메뉴 건너뛰기




Volumn 19, Issue 12, 2012, Pages 1356-1362

Structure of the vacuolar-type ATPase from Saccharomyces cerevisiae at 11-Å resolution

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; UNCLASSIFIED DRUG; VACUOLAR TYPE ADENOSINE TRIPHOSPHATASE;

EID: 84870842660     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.2422     Document Type: Article
Times cited : (74)

References (60)
  • 1
    • 38349193176 scopus 로고    scopus 로고
    • The long physiological reach of the yeast vacuolar H+-ATPase
    • Kane, P.M. The long physiological reach of the yeast vacuolar H+-ATPase. J. Bioenerg. Biomembr. 39, 415-421 (2007).
    • (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
    • Forgac, M. Vacuolar ATPases: rotary proton pumps in physiology and pathophysiology. Nat. Rev. Mol. Cell Biol. 8, 917-929 (2007).
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 917-929
    • Forgac, M.1
  • 3
    • 77950378868 scopus 로고    scopus 로고
    • Inhibition of host vacuolar H+-ATPase activity by a Legionella pneumophila effector
    • Xu, L. et al. Inhibition of host vacuolar H+-ATPase activity by a Legionella pneumophila effector. PLoS Pathog. 6, e1000822 (2010).
    • (2010) PLoS Pathog. , vol.6
    • Xu, L.1
  • 4
    • 0024461376 scopus 로고
    • Osteoclastic bone resorption by a polarized vacuolar proton pump
    • Blair, H.C., Teitelbaum, S.L., Ghiselli, R. & Gluck, S. Osteoclastic bone resorption by a polarized vacuolar proton pump. Science 245, 855-857 (1989).
    • (1989) Science , vol.245 , pp. 855-857
    • Blair, H.C.1    Teitelbaum, S.L.2    Ghiselli, R.3    Gluck, S.4
  • 5
    • 4644245032 scopus 로고    scopus 로고
    • Renal vacuolar H+-ATPase
    • Wagner, C.A. et al. Renal vacuolar H+-ATPase. Physiol. Rev. 84, 1263-1314 (2004).
    • (2004) Physiol. Rev. , vol.84 , pp. 1263-1314
    • Wagner, C.A.1
  • 6
    • 67650236818 scopus 로고    scopus 로고
    • Function of a subunit isoforms of the V-ATPase in pH homeostasis and in vitro invasion of MDA-MB231 human breast cancer cells
    • Hinton, A. et al. Function of a subunit isoforms of the V-ATPase in pH homeostasis and in vitro invasion of MDA-MB231 human breast cancer cells. J. Biol. Chem. 284, 16400-16408 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 16400-16408
    • Hinton, A.1
  • 7
    • 58149088485 scopus 로고    scopus 로고
    • Structure of the yeast vacuolar ATPase
    • Zhang, Z. et al. Structure of the yeast vacuolar ATPase. J. Biol. Chem. 283, 35983-35995 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 35983-35995
    • Zhang, Z.1
  • 8
    • 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. 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).
    • (2004) J. Biol. Chem. , vol.279 , pp. 41942-41949
    • Wilkens, S.1    Inoue, T.2    Forgac, M.3
  • 9
    • 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. 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).
    • (2008) Structure , vol.16 , pp. 1789-1798
    • Diepholz, M.1
  • 10
    • 60149087436 scopus 로고    scopus 로고
    • Cryo-electron microscopy of the vacuolar ATPase motor reveals its mechanical and regulatory complexity
    • Muench, S.P. et al. Cryo-electron microscopy of the vacuolar ATPase motor reveals its mechanical and regulatory complexity. J. Mol. Biol. 386, 989-999 (2009).
    • (2009) J. Mol. Biol. , vol.386 , pp. 989-999
    • Muench, S.P.1
  • 11
    • 51349153212 scopus 로고    scopus 로고
    • Cryo-EM structure of the yeast ATP synthase
    • Lau, W.C., Baker, L.A. & Rubinstein, J.L. Cryo-EM structure of the yeast ATP synthase. J. Mol. Biol. 382, 1256-1264 (2008).
    • (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, J.L., Walker, J.E. & Henderson, R. Structure of the mitochondrial ATP synthase by electron cryomicroscopy. EMBO J. 22, 6182-6192 (2003).
    • (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. Stoichiometry and localization of the stator subunits E and G in Thermus thermophilus H+-ATPase/synthase. J. Biol. Chem. 283, 2595-2603 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 2595-2603
    • Esteban, O.1
  • 14
    • 76549094484 scopus 로고    scopus 로고
    • Structure of intact Thermus thermophilus V-ATPase by cryo-EM reveals organization of the membrane-bound V(O) motor
    • Lau, W.C. & Rubinstein, J.L. Structure of intact Thermus thermophilus V-ATPase by cryo-EM reveals organization of the membrane-bound V(O) motor. Proc. Natl. Acad. Sci. USA 107, 1367-1372 (2010).
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 1367-1372
    • Lau, W.C.1    Rubinstein, J.L.2
  • 15
    • 65649105054 scopus 로고    scopus 로고
    • Three-dimensional structure of A1A0 ATP synthase from the hyperthermophilic archaeon Pyrococcus furiosus by electron microscopy
    • Vonck, J., Pisa, K.Y., Morgner, N., Brutschy, B. & Muller, V. Three-dimensional structure of A1A0 ATP synthase from the hyperthermophilic archaeon Pyrococcus furiosus by electron microscopy. J. Biol. Chem. 284, 10110-10119 (2009).
    • (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
  • 16
    • 77949269543 scopus 로고    scopus 로고
    • The structure of the peripheral stalk of Thermus thermophilus H+-ATPase/synthase
    • Lee, L.K., Stewart, A.G., Donohoe, M., Bernal, R.A. & Stock, D. The structure of the peripheral stalk of Thermus thermophilus H+-ATPase/synthase. Nat. Struct. Mol. Biol. 17, 373-378 (2010).
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 373-378
    • Lee, L.K.1    Stewart, A.G.2    Donohoe, M.3    Bernal, R.A.4    Stock, D.5
  • 17
    • 12144279605 scopus 로고    scopus 로고
    • Crystal structure of yeast V-ATPase subunit C reveals its stator function
    • Drory, O., Frolow, F. & Nelson, N. Crystal structure of yeast V-ATPase subunit C reveals its stator function. EMBO Rep. 5, 1148-1152 (2004).
    • (2004) EMBO Rep. , vol.5 , pp. 1148-1152
    • Drory, O.1    Frolow, F.2    Nelson, N.3
  • 18
    • 0035912787 scopus 로고    scopus 로고
    • Crystal structure of the regulatory subunit H of the V-type ATPase of Saccharomyces cerevisiae
    • Sagermann, M., Stevens, T.H. & Matthews, B.W. Crystal structure of the regulatory subunit H of the V-type ATPase of Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 98, 7134-7139 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 7134-7139
    • Sagermann, M.1    Stevens, T.H.2    Matthews, B.W.3
  • 19
    • 70449115562 scopus 로고    scopus 로고
    • Inter-subunit interaction and quaternary rearrangement defined by the central stalk of prokaryotic V1-ATPase
    • Numoto, N., Hasegawa, Y., Takeda, K. & Miki, K. Inter-subunit interaction and quaternary rearrangement defined by the central stalk of prokaryotic V1-ATPase. EMBO Rep. 10, 1228-1234 (2009).
    • (2009) EMBO Rep. , vol.10 , pp. 1228-1234
    • Numoto, N.1    Hasegawa, Y.2    Takeda, K.3    Miki, K.4
  • 20
    • 71249133243 scopus 로고    scopus 로고
    • Crystal structure of A3B3 complex of V-ATPase from Thermus thermophilus
    • Maher, M.J. et al. Crystal structure of A3B3 complex of V-ATPase from Thermus thermophilus. EMBO J. 28, 3771-3779 (2009).
    • (2009) EMBO J. , vol.28 , pp. 3771-3779
    • Maher, M.J.1
  • 21
    • 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. 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).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 59-64
    • Iwata, M.1
  • 22
    • 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, A.G. & Walker, J.E. Structure of the rotor of the V-Type Na+-ATPase from Enterococcus hirae. Science 308, 654-659 (2005).
    • (2005) Science , vol.308 , pp. 654-659
    • Murata, T.1    Yamato, I.2    Kakinuma, Y.3    Leslie, A.G.4    Walker, J.E.5
  • 23
    • 84860388832 scopus 로고    scopus 로고
    • Crystal structure of the cytoplasmic N-terminal domain of subunit I, a homolog of subunit a, of V-ATPase
    • Srinivasan, S., Vyas, N.K., Baker, M.L. & Quiocho, F.A. Crystal structure of the cytoplasmic N-terminal domain of subunit I, a homolog of subunit a, of V-ATPase. J. Mol. Biol. 412, 14-21 (2011).
    • (2011) J. Mol. Biol. , vol.412 , pp. 14-21
    • Srinivasan, S.1    Vyas, N.K.2    Baker, M.L.3    Quiocho, F.A.4
  • 24
    • 0029063512 scopus 로고
    • Disassembly and reassembly of the yeast vacuolar H(+)-ATPase in vivo
    • Kane, P.M. Disassembly and reassembly of the yeast vacuolar H(+)-ATPase in vivo. J. Biol. Chem. 270, 17025-17032 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 17025-17032
    • Kane, P.M.1
  • 25
    • 0028898233 scopus 로고
    • Regulation of plasma membrane V-ATPase activity by dissociation of peripheral subunits
    • Sumner, J.P. et al. Regulation of plasma membrane V-ATPase activity by dissociation of peripheral subunits. J. Biol. Chem. 270, 5649-5653 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 5649-5653
    • Sumner, J.P.1
  • 26
    • 0029812004 scopus 로고    scopus 로고
    • Purification and properties of a cytosolic V1-ATPase
    • Gräf, R., Harvey, W.R. & Wieczorek, H. Purification and properties of a cytosolic V1-ATPase. J. Biol. Chem. 271, 20908-20913 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 20908-20913
    • Gräf, R.1    Harvey, W.R.2    Wieczorek, H.3
  • 27
    • 0026768406 scopus 로고
    • The membrane sector of vacuolar H(+)-ATPase by itself is impermeable to protons
    • Beltrán, C. & Nelson, N. The membrane sector of vacuolar H(+)-ATPase by itself is impermeable to protons. Acta Physiol. Scand. Suppl. 607, 41-47 (1992).
    • (1992) Acta Physiol. Scand. Suppl. , vol.607 , pp. 41-47
    • Beltrán, C.1    Nelson, N.2
  • 28
    • 77958576210 scopus 로고    scopus 로고
    • The C-H peripheral stalk base: A novel component in V1-ATPase assembly
    • Hildenbrand, Z.L., Molugu, S.K., Stock, D. & Bernal, R.A. The C-H peripheral stalk base: a novel component in V1-ATPase assembly. PLoS ONE 5, e12588 (2010).
    • (2010) PLoS ONE , vol.5
    • Hildenbrand, Z.L.1    Molugu, S.K.2    Stock, D.3    Bernal, R.A.4
  • 29
    • 0344875467 scopus 로고    scopus 로고
    • Yeast V1-ATPase: Affinity purification and structural features by electron microscopy
    • Zhang, Z., Charsky, C., Kane, P.M. & Wilkens, S. Yeast V1-ATPase: affinity purification and structural features by electron microscopy. J. Biol. Chem. 278, 47299-47306 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 47299-47306
    • Zhang, Z.1    Charsky, C.2    Kane, P.M.3    Wilkens, S.4
  • 30
    • 0027169669 scopus 로고
    • Partial assembly of the yeast vacuolar H(+)-ATPase in mutants lacking one subunit of the enzyme
    • Doherty, R.D. & Kane, P.M. Partial assembly of the yeast vacuolar H(+)-ATPase in mutants lacking one subunit of the enzyme. J. Biol. Chem. 268, 16845-16851 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 16845-16851
    • Doherty, R.D.1    Kane, P.M.2
  • 31
    • 42649144152 scopus 로고    scopus 로고
    • Angle determination for side views in single particle electron microscopy
    • Baker, L.A. & Rubinstein, J.L. Angle determination for side views in single particle electron microscopy. J. Struct. Biol. 162, 260-270 (2008).
    • (2008) J. Struct. Biol. , vol.162 , pp. 260-270
    • Baker, L.A.1    Rubinstein, J.L.2
  • 32
    • 33845348200 scopus 로고    scopus 로고
    • FREALIGN: High-resolution refinement of single particle structures
    • Grigorieff, N. FREALIGN: high-resolution refinement of single particle structures. J. Struct. Biol. 157, 117-125 (2007).
    • (2007) J. Struct. Biol. , vol.157 , pp. 117-125
    • Grigorieff, N.1
  • 33
    • 0348016127 scopus 로고    scopus 로고
    • An objective criterion for resolution assessment in single-particle electron microscopy (appendix)
    • Rosenthal, P.B., Crowther, R.A. & Henderson, R. An objective criterion for resolution assessment in single-particle electron microscopy (appendix). J. Mol. Biol. 333, 743-745 (2003).
    • (2003) J. Mol. Biol. , vol.333 , pp. 743-745
    • Rosenthal, P.B.1    Crowther, R.A.2    Henderson, R.3
  • 34
    • 33845291163 scopus 로고    scopus 로고
    • Ab initio resolution measurement for single particle structures
    • Sousa, D. & Grigorieff, N. Ab initio resolution measurement for single particle structures. J. Struct. Biol. 157, 201-210 (2007).
    • (2007) J. Struct. Biol. , vol.157 , pp. 201-210
    • Sousa, D.1    Grigorieff, N.2
  • 35
    • 0142042865 scopus 로고    scopus 로고
    • Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy
    • Rosenthal, P.B. & Henderson, R. Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy. J. Mol. Biol. 333, 721-745 (2003).
    • (2003) J. Mol. Biol. , vol.333 , pp. 721-745
    • Rosenthal, P.B.1    Henderson, R.2
  • 36
    • 33744951023 scopus 로고    scopus 로고
    • Vma9p (subunit e) is an integral membrane V0 subunit of the yeast V-ATPase
    • Compton, M.A., Graham, L.A. & Stevens, T.H. Vma9p (subunit e) is an integral membrane V0 subunit of the yeast V-ATPase. J. Biol. Chem. 281, 15312-15319 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 15312-15319
    • Compton, M.A.1    Graham, L.A.2    Stevens, T.H.3
  • 37
    • 84855793968 scopus 로고    scopus 로고
    • Subnanometre-resolution structure of the intact Thermus thermophilus H+-driven ATP synthase
    • Lau, W.C.Y. & Rubinstein, J.L. Subnanometre-resolution structure of the intact Thermus thermophilus H+-driven ATP synthase. Nature 481, 214-218 (2012).
    • (2012) Nature , vol.481 , pp. 214-218
    • Lau, W.C.Y.1    Rubinstein, J.L.2
  • 38
    • 0031008228 scopus 로고    scopus 로고
    • The ATP synthase-A splendid molecular machine
    • Boyer, P.D. The ATP synthase-a splendid molecular machine. Annu. Rev. Biochem. 66, 717-749 (1997).
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 717-749
    • Boyer, P.D.1
  • 39
    • 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. Domain characterization and interaction of the yeast vacuolar ATPase subunit C with the peripheral stator stalk subunits E and G. J. Biol. Chem. 285, 24654-24664 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 24654-24664
    • Oot, R.A.1    Wilkens, S.2
  • 40
    • 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
    • Féthière, J., Venzke, D., Madden, D.R. & Bottcher, B. Peripheral stator of the yeast V-ATPase: stoichiometry and specificity of interaction between the EG complex and subunits C and H. Biochemistry 44, 15906-15914 (2005).
    • (2005) Biochemistry , vol.44 , pp. 15906-15914
    • Féthière, J.1    Venzke, D.2    Madden, D.R.3    Bottcher, B.4
  • 41
  • 42
    • 57649158499 scopus 로고    scopus 로고
    • Functional characterization of the N-terminal domain of subunit H (Vma13p) of the yeast vacuolar ATPase
    • Flannery, A.R. & Stevens, T.H. Functional characterization of the N-terminal domain of subunit H (Vma13p) of the yeast vacuolar ATPase. J. Biol. Chem. 283, 29099-29108 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 29099-29108
    • Flannery, A.R.1    Stevens, T.H.2
  • 43
    • 0034647941 scopus 로고    scopus 로고
    • The H subunit (Vma13p) of the yeast V-ATPase inhibits the ATPase activity of cytosolic V1 complexes
    • Parra, K.J., Keenan, K.L. & Kane, P.M. The H subunit (Vma13p) of the yeast V-ATPase inhibits the ATPase activity of cytosolic V1 complexes. J. Biol. Chem. 275, 21761-21767 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 21761-21767
    • Parra, K.J.1    Keenan, K.L.2    Kane, P.M.3
  • 44
    • 67649405059 scopus 로고    scopus 로고
    • Subunit interactions and requirements for inhibition of the yeast V1-ATPase
    • Diab, H., Ohira, M., Liu, M., Cobb, E. & Kane, P.M. Subunit interactions and requirements for inhibition of the yeast V1-ATPase. J. Biol. Chem. 284, 13316-13325 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 13316-13325
    • Diab, H.1    Ohira, M.2    Liu, M.3    Cobb, E.4    Kane, P.M.5
  • 45
    • 41949126316 scopus 로고    scopus 로고
    • Subunit H of the vacuolar (H+) ATPase inhibits ATP hydrolysis by the free V1 domain by interaction with the rotary subunit F
    • Jefferies, K.C. & Forgac, M. Subunit H of the vacuolar (H+) ATPase inhibits ATP hydrolysis by the free V1 domain by interaction with the rotary subunit F. J. Biol. Chem. 283, 4512-4519 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 4512-4519
    • Jefferies, K.C.1    Forgac, M.2
  • 46
    • 0035807931 scopus 로고    scopus 로고
    • Host-guest study of left-handed polyproline II helix formation
    • Kelly, M.A. et al. Host-guest study of left-handed polyproline II helix formation. Biochemistry 40, 14376-14383 (2001).
    • (2001) Biochemistry , vol.40 , pp. 14376-14383
    • Kelly, M.A.1
  • 47
    • 0031040410 scopus 로고    scopus 로고
    • VMA11 and VMA16 encode second and third proteolipid subunits of the Saccharomyces cerevisiae vacuolar membrane H+-ATPase
    • Hirata, R., Graham, L.A., Takatsuki, A., Stevens, T.H. & Anraku, Y. VMA11 and VMA16 encode second and third proteolipid subunits of the Saccharomyces cerevisiae vacuolar membrane H+-ATPase. J. Biol. Chem. 272, 4795-4803 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 4795-4803
    • Hirata, R.1    Graham, L.A.2    Takatsuki, A.3    Stevens, T.H.4    Anraku, Y.5
  • 48
    • 0023930674 scopus 로고
    • Topography and subunit stoichiometry of the coated vesicle proton pump
    • Arai, H., Terres, G., Pink, S. & Forgac, M. Topography and subunit stoichiometry of the coated vesicle proton pump. J. Biol. Chem. 263, 8796-8802 (1988).
    • (1988) J. Biol. Chem. , vol.263 , pp. 8796-8802
    • Arai, H.1    Terres, G.2    Pink, S.3    Forgac, M.4
  • 49
    • 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. Function and subunit interactions of the N-terminal domain of subunit a (Vph1p) of the yeast V-ATPase. J. Biol. Chem. 283, 19274-19282 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 19274-19282
    • Qi, J.1    Forgac, M.2
  • 50
    • 33645021327 scopus 로고    scopus 로고
    • RF cloning: A restriction-free method for inserting target genes into plasmids
    • van den Ent, F. & Lowe, J. RF cloning: a restriction-free method for inserting target genes into plasmids. J. Biochem. Biophys. Methods 67, 67-74 (2006).
    • (2006) J. Biochem. Biophys. Methods , vol.67 , pp. 67-74
    • Van Den Ent, F.1    Lowe, J.2
  • 51
    • 9644265246 scopus 로고    scopus 로고
    • ATP synthase from Saccharomyces cerevisiae: Location of subunit h in the peripheral stalk region
    • Rubinstein, J.L., Dickson, V.K., Runswick, M.J. & Walker, J.E. ATP synthase from Saccharomyces cerevisiae: location of subunit h in the peripheral stalk region. J. Mol. Biol. 345, 513-520 (2005).
    • (2005) J. Mol. Biol. , vol.345 , pp. 513-520
    • Rubinstein, J.L.1    Dickson, V.K.2    Runswick, M.J.3    Walker, J.E.4
  • 53
    • 0029975088 scopus 로고    scopus 로고
    • SPIDER and WEB: Processing and visualization of images in 3D electron microscopy and related fields
    • Frank, J. et al. SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields. J. Struct. Biol. 116, 190-199 (1996).
    • (1996) J. Struct. Biol. , vol.116 , pp. 190-199
    • Frank, J.1
  • 54
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: Semiautomated software for high-resolution single-particle reconstructions
    • Ludtke, S.J., Baldwin, P.R. & Chiu, W. EMAN: semiautomated software for high-resolution single-particle reconstructions. J. Struct. Biol. 128, 82-97 (1999).
    • (1999) J. Struct. Biol. , vol.128 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 55
    • 79952426683 scopus 로고    scopus 로고
    • SciNet: Lessons learned from building a power-efficient top-20 system and data centre
    • Loken, C. et al. SciNet: Lessons learned from building a power-efficient top-20 system and data centre. J. Phys.: Conf. Ser. 256 (2010).
    • (2010) J. Phys.: Conf. Ser. , vol.256
    • Loken, C.1
  • 56
    • 80052290628 scopus 로고    scopus 로고
    • Edged Watershed Segmentation: A semi-interactive algorithm for segmentation of low-resolution maps from electron cryomicroscopy
    • Baker, L.A. & Rubinstein, J.L. Edged Watershed Segmentation: A semi-interactive algorithm for segmentation of low-resolution maps from electron cryomicroscopy. J. Struct. Biol. 176, 127-132 (2011).
    • (2011) J. Struct. Biol. , vol.176 , pp. 127-132
    • Baker, L.A.1    Rubinstein, J.L.2
  • 57
    • 0036297629 scopus 로고    scopus 로고
    • Multi-resolution contour-based fitting of macromolecular structures
    • Chacón, P. & Wriggers, W. Multi-resolution contour-based fitting of macromolecular structures. J. Mol. Biol. 317, 375-384 (2002).
    • (2002) J. Mol. Biol. , vol.317 , pp. 375-384
    • Chacón, P.1    Wriggers, W.2
  • 58
    • 54949109449 scopus 로고    scopus 로고
    • Biomolecular pleiomorphism probed by spatial interpolation of coarse models
    • Rusu, M., Birmanns, S. & Wriggers, W. Biomolecular pleiomorphism probed by spatial interpolation of coarse models. Bioinformatics 24, 2460-2466 (2008).
    • (2008) Bioinformatics , vol.24 , pp. 2460-2466
    • Rusu, M.1    Birmanns, S.2    Wriggers, W.3
  • 59
    • 33845345287 scopus 로고    scopus 로고
    • Visualizing density maps with UCSF Chimera
    • Goddard, T.D., Huang, C.C. & Ferrin, T.E. Visualizing density maps with UCSF Chimera. J. Struct. Biol. 157, 281-287 (2007).
    • (2007) J. Struct. Biol. , vol.157 , pp. 281-287
    • Goddard, T.D.1    Huang, C.C.2    Ferrin, T.E.3
  • 60
    • 3242875210 scopus 로고    scopus 로고
    • ElNemo: A normal mode web server for protein movement analysis and the generation of templates for molecular replacement
    • Suhre, K. & Sanejouand, Y.H. ElNemo: a normal mode web server for protein movement analysis and the generation of templates for molecular replacement. Nucleic Acids Res. 32, W610-W614 (2004).
    • (2004) Nucleic Acids Res. , vol.32
    • Suhre, K.1    Sanejouand, Y.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.