메뉴 건너뛰기




Volumn 7, Issue 9, 2012, Pages

Structure and Flexibility of the C-Ring in the Electromotor of Rotary FoF1-ATPase of Pea Chloroplasts

Author keywords

[No Author keywords available]

Indexed keywords

PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE;

EID: 84866688335     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0043045     Document Type: Article
Times cited : (28)

References (65)
  • 1
    • 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
  • 2
    • 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
  • 3
    • 48249108462 scopus 로고    scopus 로고
    • Unique rotary ATP synthase and its biological diversity
    • von Ballmoos C, Cook GM, Dimroth P, (2008) Unique rotary ATP synthase and its biological diversity. Annu Rev Biophys 37: 43-64.
    • (2008) Annu Rev Biophys , vol.37 , pp. 43-64
    • von Ballmoos, C.1    Cook, G.M.2    Dimroth, P.3
  • 5
    • 66249132322 scopus 로고    scopus 로고
    • Torque generation and elastic power transmission in the rotary F(O)F(1)-ATPase
    • Junge W, Sielaff H, Engelbrecht S, (2009) Torque generation and elastic power transmission in the rotary F(O)F(1)-ATPase. Nature 459: 364-370.
    • (2009) Nature , vol.459 , pp. 364-370
    • Junge, W.1    Sielaff, H.2    Engelbrecht, S.3
  • 7
    • 34547732425 scopus 로고    scopus 로고
    • The oligomeric state of c rings from cyanobacterial F-ATP synthases varies from 13 to 15
    • Pogoryelov D, Reichen C, Klyszejko AL, Brunisholz R, Muller DJ, et al. (2007) The oligomeric state of c rings from cyanobacterial F-ATP synthases varies from 13 to 15. J Bacteriol 189: 5895-5902.
    • (2007) J Bacteriol , vol.189 , pp. 5895-5902
    • Pogoryelov, D.1    Reichen, C.2    Klyszejko, A.L.3    Brunisholz, R.4    Muller, D.J.5
  • 8
    • 64049091511 scopus 로고    scopus 로고
    • Constant c10 ring stoichiometry in the Escherichia coli ATP synthase analyzed by cross-linking
    • Ballhausen B, Altendorf K, Deckers-Hebestreit G, (2009) Constant c10 ring stoichiometry in the Escherichia coli ATP synthase analyzed by cross-linking. J Bacteriol 191: 2400-2404.
    • (2009) J Bacteriol , vol.191 , pp. 2400-2404
    • Ballhausen, B.1    Altendorf, K.2    Deckers-Hebestreit, G.3
  • 9
    • 46049096340 scopus 로고    scopus 로고
    • The stoichiometry of subunit c of Escherichia coli ATP synthase is independent of its rate of synthesis
    • Krebstakies T, Aldag I, Altendorf K, Greie JC, Deckers-Hebestreit G, (2008) The stoichiometry of subunit c of Escherichia coli ATP synthase is independent of its rate of synthesis. Biochemistry 47: 6907-6916.
    • (2008) Biochemistry , vol.47 , pp. 6907-6916
    • Krebstakies, T.1    Aldag, I.2    Altendorf, K.3    Greie, J.C.4    Deckers-Hebestreit, G.5
  • 10
    • 0036496185 scopus 로고    scopus 로고
    • Mechanism of the F(1)F(0)-type ATP synthase, a biological rotary motor
    • Capaldi RA, Aggeler R, (2002) Mechanism of the F(1)F(0)-type ATP synthase, a biological rotary motor. Trends Biochem Sci 27: 154-160.
    • (2002) Trends Biochem Sci , vol.27 , pp. 154-160
    • Capaldi, R.A.1    Aggeler, R.2
  • 11
    • 0034713072 scopus 로고    scopus 로고
    • Structural biology. Proton-powered turbine of a plant motor
    • Seelert H, Poetsch A, Dencher NA, Engel A, Stahlberg H, et al. (2000) Structural biology. Proton-powered turbine of a plant motor. Nature 405: 418-419.
    • (2000) Nature , vol.405 , pp. 418-419
    • Seelert, H.1    Poetsch, A.2    Dencher, N.A.3    Engel, A.4    Stahlberg, H.5
  • 12
    • 67650546998 scopus 로고    scopus 로고
    • Structure of the c14 rotor ring of the proton translocating chloroplast ATP synthase
    • Vollmar M, Schlieper D, Winn M, Buchner C, Groth G, (2009) Structure of the c14 rotor ring of the proton translocating chloroplast ATP synthase. J Biol Chem 284: 18228-18235.
    • (2009) J Biol Chem , vol.284 , pp. 18228-18235
    • Vollmar, M.1    Schlieper, D.2    Winn, M.3    Buchner, C.4    Groth, G.5
  • 13
    • 0030715561 scopus 로고    scopus 로고
    • ATP synthase: an electrochemical transducer with rotatory mechanics
    • Junge W, 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
  • 14
    • 0027970177 scopus 로고
    • A mechanism of proton translocation by F1F0 ATP synthases suggested by double mutants of the a subunit
    • Vik SB, Antonio BJ, (1994) A mechanism of proton translocation by F1F0 ATP synthases suggested by double mutants of the a subunit. J Biol Chem 269: 30364-30369.
    • (1994) J Biol Chem , vol.269 , pp. 30364-30369
    • Vik, S.B.1    Antonio, B.J.2
  • 15
    • 70349216367 scopus 로고    scopus 로고
    • 36 degrees step size of proton-driven c-ring rotation in FoF1-ATP synthase
    • Duser MG, Zarrabi N, Cipriano DJ, Ernst S, Glick GD, et al. (2009) 36 degrees step size of proton-driven c-ring rotation in FoF1-ATP synthase. EMBO J 28: 2689-2696.
    • (2009) EMBO J , vol.28 , pp. 2689-2696
    • Duser, M.G.1    Zarrabi, N.2    Cipriano, D.J.3    Ernst, S.4    Glick, G.D.5
  • 16
    • 78649688361 scopus 로고    scopus 로고
    • Direct observation of stepped proteolipid ring rotation in E. coli FF-ATP synthase
    • Ishmukhametov R, Hornung T, Spetzler D, Frasch WD, (2010) Direct observation of stepped proteolipid ring rotation in E. coli FF-ATP synthase. EMBO J 29: 3911-3923.
    • (2010) EMBO J , vol.29 , pp. 3911-3923
    • Ishmukhametov, R.1    Hornung, T.2    Spetzler, D.3    Frasch, W.D.4
  • 17
    • 79952758006 scopus 로고    scopus 로고
    • Two rotary motors in F-ATP synthase are elastically coupled by a flexible rotor and a stiff stator stalk
    • Wachter A, Bi Y, Dunn SD, Cain BD, Sielaff H, et al. (2011) Two rotary motors in F-ATP synthase are elastically coupled by a flexible rotor and a stiff stator stalk. Proc Natl Acad Sci U S A 108: 3924-3929.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 3924-3929
    • Wachter, A.1    Bi, Y.2    Dunn, S.D.3    Cain, B.D.4    Sielaff, H.5
  • 18
    • 0034859197 scopus 로고    scopus 로고
    • Viscoelastic dynamics of actin filaments coupled to rotary F-ATPase: curvature as an indicator of the torque
    • Cherepanov DA, Junge W, (2001) Viscoelastic dynamics of actin filaments coupled to rotary F-ATPase: curvature as an indicator of the torque. Biophysl J 81: 1234-1244.
    • (2001) Biophysl J , vol.81 , pp. 1234-1244
    • Cherepanov, D.A.1    Junge, W.2
  • 19
    • 0035979760 scopus 로고    scopus 로고
    • Inter-subunit rotation and elastic power transmission in F0F1-ATPase
    • Junge W, Panke O, Cherepanov DA, Gumbiowski K, Muller M, et al. (2001) Inter-subunit rotation and elastic power transmission in F0F1-ATPase. FEBS Lett 504: 152-160.
    • (2001) FEBS Lett , vol.504 , pp. 152-160
    • Junge, W.1    Panke, O.2    Cherepanov, D.A.3    Gumbiowski, K.4    Muller, M.5
  • 20
    • 0034866072 scopus 로고    scopus 로고
    • Viscoelastic dynamics of actin filaments coupled to rotary F-ATPase: angular torque profile of the enzyme
    • Panke O, Cherepanov DA, Gumbiowski K, Engelbrecht S, Junge W, (2001) Viscoelastic dynamics of actin filaments coupled to rotary F-ATPase: angular torque profile of the enzyme. Biophys j 81: 1220-1233.
    • (2001) Biophys J , vol.81 , pp. 1220-1233
    • Panke, O.1    Cherepanov, D.A.2    Gumbiowski, K.3    Engelbrecht, S.4    Junge, W.5
  • 21
    • 56649088286 scopus 로고    scopus 로고
    • Domain compliance and elastic power transmission in rotary F(O)F(1)-ATPase
    • Sielaff H, Rennekamp H, Wachter A, Xie H, Hilbers F, et al. (2008) Domain compliance and elastic power transmission in rotary F(O)F(1)-ATPase. Proc Natl Acad Sci U S A 105: 17760-17765.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 17760-17765
    • Sielaff, H.1    Rennekamp, H.2    Wachter, A.3    Xie, H.4    Hilbers, F.5
  • 22
    • 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
  • 23
    • 17844367330 scopus 로고    scopus 로고
    • Structure of the rotor ring of F-Type Na+-ATPase from Ilyobacter tartaricus
    • Meier T, Polzer P, Diederichs K, Welte W, Dimroth P, (2005) Structure of the rotor ring of F-Type Na+-ATPase from Ilyobacter tartaricus. Science 308: 659-662.
    • (2005) Science , vol.308 , pp. 659-662
    • Meier, T.1    Polzer, P.2    Diederichs, K.3    Welte, W.4    Dimroth, P.5
  • 24
    • 70349828967 scopus 로고    scopus 로고
    • High-resolution structure of the rotor ring of a proton-dependent ATP synthase
    • Pogoryelov D, Yildiz O, Faraldo-Gomez JD, Meier T, (2009) High-resolution structure of the rotor ring of a proton-dependent ATP synthase. Nat Struct Mol Biol 16: 1068-1073.
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 1068-1073
    • Pogoryelov, D.1    Yildiz, O.2    Faraldo-Gomez, J.D.3    Meier, T.4
  • 25
    • 77956869807 scopus 로고    scopus 로고
    • A new type of proton coordination in an F(1)F(o)-ATP synthase rotor ring
    • Preiss L, Yildiz O, Hicks DB, Krulwich TA, Meier T, (2010) A new type of proton coordination in an F(1)F(o)-ATP synthase rotor ring. PLoS Biol 8: e1000443.
    • (2010) PLoS Biol , vol.8
    • Preiss, L.1    Yildiz, O.2    Hicks, D.B.3    Krulwich, T.A.4    Meier, T.5
  • 26
    • 77956552341 scopus 로고    scopus 로고
    • Crystal structure of the Mg. ADP-inhibited state of the yeast F1c10-ATP synthase
    • Dautant A, Velours J, Giraud MF, (2010) Crystal structure of the Mg. ADP-inhibited state of the yeast F1c10-ATP synthase. J Biol Chem 285: 29502-29510.
    • (2010) J Biol Chem , vol.285 , pp. 29502-29510
    • Dautant, A.1    Velours, J.2    Giraud, M.F.3
  • 27
    • 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
  • 28
    • 78649327875 scopus 로고    scopus 로고
    • Microscopic rotary mechanism of ion translocation in the F(o) complex of ATP synthases
    • Pogoryelov D, Krah A, Langer JD, Yildiz O, Faraldo-Gomez JD, et al. (2010) Microscopic rotary mechanism of ion translocation in the F(o) complex of ATP synthases. Nat Chem Biol 6: 891-899.
    • (2010) Nat Chem Biol , vol.6 , pp. 891-899
    • Pogoryelov, D.1    Krah, A.2    Langer, J.D.3    Yildiz, O.4    Faraldo-Gomez, J.D.5
  • 29
    • 70450221664 scopus 로고    scopus 로고
    • On the structure of the proton-binding site in the F(o) rotor of chloroplast ATP synthases
    • Krah A, Pogoryelov D, Meier T, Faraldo-Gomez JD, (2010) On the structure of the proton-binding site in the F(o) rotor of chloroplast ATP synthases. J Mol Biol 395: 20-27.
    • (2010) J Mol Biol , vol.395 , pp. 20-27
    • Krah, A.1    Pogoryelov, D.2    Meier, T.3    Faraldo-Gomez, J.D.4
  • 30
    • 0012633142 scopus 로고
    • Complete Tracking of Proton Flow in Thylakoids - the Unit Conductance of Cf0 Is Greater Than 10 Fs
    • Schoenknecht G, Junge W, Lill H, Engelbrecht S, (1986) Complete Tracking of Proton Flow in Thylakoids - the Unit Conductance of Cf0 Is Greater Than 10 Fs. FEBS Lett 203: 289-294.
    • (1986) FEBS Lett , vol.203 , pp. 289-294
    • Schoenknecht, G.1    Junge, W.2    Lill, H.3    Engelbrecht, S.4
  • 31
    • 2942675081 scopus 로고    scopus 로고
    • The proton-driven rotor of ATP synthase: ohmic conductance (10 fS), and absence of voltage gating
    • Feniouk BA, Kozlova MA, Knorre DA, Cherepanov DA, Mulkidjanian AY, et al. (2004) The proton-driven rotor of ATP synthase: ohmic conductance (10 fS), and absence of voltage gating. Biophys J 86: 4094-4109.
    • (2004) Biophys J , vol.86 , pp. 4094-4109
    • Feniouk, B.A.1    Kozlova, M.A.2    Knorre, D.A.3    Cherepanov, D.A.4    Mulkidjanian, A.Y.5
  • 32
    • 16344382800 scopus 로고    scopus 로고
    • Determination of proton flux and conductance at pH 6.8 through single FO sectors from Escherichia coli
    • Franklin MJ, Brusilow WS, Woodbury DJ, (2004) Determination of proton flux and conductance at pH 6.8 through single FO sectors from Escherichia coli. Biophys J 87: 3594-3599.
    • (2004) Biophys J , vol.87 , pp. 3594-3599
    • Franklin, M.J.1    Brusilow, W.S.2    Woodbury, D.J.3
  • 33
    • 25844431698 scopus 로고    scopus 로고
    • Coarse-grained normal mode analysis in structural biology
    • Bahar I, Rader AJ, (2005) Coarse-grained normal mode analysis in structural biology. Curr Opin Struct Biol 15: 586-592.
    • (2005) Curr Opin Struct Biol , vol.15 , pp. 586-592
    • Bahar, I.1    Rader, A.J.2
  • 35
    • 77949634796 scopus 로고    scopus 로고
    • Normal mode analysis of biomolecular structures: functional mechanisms of membrane proteins
    • Bahar I, Lezon TR, Bakan A, Shrivastava IH, (2010) Normal mode analysis of biomolecular structures: functional mechanisms of membrane proteins. Chem Rev 110: 1463-1497.
    • (2010) Chem Rev , vol.110 , pp. 1463-1497
    • Bahar, I.1    Lezon, T.R.2    Bakan, A.3    Shrivastava, I.H.4
  • 37
    • 0030623823 scopus 로고    scopus 로고
    • Direct evaluation of thermal fluctuations in proteins using a single-parameter harmonic potential
    • Bahar I, Atilgan AR, Erman B, (1997) Direct evaluation of thermal fluctuations in proteins using a single-parameter harmonic potential. Folding & design 2: 173-181.
    • (1997) Folding & Design , vol.2 , pp. 173-181
    • Bahar, I.1    Atilgan, A.R.2    Erman, B.3
  • 38
    • 0035132230 scopus 로고    scopus 로고
    • Anisotropy of fluctuation dynamics of proteins with an elastic network model
    • Atilgan AR, Durell SR, Jernigan RL, Demirel MC, Keskin O, et al. (2001) Anisotropy of fluctuation dynamics of proteins with an elastic network model. Biophys j 80: 505-515.
    • (2001) Biophys J , vol.80 , pp. 505-515
    • Atilgan, A.R.1    Durell, S.R.2    Jernigan, R.L.3    Demirel, M.C.4    Keskin, O.5
  • 39
    • 29144468957 scopus 로고    scopus 로고
    • Solving the structure of plant photosystem I-biochemistry is vital
    • Amunts A, Ben-Shem A, Nelson N, (2005) Solving the structure of plant photosystem I-biochemistry is vital. Photoch Photobiol Sci 4: 1011-1015.
    • (2005) Photoch Photobiol Sci , vol.4 , pp. 1011-1015
    • Amunts, A.1    Ben-Shem, A.2    Nelson, N.3
  • 41
    • 33744459472 scopus 로고    scopus 로고
    • Toward the structural genomics of complexes: crystal structure of a PE/PPE protein complex from Mycobacterium tuberculosis
    • Strong M, Sawaya MR, Wang S, Phillips M, Cascio D, et al. (2006) Toward the structural genomics of complexes: crystal structure of a PE/PPE protein complex from Mycobacterium tuberculosis. Proc Natl Acad Sci U S A 103: 8060-8065.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 8060-8065
    • Strong, M.1    Sawaya, M.R.2    Wang, S.3    Phillips, M.4    Cascio, D.5
  • 42
    • 33846426122 scopus 로고    scopus 로고
    • Solving structures of protein complexes by molecular replacement with Phaser
    • McCoy AJ, (2007) Solving structures of protein complexes by molecular replacement with Phaser. Acta Crystallogr D 63: 32-41.
    • (2007) Acta Crystallogr D , vol.63 , pp. 32-41
    • McCoy, A.J.1
  • 44
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: a comprehensive Python-based system for macromolecular structure solution
    • Adams PD, Afonine PV, Bunkoczi G, Chen VB, Davis IW, et al. (2010) PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr D 66: 213-221.
    • (2010) Acta Crystallogr D , vol.66 , pp. 213-221
    • Adams, P.D.1    Afonine, P.V.2    Bunkoczi, G.3    Chen, V.B.4    Davis, I.W.5
  • 46
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: a new generation of protein database search programs
    • Altschul SF, Madden TL, Schaffer AA, Zhang J, Zhang Z, et al. (1997) Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res 25: 3389-3402.
    • (1997) Nucleic Acids Res , vol.25 , pp. 3389-3402
    • Altschul, S.F.1    Madden, T.L.2    Schaffer, A.A.3    Zhang, J.4    Zhang, Z.5
  • 47
    • 34347388470 scopus 로고    scopus 로고
    • UniRef: comprehensive and non-redundant UniProt reference clusters
    • Suzek BE, Huang H, McGarvey P, Mazumder R, Wu CH, (2007) UniRef: comprehensive and non-redundant UniProt reference clusters. Bioinformatics 23: 1282-1288.
    • (2007) Bioinformatics , vol.23 , pp. 1282-1288
    • Suzek, B.E.1    Huang, H.2    McGarvey, P.3    Mazumder, R.4    Wu, C.H.5
  • 48
    • 13744252890 scopus 로고    scopus 로고
    • MAFFT version 5: improvement in accuracy of multiple sequence alignment
    • Katoh K, Kuma K, Toh H, Miyata T, (2005) MAFFT version 5: improvement in accuracy of multiple sequence alignment. Nucleic Acids Res 33: 511-518.
    • (2005) Nucleic Acids Res , vol.33 , pp. 511-518
    • Katoh, K.1    Kuma, K.2    Toh, H.3    Miyata, T.4
  • 49
    • 77954257799 scopus 로고    scopus 로고
    • ConSurf 2010: calculating evolutionary conservation in sequence and structure of proteins and nucleic acids
    • Ashkenazy H, Erez E, Martz E, Pupko T, Ben-Tal N, (2010) ConSurf 2010: calculating evolutionary conservation in sequence and structure of proteins and nucleic acids. Nucleic Acids Res 38: W529-533.
    • (2010) Nucleic Acids Res , vol.38
    • Ashkenazy, H.1    Erez, E.2    Martz, E.3    Pupko, T.4    Ben-Tal, N.5
  • 50
    • 80054796108 scopus 로고    scopus 로고
    • Using the T-Coffee package to build multiple sequence alignments of protein, RNA, DNA sequences and 3D structures
    • Taly JF, Magis C, Bussotti G, Chang JM, Di Tommaso P, et al. (2011) Using the T-Coffee package to build multiple sequence alignments of protein, RNA, DNA sequences and 3D structures. Nat Protoc 6: 1669-1682.
    • (2011) Nat Protoc , vol.6 , pp. 1669-1682
    • Taly, J.F.1    Magis, C.2    Bussotti, G.3    Chang, J.M.4    Di Tommaso, P.5
  • 51
    • 79951476387 scopus 로고    scopus 로고
    • PROPKA3: Consistent Treatment of Internal and Surface Residues in Empirical pK(a) Predictions
    • Olsson MHM, Sondergaard CR, Rostkowski M, Jensen JH, (2011) PROPKA3: Consistent Treatment of Internal and Surface Residues in Empirical pK(a) Predictions. J Cheml Theory Comput 7: 525-537.
    • (2011) J Cheml Theory Comput , vol.7 , pp. 525-537
    • Olsson, M.H.M.1    Sondergaard, C.R.2    Rostkowski, M.3    Jensen, J.H.4
  • 52
    • 77952721198 scopus 로고    scopus 로고
    • Independent and cooperative motions of the Kv1.2 channel: voltage sensing and gating
    • Yeheskel A, Haliloglu T, Ben-Tal N, (2010) Independent and cooperative motions of the Kv1.2 channel: voltage sensing and gating. Biophys J 98: 2179-2188.
    • (2010) Biophys J , vol.98 , pp. 2179-2188
    • Yeheskel, A.1    Haliloglu, T.2    Ben-Tal, N.3
  • 53
    • 50949126927 scopus 로고    scopus 로고
    • Cooperative transition between open and closed conformations in potassium channels
    • Haliloglu T, Ben-Tal N, (2008) Cooperative transition between open and closed conformations in potassium channels. PLoS Comput Biol 4: e1000164.
    • (2008) PLoS Comput Biol , vol.4
    • Haliloglu, T.1    Ben-Tal, N.2
  • 54
    • 33744926664 scopus 로고    scopus 로고
    • Common mechanism of pore opening shared by five different potassium channels
    • Shrivastava IH, Bahar I, (2006) Common mechanism of pore opening shared by five different potassium channels. Biophys J 90: 3929-3940.
    • (2006) Biophys J , vol.90 , pp. 3929-3940
    • Shrivastava, I.H.1    Bahar, I.2
  • 55
    • 77954629362 scopus 로고    scopus 로고
    • C(alpha)-trace model of the transmembrane domain of human copper transporter 1, motion and functional implications
    • Schushan M, Barkan Y, Haliloglu T, Ben-Tal N, (2010) C(alpha)-trace model of the transmembrane domain of human copper transporter 1, motion and functional implications. Proc Natl Acad Sci U S A 107: 10908-10913.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 10908-10913
    • Schushan, M.1    Barkan, Y.2    Haliloglu, T.3    Ben-Tal, N.4
  • 57
    • 33750407288 scopus 로고    scopus 로고
    • Anisotropic network model: systematic evaluation and a new web interface
    • Eyal E, Yang LW, Bahar I, (2006) Anisotropic network model: systematic evaluation and a new web interface. Bioinformatics 22: 2619-2627.
    • (2006) Bioinformatics , vol.22 , pp. 2619-2627
    • Eyal, E.1    Yang, L.W.2    Bahar, I.3
  • 59
    • 27644566520 scopus 로고    scopus 로고
    • The c15 ring of the Spirulina platensis F-ATP synthase: F1/F0 symmetry mismatch is not obligatory
    • Pogoryelov D, Yu J, Meier T, Vonck J, Dimroth P, et al. (2005) The c15 ring of the Spirulina platensis F-ATP synthase: F1/F0 symmetry mismatch is not obligatory. EMBO Rep 6: 1040-1044.
    • (2005) EMBO Rep , vol.6 , pp. 1040-1044
    • Pogoryelov, D.1    Yu, J.2    Meier, T.3    Vonck, J.4    Dimroth, P.5
  • 60
    • 0037227431 scopus 로고    scopus 로고
    • Evidence for structural integrity in the undecameric c-rings isolated from sodium ATP synthases
    • Meier T, Matthey U, von Ballmoos C, Vonck J, Krug von Nidda T, et al. (2003) Evidence for structural integrity in the undecameric c-rings isolated from sodium ATP synthases. J Mol B 325: 389-397.
    • (2003) J Mol B , vol.325 , pp. 389-397
    • Meier, T.1    Matthey, U.2    von Ballmoos, C.3    Vonck, J.4    Krug von Nidda, T.5
  • 61
    • 35448950945 scopus 로고    scopus 로고
    • Peptide-Lipid Interactions: Free energy determinants of peptide association with lipid bilayers
    • Kessel A, Ben-Tal N, (2002) Peptide-Lipid Interactions: Free energy determinants of peptide association with lipid bilayers. Curr Top Membr 52: 205-253.
    • (2002) Curr Top Membr , vol.52 , pp. 205-253
    • Kessel, A.1    Ben-Tal, N.2
  • 62
    • 70349661903 scopus 로고    scopus 로고
    • Global motions of the nuclear pore complex: insights from elastic network models
    • Lezon TR, Sali A, Bahar I, (2009) Global motions of the nuclear pore complex: insights from elastic network models. PLoS Comput Biol 5: e1000496.
    • (2009) PLoS Comput Biol , vol.5
    • Lezon, T.R.1    Sali, A.2    Bahar, I.3
  • 63
    • 85028099698 scopus 로고    scopus 로고
    • Crystal structure of oxygen-evolving photosystem II at a resolution of 1.9 A
    • Umena Y, Kawakami K, Shen JR, Kamiya N, (2011) Crystal structure of oxygen-evolving photosystem II at a resolution of 1.9 A. Nature. 473: 55-60.
    • (2011) Nature , vol.473 , pp. 55-60
    • Umena, Y.1    Kawakami, K.2    Shen, J.R.3    Kamiya, N.4
  • 64
    • 78649327875 scopus 로고    scopus 로고
    • Microscopic rotary mechanism of ion translocation in the F(o) complex of ATP synthases
    • Pogoryelov D, Krah A, Langer JD, Yildiz O, Faraldo-Gomez JD, et al. (2010) Microscopic rotary mechanism of ion translocation in the F(o) complex of ATP synthases. Nat Chem Biol 6: 891-899.
    • (2010) Nat Chem Biol , vol.6 , pp. 891-899
    • Pogoryelov, D.1    Krah, A.2    Langer, J.D.3    Yildiz, O.4    Faraldo-Gomez, J.D.5
  • 65
    • 84855793968 scopus 로고    scopus 로고
    • Subnanometre-resolution structure of the intact Thermus thermophilus H+-driven ATP synthase
    • Lau WC, Rubinstein JL, (2012) Subnanometre-resolution structure of the intact Thermus thermophilus H+-driven ATP synthase. Nature 481: 214-218.
    • (2012) Nature , vol.481 , pp. 214-218
    • Lau, W.C.1    Rubinstein, J.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.