelec-tronmicroscopy. Biological Chemistry Hoppe-Seyler 375, 43-51. (Pubitemid 2043859)
    • (1994) Biological Chemistry Hoppe-Seyler , vol.375 , Issue.1 , pp. 43-51
    • Wilkens, S.1    Capaldi, R.A.2
  • 280
    • 0035941232 scopus 로고    scopus 로고
    • Three-dimensional structure of the vacuolar ATPase proton channel by electron microscopy
    • WILKENS, S. & FORGAC, M. (2001). Three-dimensional structure of the vacuolar ATPase proton channel by electron microscopy. Journal of Biological Chemistry 276, 44064-44068.
    • (2001) Journal of Biological Chemistry , vol.276 , pp. 44064-44068
    • Wilkens, S.1    Forgac, M.2
  • 281
    • 4744375526 scopus 로고    scopus 로고
    • Three-dimensional structure of the vacuolar ATPase: Localization of
    • DOI 10.1074/jbc.M407821200
    • WILKENS, S., INOUE, T. & FORGAC, M. (2004). Three-dimensional structure of the vacuolar ATPase: localization of subunit H by difference imaging and chemical cross-linking. Journal of Biological Chemistry 279, 41942-41949. (Pubitemid 39313644)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.40 , pp. 41942-41949
    • Wilkens, S.1    Inoue, T.2    Forgac, M.3
  • 282
  • 283
  • 284
    • 0032829686 scopus 로고    scopus 로고
    • Subunit interactions in the clathrin-coated vesicle vacuolar (H+)- ATPase complex
    • XU, T., VASILYEVA, E. & FORGAC, M. (1999). Subunit interactions in the clathrin-coated vesicle vacuolar (H+)- ATPase complex. Journal of Biological Chemistry 274, 28909-28915.
    • (1999) Journal of Biological Chemistry , vol.274 , pp. 28909-28915
    • X, U.T.1    Vasilyeva, E.2    Forgac, M.3
  • 289
    • 0035912221 scopus 로고    scopus 로고
    • 1-ATPase
    • DOI 10.1038/35073513
    • YASUDA, R., NOJI, H., YOSHIDA, M., KINOSITA, K. & ITOH, H. (2001). Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPase. Nature 410, 898-904. (Pubitemid 32335828)
    • (2001) Nature , vol.410 , Issue.6831 , pp. 898-904
    • Yasuda, R.1    Noji, H.2    Yoshida, M.3    Kinosita Jr., K.4    Itoh, H.5
  • 290
    • 0028180207 scopus 로고
    • 1-ATPase from a thermophilic eubacterium Thermus thermophilus
    • YOKOYAMA, K., AKABANE, Y., ISHII, N. & YOSHIDA, M. (1994). Isolation of prokaryotic V0V1-ATPase from a thermophilic eubacterium Thermus thermophilus. Journal of Biological Chemistry 269, 12248-12253.
    • (1994) Journal of Biological Chemistry , vol.269 , pp. 12248-12253
    • Yokoyama, K.1    Akabane, Y.2    Ishii, N.3    Yoshida, M.4
  • 293
    • 0035461311 scopus 로고    scopus 로고
    • ATP synthase - A marvellous rotary engine of the cell
    • DOI 10.1038/35089509
    • YOSHIDA, M., MUNEYUKI, E. & HISABORI, T. (2001). ATP synthase- a marvellous rotary engine of the cell. Nature Reviews Molecular and Cellular Biology 2, 669-677. (Pubitemid 33674070)
    • (2001) Nature Reviews Molecular Cell Biology , vol.2 , Issue.9 , pp. 669-677
    • Yoshida, M.1    Muneyuki, E.2    Hisabori, T.3
  • 294
    • 0026612693 scopus 로고
    • 0 domain of the coated vesicle (H+)- ATPase
    • ZHANG, J., MYERS, M. & FORGAC, M. (1992). Characterization of the V0 domain of the coated vesicle (H+)- ATPase. Journal of Biological Chemistry 267, 9773-9778.
    • (1992) Journal of Biological Chemistry , vol.267 , pp. 9773-9778
    • Zhang, J.1    Myers, M.2    Forgac, M.3
  • 295
    • 0001602429 scopus 로고    scopus 로고
    • Characterization of a temperature-sensitive yeast vacuolar ATPase mutant with defects in actin distribution and bud morphology
    • DOI 10.1074/jbc.273.29.18470
    • ZHANG, J. W., PARRA, K. J., LIU, J. & KANE, P. M. (1998). Characterization of a temperature-sensitive yeast vacuolar ATPase mutant with defects in actin distribution and bud morphology. Journal of Biological Chemistry 273, 18470-18480. (Pubitemid 28334775)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.29 , pp. 18470-18480
    • Zhang, J.W.1    Parra, K.J.2    Liu, J.3    Kane, P.M.4
  • 296
    • 0344875467 scopus 로고    scopus 로고
    • 1-ATPase: Affinity purification and structural features by electron microscopy
    • DOI 10.1074/jbc.M309445200
    • ZHANG, Z., CHARSKY, C., KANE, P.M. & WILKENS, S. (2003). Yeast V1-ATPase: affinity purification and structural features by electron microscopy. Journal of Biological Chemistry 278, 47299-47306. (Pubitemid 37452319)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.47 , pp. 47299-47306
    • Zhang, Z.1    Charsky, C.2    Kane, P.M.3    Wilkens, S.4
  • 298
    • 21844466207 scopus 로고    scopus 로고
    • +-ATP synthase
    • DOI 10.1038/sj.emboj.7600682
    • ZIMMERMANN, B., DIEZ, M., ZARRABI, N., GRÄBER, P. & BÖRSCH, M. (2005). Movements of the e-subunit during catalysis and activation in single membrane-bound H+-ATP synthase. EMBO Journal 24, 2053-2063. (Pubitemid 40961790)
    • (2005) EMBO Journal , vol.24 , Issue.12 , pp. 2053-2063
    • Zimmermann, B.1    Diez, M.2    Zarrabi, N.3    Graber, P.4    Borsch, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.