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Volumn 107, Issue 4, 2010, Pages 1367-1372

Structure of intact Thermus thermophilus V-ATPase by cryo-EM reveals organization of the membrane-bound VO motor

Author keywords

Membrane protein; Single particle analysis

Indexed keywords

ADENOSINE TRIPHOSPHATASE;

EID: 76549094484     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0911085107     Document Type: Article
Times cited : (64)

References (57)
  • 1
    • 38349193176 scopus 로고    scopus 로고
    • The long physiological reach of the yeast vacuolar H+-ATPase
    • Kane PM (2007) The long physiological reach of the yeast vacuolar H+-ATPase. J Bioenerg Biomembr, 39:415-421.
    • (2007) J Bioenerg Biomembr , vol.39 , pp. 415-421
    • Kane, P.M.1
  • 2
    • 35448946098 scopus 로고    scopus 로고
    • Vacuolar ATPases: Rotary proton pumps in physiology and pathophysiology
    • ForgacM
    • ForgacM(2007) Vacuolar ATPases: Rotary proton pumps in physiology and pathophysiology. Nat Rev Mol Cell Biol, 8:917-929.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 917-929
  • 3
    • 0028114231 scopus 로고
    • Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria
    • Abrahams JP, Leslie AG, Lutter R, Walker JE (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
  • 4
    • 0030934380 scopus 로고    scopus 로고
    • Direct observation of the rotation of F1-ATPase
    • Noji H, Yasuda R, Yoshida M, Kinosita K Jr (1997) Direct observation of the rotation of F1-ATPase. Nature, 386:299-302.
    • (1997) Nature , vol.386 , pp. 299-302
    • Noji, H.1    Yasuda, R.2    Yoshida, M.3    Kinosita Jr, K.4
  • 5
    • 0029893335 scopus 로고    scopus 로고
    • Intersubunit rotation in active F-ATPase
    • Sabbert D, Engelbrecht S, Junge W (1996) Intersubunit rotation in active F-ATPase. Nature, 381:623-625.
    • (1996) Nature , vol.381 , pp. 623-625
    • Sabbert, D.1    Engelbrecht, S.2    Junge, W.3
  • 6
    • 0037418211 scopus 로고    scopus 로고
    • Evidence for rotation of V1-ATPase
    • Imamura H, et al. (2003) Evidence for rotation of V1-ATPase. Proc Natl Acad Sci USA, 100:2312-2315.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 2312-2315
    • Imamura, H.1
  • 7
    • 33646555807 scopus 로고    scopus 로고
    • Rotation, structure, and classification of prokaryotic V-ATPase
    • Yokoyama K, Imamura H (2005) Rotation, structure, and classification of prokaryotic V-ATPase. J Bioenerg Biomembr, 37:405-410.
    • (2005) J Bioenerg Biomembr , vol.37 , pp. 405-410
    • Yokoyama, K.1    Imamura, H.2
  • 8
    • 0029063512 scopus 로고
    • Disassembly and reassembly of the yeast vacuolar H(+)-ATPase in vivo
    • Kane PM (1995) Disassembly and reassembly of the yeast vacuolar H(+)-ATPase in vivo. J Biol Chem, 270:17025-17032.
    • (1995) J Biol Chem , vol.270 , pp. 17025-17032
    • Kane, P.M.1
  • 9
    • 0028898233 scopus 로고
    • Regulation of plasma membrane V-ATPase activity by dissociation of peripheral subunits
    • Sumner JP, et al. (1995) Regulation of plasma membrane V-ATPase activity by dissociation of peripheral subunits. J Biol Chem, 270:5649-5653.
    • (1995) J Biol Chem , vol.270 , pp. 5649-5653
    • Sumner, J.P.1
  • 10
    • 10344240424 scopus 로고    scopus 로고
    • Involvement of the nonhomologous region of subunit A of the yeast V-ATPase in coupling and in vivodissociation
    • Shao E, Forgac M (2004) Involvement of the nonhomologous region of subunit A of the yeast V-ATPase in coupling and in vivodissociation. J Biol Chem, 279:48663-48670.
    • (2004) J Biol Chem , vol.279 , pp. 48663-48670
    • Shao, E.1    Forgac, M.2
  • 11
    • 51349153212 scopus 로고    scopus 로고
    • Cryo-EM structure of the yeast ATP synthase
    • Lau WC, Baker LA, Rubinstein JL (2008) Cryo-EM structure of the yeast ATP synthase. J Mol Biol, 382:1256-1264.
    • (2008) J Mol Biol , vol.382 , pp. 1256-1264
    • Lau, W.C.1    Baker, L.A.2    Rubinstein, J.L.3
  • 12
    • 0347504884 scopus 로고    scopus 로고
    • Structure of the mitochondrial ATP synthase by electron cryomicroscopy
    • Rubinstein JL, Walker JE, Henderson R (2003) Structure of the mitochondrial ATP synthase by electron cryomicroscopy. EMBO J, 22:6182-6192.
    • (2003) EMBO J , vol.22 , pp. 6182-6192
    • Rubinstein, J.L.1    Walker, J.E.2    Henderson, R.3
  • 13
    • 41449111510 scopus 로고    scopus 로고
    • Stoichiometry and localization of the stator subunits E and G in Thermus thermophilus H+-ATPase/synthase
    • Esteban O, et al. (2008) Stoichiometry and localization of the stator subunits E and G in Thermus thermophilus H+-ATPase/synthase. J Biol Chem, 283:2595-2603.
    • (2008) J Biol Chem , vol.283 , pp. 2595-2603
    • Esteban, O.1
  • 14
    • 38049119866 scopus 로고    scopus 로고
    • Dodecamer rotor ring defines H+/ATP ratio for ATP synthesis of prokaryotic V-ATPase from Thermus thermophilus
    • Toei M, et al. (2007) Dodecamer rotor ring defines H+/ATP ratio for ATP synthesis of prokaryotic V-ATPase from Thermus thermophilus. Proc Natl Acad Sci USA, 104:20256-20261.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 20256-20261
    • Toei, M.1
  • 15
    • 0142211194 scopus 로고    scopus 로고
    • Subunit arrangement in V-ATPase from Thermus thermophilus
    • Yokoyama K, et al. (2003) Subunit arrangement in V-ATPase from Thermus thermophilus. J Biol Chem, 278:42686-42691.
    • (2003) J Biol Chem , vol.278 , pp. 42686-42691
    • Yokoyama, K.1
  • 16
    • 4644290116 scopus 로고    scopus 로고
    • Three-dimensional structure of the intact Thermus thermophilus H+-ATPase/synthase by electron microscopy
    • Bernal RA, Stock D (2004) Three-dimensional structure of the intact Thermus thermophilus H+-ATPase/synthase by electron microscopy. Structure, 12:1789-1798.
    • (2004) Structure , vol.12 , pp. 1789-1798
    • Bernal, R.A.1    Stock, D.2
  • 17
    • 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, et al. (2008) 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
  • 18
    • 65649105054 scopus 로고    scopus 로고
    • Three-dimensional structure of A1A0 ATP synthase from the hyperthermophilic archaeon Pyrococcus furiosus by electron microscopy
    • Vonck J, Pisa KY, Morgner N, Brutschy B, Muller V (2009) Three-dimensional structure of A1A0 ATP synthase from the hyperthermophilic archaeon Pyrococcus furiosus by electron microscopy. J Biol Chem, 284:10110-10119.
    • (2009) J Biol Chem , vol.284 , pp. 10110-10119
    • Vonck, J.1    Pisa, K.Y.2    Morgner, N.3    Brutschy, B.4    Muller, V.5
  • 19
    • 4744375526 scopus 로고    scopus 로고
    • Three-dimensional structure of the vacuolar ATPase. Localization of subunit H by difference imaging and chemical cross-linking
    • 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. J Biol Chem, 279:41942-41949.
    • (2004) J Biol Chem , vol.279 , pp. 41942-41949
    • Wilkens, S.1    Inoue, T.2    Forgac, M.3
  • 20
    • 58149088485 scopus 로고    scopus 로고
    • Structure of the yeast vacuolar ATPase
    • Zhang Z, et al. (2008) Structure of the yeast vacuolar ATPase. J Biol Chem, 283:35983-35995.
    • (2008) J Biol Chem , vol.283 , pp. 35983-35995
    • Zhang, Z.1
  • 21
    • 60149087436 scopus 로고    scopus 로고
    • Cryo-electron microscopy of the vacuolar ATPase motor reveals its mechanical and regulatory complexity
    • Muench SP, et al. (2009) Cryo-electron microscopy of the vacuolar ATPase motor reveals its mechanical and regulatory complexity. J Mol Biol, 386:989-999.
    • (2009) J Mol Biol , vol.386 , pp. 989-999
    • Muench, S.P.1
  • 22
    • 71249133243 scopus 로고    scopus 로고
    • Crystal structure of A(3)B(3) complex of V-ATPase from Thermus thermophilus
    • In Press
    • Maher MJ, et al. (2009) Crystal structure of A(3)B(3) complex of V-ATPase from Thermus thermophilus. EMBO J In Press.
    • (2009) EMBO J
    • Maher, M.J.1
  • 23
    • 70449115562 scopus 로고    scopus 로고
    • Inter-subunit interaction and quaternary rearrangement defined by the central stalk of prokaryotic V1-ATPase
    • In Press
    • 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 Rep In Press.
    • (2009) EMBO Rep
    • Numoto, N.1    Hasegawa, Y.2    Takeda, K.3    Miki, K.4
  • 24
    • 9144222170 scopus 로고    scopus 로고
    • Crystal structure of a central stalk subunit C and reversible association/dissociation of vacuole-type ATPase
    • Iwata M, et al. (2004) Crystal structure of a central stalk subunit C and reversible association/dissociation of vacuole-type ATPase. Proc Natl Acad Sci USA, 101:59-64.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 59-64
    • Iwata, M.1
  • 26
    • 17844369968 scopus 로고    scopus 로고
    • Structure of the rotor of the V-Type Na+-ATPase from Enterococcus hirae
    • Murata T, Yamato I, Kakinuma Y, Leslie AG, Walker JE (2005) Structure of the rotor of the V-Type Na+-ATPase from Enterococcus hirae. Science, 308:654-659.
    • (2005) Science , vol.308 , pp. 654-659
    • Murata, T.1    Yamato, I.2    Kakinuma, Y.3    Leslie, A.G.4    Walker, J.E.5
  • 27
    • 12144279605 scopus 로고    scopus 로고
    • Crystal structure of yeast V-ATPase subunit C reveals its stator function
    • Drory O, Frolow F, Nelson N (2004) Crystal structure of yeast V-ATPase subunit C reveals its stator function. EMBO Rep, 5:1148-1152.
    • (2004) EMBO Rep , vol.5 , pp. 1148-1152
    • Drory, O.1    Frolow, F.2    Nelson, N.3
  • 28
    • 0035912787 scopus 로고    scopus 로고
    • Crystal structure of the regulatory subunit H of the V-type ATPase of Saccharomyces cerevisiae
    • Sagermann M, Stevens TH, Matthews BW (2001) Crystal structure of the regulatory subunit H of the V-type ATPase of Saccharomyces cerevisiae. Proc Natl Acad Sci USA, 98:7134-7139.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 7134-7139
    • Sagermann, M.1    Stevens, T.H.2    Matthews, B.W.3
  • 29
    • 0031008228 scopus 로고    scopus 로고
    • The ATP SYNTHASE-A splendid molecular machine
    • Boyer PD (1997) The ATP SYNTHASE-A splendid molecular machine. Annu Rev Biochem, 66:717-749.
    • (1997) Annu Rev Biochem , vol.66 , pp. 717-749
    • Boyer, P.D.1
  • 30
    • 0032544312 scopus 로고    scopus 로고
    • ATP synthesis by rotary catalysis (Nobel Lecture)
    • Walker JE (1998) ATP synthesis by rotary catalysis (Nobel Lecture). Angew Chem, Int Ed, 37:2309-2319.
    • (1998) Angew Chem, Int Ed , vol.37 , pp. 2309-2319
    • Walker, J.E.1
  • 31
    • 17844392351 scopus 로고    scopus 로고
    • Structural biology. Nature's rotary electromotors
    • Junge W, Nelson N (2005) Structural biology. Nature's rotary electromotors. Science, 308:642-644.
    • (2005) Science , vol.308 , pp. 642-644
    • Junge, W.1    Nelson, N.2
  • 32
    • 0030715561 scopus 로고    scopus 로고
    • ATP synthase: An electrochemical transducer with rotatory mechanics
    • JungeW, Lill H, Engelbrecht S (1997) ATP synthase: An electrochemical transducer with rotatory mechanics. Trends Biochem Sci, 22:420-423.
    • (1997) Trends Biochem Sci , vol.22 , pp. 420-423
    • Junge, W.1    Lill, H.2    Engelbrecht, S.3
  • 33
    • 0034607982 scopus 로고    scopus 로고
    • V-Type H+-ATPase/synthase from a thermophilic eubacterium, Thermus thermophilus. Subunit structure and operon
    • Yokoyama K, et al. (2000) V-Type H+-ATPase/synthase from a thermophilic eubacterium, Thermus thermophilus. Subunit structure and operon. J Biol Chem, 275:13955-13961.
    • (2000) J Biol Chem , vol.275 , pp. 13955-13961
    • Yokoyama, K.1
  • 34
    • 0024977998 scopus 로고
    • Proton translocation by the F1F0ATPase of Escherichia coli. Mutagenic analysis of the a subunit
    • Cain BD, Simoni RD (1989) Proton translocation by the F1F0ATPase of Escherichia coli. Mutagenic analysis of the a subunit. J Biol Chem, 264:3292-3300.
    • (1989) J Biol Chem , vol.264 , pp. 3292-3300
    • Cain, B.D.1    Simoni, R.D.2
  • 35
    • 0035940474 scopus 로고    scopus 로고
    • Arg-735 of the 100-kDa subunit a of the yeast V-ATPase is essential for proton translocation
    • Kawasaki-Nishi S, Nishi T, Forgac M (2001) Arg-735 of the 100-kDa subunit a of the yeast V-ATPase is essential for proton translocation. Proc Natl Acad Sci USA, 98:12397-12402.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 12397-12402
    • Kawasaki-Nishi, S.1    Nishi, T.2    Forgac, M.3
  • 36
    • 17844367330 scopus 로고    scopus 로고
    • Meier T, Polzer P, Diederichs K,WelteW, Dimroth P (2005) Structure of the rotor ring of F-Type Na+-ATPase from Ilyobacter tartaricus. Science, 308:659-662.
    • Meier T, Polzer P, Diederichs K,WelteW, Dimroth P (2005) Structure of the rotor ring of F-Type Na+-ATPase from Ilyobacter tartaricus. Science, 308:659-662.
  • 37
    • 42649144152 scopus 로고    scopus 로고
    • Angle determination for side views in single particle electron microscopy
    • Baker LA, Rubinstein JL (2008) Angle determination for side views in single particle electron microscopy. J Struct Biol, 162:260-270.
    • (2008) J Struct Biol , vol.162 , pp. 260-270
    • Baker, L.A.1    Rubinstein, J.L.2
  • 38
    • 33845348200 scopus 로고    scopus 로고
    • FREALIGN: High-resolution refinement of single particle structures
    • Grigorieff N (2007) FREALIGN: High-resolution refinement of single particle structures. J Struct Biol, 157:117-125.
    • (2007) J Struct Biol , vol.157 , pp. 117-125
    • Grigorieff, N.1
  • 39
    • 0348016127 scopus 로고    scopus 로고
    • An objective criterion for resolution assessment in single-particle electron microscopy (appendix)
    • Rosenthal PB, Crowther RA, Henderson R (2003) An objective criterion for resolution assessment in single-particle electron microscopy (appendix). J Mol Biol, 333:743-745.
    • (2003) J Mol Biol , vol.333 , pp. 743-745
    • Rosenthal, P.B.1    Crowther, R.A.2    Henderson, R.3
  • 40
    • 33845291163 scopus 로고    scopus 로고
    • Ab initio resolution measurement for single particle structures
    • Sousa D, Grigorieff N (2007) Ab initio resolution measurement for single particle structures. J Struct Biol, 157:201-210.
    • (2007) J Struct Biol , vol.157 , pp. 201-210
    • Sousa, D.1    Grigorieff, N.2
  • 41
    • 0142042865 scopus 로고    scopus 로고
    • Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy
    • Rosenthal PB, Henderson R (2003) Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy. J Mol Biol, 333:721-745.
    • (2003) J Mol Biol , vol.333 , pp. 721-745
    • Rosenthal, P.B.1    Henderson, R.2
  • 42
    • 0000493852 scopus 로고
    • A physical characterization of some detergents of potential use for membrane protein crystallization
    • Timmins PA, Leonhard M, Weltzien HU, Wacker T, Welte W (1988) A physical characterization of some detergents of potential use for membrane protein crystallization. FEBS Lett, 2:361-368.
    • (1988) FEBS Lett , vol.2 , pp. 361-368
    • Timmins, P.A.1    Leonhard, M.2    Weltzien, H.U.3    Wacker, T.4    Welte, W.5
  • 43
    • 0022202717 scopus 로고
    • An apparent first-order transition between two amorphous phases of ice induced by pressure
    • Mishima O, Calvert LD, Whalley E (1985) An apparent first-order transition between two amorphous phases of ice induced by pressure. Nature, 314:76-78.
    • (1985) Nature , vol.314 , pp. 76-78
    • Mishima, O.1    Calvert, L.D.2    Whalley, E.3
  • 44
    • 33947180023 scopus 로고    scopus 로고
    • Structural analysis of membrane protein complexes by single particle electron microscopy
    • Rubinstein JL (2007) Structural analysis of membrane protein complexes by single particle electron microscopy. Methods, 41:409-416.
    • (2007) Methods , vol.41 , pp. 409-416
    • Rubinstein, J.L.1
  • 45
    • 33750819088 scopus 로고    scopus 로고
    • Yeast mitochondrial ADP/ATP carriers are monomeric in detergents
    • Bamber L, Harding M, Butler PJ, Kunji ER (2006) Yeast mitochondrial ADP/ATP carriers are monomeric in detergents. Proc Natl Acad Sci USA, 103:16224-16229.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 16224-16229
    • Bamber, L.1    Harding, M.2    Butler, P.J.3    Kunji, E.R.4
  • 46
    • 37349107850 scopus 로고    scopus 로고
    • Ribosome binding of a single copy of the SecY complex: Implications for protein translocation
    • Menetret JF, et al. (2007) Ribosome binding of a single copy of the SecY complex: Implications for protein translocation. Mol Cell, 28:1083-1092.
    • (2007) Mol Cell , vol.28 , pp. 1083-1092
    • Menetret, J.F.1
  • 47
    • 33645119556 scopus 로고    scopus 로고
    • The where, when, and how of organelle acidification by the yeast vacuolar H+-ATPase
    • Kane PM (2006) The where, when, and how of organelle acidification by the yeast vacuolar H+-ATPase. Microbiol Mol Biol Rev, 70:177-191.
    • (2006) Microbiol Mol Biol Rev , vol.70 , pp. 177-191
    • Kane, P.M.1
  • 48
    • 0033607504 scopus 로고    scopus 로고
    • Molecular architecture of the rotary motor in ATP synthase
    • Stock D, Leslie AG, Walker JE (1999) Molecular architecture of the rotary motor in ATP synthase. Science, 286:1700-1705.
    • (1999) Science , vol.286 , pp. 1700-1705
    • Stock, D.1    Leslie, A.G.2    Walker, J.E.3
  • 49
    • 0035929328 scopus 로고    scopus 로고
    • The central plug in the reconstituted undecameric c cylinder of a bacterial ATP synthase consists of phospholipids
    • Meier T, Matthey U, Henzen F, Dimroth P, Muller DJ (2001) The central plug in the reconstituted undecameric c cylinder of a bacterial ATP synthase consists of phospholipids. FEBS Lett, 505:353-356.
    • (2001) FEBS Lett , vol.505 , pp. 353-356
    • Meier, T.1    Matthey, U.2    Henzen, F.3    Dimroth, P.4    Muller, D.J.5
  • 50
    • 0032493661 scopus 로고    scopus 로고
    • V-ATPase of Thermus thermophilus is inactivated during ATP hydrolysis but can synthesize ATP
    • Yokoyama K, et al. (1998) V-ATPase of Thermus thermophilus is inactivated during ATP hydrolysis but can synthesize ATP. J Biol Chem, 273:20504-20510.
    • (1998) J Biol Chem , vol.273 , pp. 20504-20510
    • Yokoyama, K.1
  • 51
    • 51049123213 scopus 로고    scopus 로고
    • ATP hydrolysis and synthesis of a rotary motor V-ATPase from Thermus thermophilus
    • Nakano M, et al. (2008) ATP hydrolysis and synthesis of a rotary motor V-ATPase from Thermus thermophilus. J Biol Chem, 283:20789-20796.
    • (2008) J Biol Chem , vol.283 , pp. 20789-20796
    • Nakano, M.1
  • 52
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: Semiautomated software for highresolution single-particle reconstructions
    • Ludtke SJ, Baldwin PR, Chiu W (1999) EMAN: Semiautomated software for highresolution single-particle reconstructions. J Struct Biol, 128:82-97.
    • (1999) J Struct Biol , vol.128 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 53
    • 0033873929 scopus 로고    scopus 로고
    • Comparative protein structure modeling of genes and genomes
    • Marti-Renom MA, et al. (2000) Comparative protein structure modeling of genes and genomes. Ann Rev Biophys Biomol Struct, 29:291-325.
    • (2000) Ann Rev Biophys Biomol Struct , vol.29 , pp. 291-325
    • Marti-Renom, M.A.1
  • 54
    • 33745726716 scopus 로고    scopus 로고
    • A composite score for predicting errors in protein structure models
    • Eramian D, et al. (2006) A composite score for predicting errors in protein structure models. Protein Sci, 15:1653-1666.
    • (2006) Protein Sci , vol.15 , pp. 1653-1666
    • Eramian, D.1
  • 55
    • 0036297629 scopus 로고    scopus 로고
    • Multi-resolution contour-based fitting of macromolecular structures
    • Chacon P, Wriggers W (2002) Multi-resolution contour-based fitting of macromolecular structures. J Mol Biol, 317:375-384.
    • (2002) J Mol Biol , vol.317 , pp. 375-384
    • Chacon, P.1    Wriggers, W.2
  • 56
    • 33845345287 scopus 로고    scopus 로고
    • Visualizing density maps with UCSF Chimera
    • Goddard TD, Huang CC, Ferrin TE (2007) Visualizing density maps with UCSF Chimera. J Struct Biol, 157:281-287.
    • (2007) J Struct Biol , vol.157 , pp. 281-287
    • Goddard, T.D.1    Huang, C.C.2    Ferrin, T.E.3
  • 57
    • 0033581879 scopus 로고    scopus 로고
    • Structural changes linked to proton translocation by subunit C of the ATP synthase
    • Rastogi VK, Girvin ME (1999) Structural changes linked to proton translocation by subunit C of the ATP synthase. Nature, 402:263-268.
    • (1999) Nature , vol.402 , pp. 263-268
    • Rastogi, V.K.1    Girvin, M.E.2


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