메뉴 건너뛰기




Volumn 167, Issue 2, 2009, Pages 97-105

Ab initio reconstruction of helical samples with heterogeneity, disorder and coexisting symmetries

Author keywords

Dam1 complex; Helical structures; Heterogeneity; Single particle reconstruction

Indexed keywords

FUNGAL PROTEIN; PROTEIN DAM1; UNCLASSIFIED DRUG;

EID: 67649986028     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2009.05.002     Document Type: Article
Times cited : (13)

References (42)
  • 1
    • 0031042321 scopus 로고    scopus 로고
    • The structure of microtubule-motor complexes
    • Amos L.A., and Hirose K. The structure of microtubule-motor complexes. Curr. Biol. 9 (1997) 4-11
    • (1997) Curr. Biol. , vol.9 , pp. 4-11
    • Amos, L.A.1    Hirose, K.2
  • 2
    • 0030266603 scopus 로고    scopus 로고
    • Three-dimensional structures of functional motor proteins on microtubules
    • Arnal I., Metoz F., DeBonis S., and Wade R.H. Three-dimensional structures of functional motor proteins on microtubules. Curr. Biol. 6 (1996) 1265-1270
    • (1996) Curr. Biol. , vol.6 , pp. 1265-1270
    • Arnal, I.1    Metoz, F.2    DeBonis, S.3    Wade, R.H.4
  • 3
    • 33745603981 scopus 로고    scopus 로고
    • The Dam1 kinetochore complex harnesses microtubule dynamics to produce force and movement
    • Asbury C.L., Gestaut D.R., Powers A.F., Franck A.D., and Davis T.N. The Dam1 kinetochore complex harnesses microtubule dynamics to produce force and movement. Proc. Natl. Acad. Sci. USA 103 (2006) 9873-9878
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 9873-9878
    • Asbury, C.L.1    Gestaut, D.R.2    Powers, A.F.3    Franck, A.D.4    Davis, T.N.5
  • 4
    • 0024163316 scopus 로고
    • The reconstruction of helical particles with variable pitch
    • Bluemke D.A., Carragher B., and Josephs R. The reconstruction of helical particles with variable pitch. Ultramicroscopy 26 (1988) 255-270
    • (1988) Ultramicroscopy , vol.26 , pp. 255-270
    • Bluemke, D.A.1    Carragher, B.2    Josephs, R.3
  • 5
    • 2542480756 scopus 로고    scopus 로고
    • The stalk region of dynamin drives the constriction of dynamin tubes
    • Chen Y.-J., Zhang P., Egelman E.H., and Hinshaw J.E. The stalk region of dynamin drives the constriction of dynamin tubes. Nat. Struct. Mol. Biol. 11 (2004) 574-575
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 574-575
    • Chen, Y.-J.1    Zhang, P.2    Egelman, E.H.3    Hinshaw, J.E.4
  • 6
    • 0000668797 scopus 로고
    • Reconstruction of three dimensional structures from electron micrographs
    • DeRoiser D.J., and Klug A. Reconstruction of three dimensional structures from electron micrographs. Nature 217 (1968) 130-134
    • (1968) Nature , vol.217 , pp. 130-134
    • DeRoiser, D.J.1    Klug, A.2
  • 7
    • 0014945329 scopus 로고
    • Reconstruction of 3-dimensional images from electron micrographs of structures with helical symmetry
    • DeRosier D.J., and Moore P.B. Reconstruction of 3-dimensional images from electron micrographs of structures with helical symmetry. J. Mol. Biol. 52 (1970) 355
    • (1970) J. Mol. Biol. , vol.52 , pp. 355
    • DeRosier, D.J.1    Moore, P.B.2
  • 8
    • 0034564239 scopus 로고    scopus 로고
    • A robust algorithm for the reconstruction of helical filaments using single-particle methods
    • Egelman E.H. A robust algorithm for the reconstruction of helical filaments using single-particle methods. Ultramicroscopy 85 (2000) 225-234
    • (2000) Ultramicroscopy , vol.85 , pp. 225-234
    • Egelman, E.H.1
  • 9
    • 33845305513 scopus 로고    scopus 로고
    • The iterative helical real space reconstruction method: surmounting the problems posed by real polymers
    • Egelman E.H. The iterative helical real space reconstruction method: surmounting the problems posed by real polymers. J. Struct. Biol. 157 (2007) 83-94
    • (2007) J. Struct. Biol. , vol.157 , pp. 83-94
    • Egelman, E.H.1
  • 10
    • 0029975088 scopus 로고    scopus 로고
    • SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields
    • Frank J., Radermacher M., Penczek P., Zhu J., Li Y., Ladjadj M., and Leith A. SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields. J. Struct. Biol. 116 (1996) 190-199
    • (1996) J. Struct. Biol. , vol.116 , pp. 190-199
    • Frank, J.1    Radermacher, M.2    Penczek, P.3    Zhu, J.4    Li, Y.5    Ladjadj, M.6    Leith, A.7
  • 12
    • 33646182429 scopus 로고    scopus 로고
    • The CH-domain of calponin does not determine the modes of calponin binding to F-actin
    • Galkin V.E., Orlova A., Fatoum A., Walsh M.P., and Egelman E.H. The CH-domain of calponin does not determine the modes of calponin binding to F-actin. J. Mol. Biol. 359 (2006) 478-485
    • (2006) J. Mol. Biol. , vol.359 , pp. 478-485
    • Galkin, V.E.1    Orlova, A.2    Fatoum, A.3    Walsh, M.P.4    Egelman, E.H.5
  • 13
    • 38649133329 scopus 로고    scopus 로고
    • Coronin-1A stabilizes F-actin by bridging adjacent actin protomers and stapling opposite strands of the actin filament
    • Galkin V.E., Orlova A., Brieher W., Kueh H.Y., Mitchison T.J., and Egelman E.H. Coronin-1A stabilizes F-actin by bridging adjacent actin protomers and stapling opposite strands of the actin filament. J. Mol. Biol. 376 (2008) 607-613
    • (2008) J. Mol. Biol. , vol.376 , pp. 607-613
    • Galkin, V.E.1    Orlova, A.2    Brieher, W.3    Kueh, H.Y.4    Mitchison, T.J.5    Egelman, E.H.6
  • 17
    • 0141843643 scopus 로고    scopus 로고
    • Electron cryo-microscopy shows how strong binding of myosin to actin releases nucleotide
    • Holmes K.C., Angert I., Kull F.J., Jahn W., and Schröder R.R. Electron cryo-microscopy shows how strong binding of myosin to actin releases nucleotide. Nature 425 (2003) 423-427
    • (2003) Nature , vol.425 , pp. 423-427
    • Holmes, K.C.1    Angert, I.2    Kull, F.J.3    Jahn, W.4    Schröder, R.R.5
  • 18
  • 20
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: semiautomated software for high-resolution single-particle reconstructions
    • Ludtke S.J., Baldwin P.R., and Chiu W. EMAN: semiautomated software for high-resolution single-particle reconstructions. J. Struct. Biol. 128 (1999) 82-97
    • (1999) J. Struct. Biol. , vol.128 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 21
    • 34347373760 scopus 로고    scopus 로고
    • Protein arms in the kinetochore-microtubule interface of the yeast DASH complex
    • Miranda J.J.L., King D.S., and Harrison S.C. Protein arms in the kinetochore-microtubule interface of the yeast DASH complex. Mol. Biol. Cell. 18 (2007) 2503-2510
    • (2007) Mol. Biol. Cell. , vol.18 , pp. 2503-2510
    • Miranda, J.J.L.1    King, D.S.2    Harrison, S.C.3
  • 23
    • 0038112088 scopus 로고    scopus 로고
    • Structure and gating mechanism of the acetylcholine receptor pore
    • Miyazawa A., Fujiyoshi Y., and Unwin N. Structure and gating mechanism of the acetylcholine receptor pore. Nature 423 (2003) 949-955
    • (2003) Nature , vol.423 , pp. 949-955
    • Miyazawa, A.1    Fujiyoshi, Y.2    Unwin, N.3
  • 24
    • 34548487953 scopus 로고    scopus 로고
    • Molecular determination by electron microscopy of the dynein-microtubule complex structure
    • Narita A., Mizuno N., Kikkawa M., and Maéda Y. Molecular determination by electron microscopy of the dynein-microtubule complex structure. J. Mol. Biol. 372 (2007) 1320-1336
    • (2007) J. Mol. Biol. , vol.372 , pp. 1320-1336
    • Narita, A.1    Mizuno, N.2    Kikkawa, M.3    Maéda, Y.4
  • 25
    • 0142059303 scopus 로고    scopus 로고
    • Topology representing network enables highly accurate classification of protein images taken by cryo electron-microscope without masking
    • Ogura T., Iwasaki K., and Sato C. Topology representing network enables highly accurate classification of protein images taken by cryo electron-microscope without masking. J. Struct. Biol. 143 (2003) 185-200
    • (2003) J. Struct. Biol. , vol.143 , pp. 185-200
    • Ogura, T.1    Iwasaki, K.2    Sato, C.3
  • 28
    • 33845305824 scopus 로고    scopus 로고
    • Application of the iterative helical real-space reconstruction method to large membranous tubular crystals of P-type ATPases
    • Pomfret A.J., Rice W.J., and Stokes D.L. Application of the iterative helical real-space reconstruction method to large membranous tubular crystals of P-type ATPases. J. Struct. Biol. 157 (2007) 106-116
    • (2007) J. Struct. Biol. , vol.157 , pp. 106-116
    • Pomfret, A.J.1    Rice, W.J.2    Stokes, D.L.3
  • 29
    • 34447649588 scopus 로고    scopus 로고
    • High-resolution electron microscopy of helical specimens: a fresh look at tobacco mosaic virus
    • Sachse C., Chen J., Coureux P.-D., Stroupe M.E., Fändrich M., and Grigorieff N. High-resolution electron microscopy of helical specimens: a fresh look at tobacco mosaic virus. J. Mol. Biol. 371 (2007) 812-835
    • (2007) J. Mol. Biol. , vol.371 , pp. 812-835
    • Sachse, C.1    Chen, J.2    Coureux, P.-D.3    Stroupe, M.E.4    Fändrich, M.5    Grigorieff, N.6
  • 30
    • 0029928871 scopus 로고    scopus 로고
    • SUPRIM: easily modified image processing software
    • Schroeter J.P., and Bretaudiere J.P. SUPRIM: easily modified image processing software. J. Struct. Biol. 116 (1996) 131-137
    • (1996) J. Struct. Biol. , vol.116 , pp. 131-137
    • Schroeter, J.P.1    Bretaudiere, J.P.2
  • 32
    • 13844271970 scopus 로고    scopus 로고
    • Refining the structure of the Halobacterium salinarum flagellar filament using the iterative helical real space reconstruction method: insights into polymorphism
    • Trachtenberg S., Galkin V.E., and Egelman E.H. Refining the structure of the Halobacterium salinarum flagellar filament using the iterative helical real space reconstruction method: insights into polymorphism. J. Mol. Biol. 346 (2005) 665-676
    • (2005) J. Mol. Biol. , vol.346 , pp. 665-676
    • Trachtenberg, S.1    Galkin, V.E.2    Egelman, E.H.3
  • 34
    • 0019728717 scopus 로고
    • Use of multivariate statistics in analysing the images of biological macromolecules
    • van Heel M., and Frank J. Use of multivariate statistics in analysing the images of biological macromolecules. Ultramicroscopy 6 (1981) 187-194
    • (1981) Ultramicroscopy , vol.6 , pp. 187-194
    • van Heel, M.1    Frank, J.2
  • 36
    • 11144231283 scopus 로고    scopus 로고
    • An iterative Fourier-Bessel algorithm for reconstruction of helical structures with severe Bessel overlap
    • Wang H.-W., and Nogales E. An iterative Fourier-Bessel algorithm for reconstruction of helical structures with severe Bessel overlap. J. Struct. Biol. 149 (2005) 65-78
    • (2005) J. Struct. Biol. , vol.149 , pp. 65-78
    • Wang, H.-W.1    Nogales, E.2
  • 38
    • 12344251956 scopus 로고    scopus 로고
    • Formation of a dynamic kinetochore-microtubule interface through assembly of the Dam1 ring complex
    • Westermann S., Avila-Sakar A., and Wang H.W. Formation of a dynamic kinetochore-microtubule interface through assembly of the Dam1 ring complex. Mol. Cell 17 2 (2005) 277-290
    • (2005) Mol. Cell , vol.17 , Issue.2 , pp. 277-290
    • Westermann, S.1    Avila-Sakar, A.2    Wang, H.W.3
  • 39
    • 33644850985 scopus 로고    scopus 로고
    • The Dam1 kinetochore ring complex moves processively on depolymerizing microtubule ends
    • Westermann S., Wang H.-W., Avila-Sakar A., Drubin D.G., Nogales E., and Barnes G. The Dam1 kinetochore ring complex moves processively on depolymerizing microtubule ends. Nature 440 (2006) 565-569
    • (2006) Nature , vol.440 , pp. 565-569
    • Westermann, S.1    Wang, H.-W.2    Avila-Sakar, A.3    Drubin, D.G.4    Nogales, E.5    Barnes, G.6
  • 40
    • 0742272143 scopus 로고    scopus 로고
    • Recognition and separation of single particles with size variation by statistical analysis of their images
    • White H.E., Saibil H.R., Ignatiou A., and Orlova E. Recognition and separation of single particles with size variation by statistical analysis of their images. J. Mol. Biol. 336 (2004) 453-460
    • (2004) J. Mol. Biol. , vol.336 , pp. 453-460
    • White, H.E.1    Saibil, H.R.2    Ignatiou, A.3    Orlova, E.4
  • 41
    • 0042238051 scopus 로고    scopus 로고
    • Complete atomic model of the bacterial flagellar filament by electron cryomicroscopy
    • Yonekura K., Maki-Yonekura S., and Namba K. Complete atomic model of the bacterial flagellar filament by electron cryomicroscopy. Nature 424 (2003) 643-650
    • (2003) Nature , vol.424 , pp. 643-650
    • Yonekura, K.1    Maki-Yonekura, S.2    Namba, K.3
  • 42
    • 0034784987 scopus 로고    scopus 로고
    • Three-dimensional reconstruction of dynamin in the constricted state
    • Zhang P., and Hinshaw J.E. Three-dimensional reconstruction of dynamin in the constricted state. Nat. Cell Biol. 3 (2001) 922-926
    • (2001) Nat. Cell Biol. , vol.3 , pp. 922-926
    • Zhang, P.1    Hinshaw, J.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.