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Volumn 133, Issue 2-3, 2001, Pages 203-213

Classification and reconstruction of a heterogeneous set of electron microscopic images: A case study of GroEL-substrate complexes

Author keywords

Chaperonin; Electron microscopy; GroEL; Image reconstruction

Indexed keywords

CHAPERONIN GLUTAMATE AMMONIA LIGASE COMPLEX; PROTEIN DERIVATIVE; UNCLASSIFIED DRUG;

EID: 0035783260     PISSN: 10478477     EISSN: None     Source Type: Journal    
DOI: 10.1006/jsbi.2001.4354     Document Type: Conference Paper
Times cited : (10)

References (20)
  • 1
    • 0029665272 scopus 로고    scopus 로고
    • A model-based approach for determining orientation of biological macromolecules imaged by cryoelectron microscopy
    • Baker, T. S., and Cheng, R. H. (1996) A model-based approach for determining orientation of biological macromolecules imaged by cryoelectron microscopy, J. Struct. Biol. 116, 120-130.
    • (1996) J. Struct. Biol. , vol.116 , pp. 120-130
    • Baker, T.S.1    Cheng, R.H.2
  • 3
    • 0033598941 scopus 로고    scopus 로고
    • The crystal structure of a GroEL/peptide complex: Plasticity as a basis for substrate diversity
    • Chen, L., and Sigler, P. B. (1999) The crystal structure of a GroEL/peptide complex: Plasticity as a basis for substrate diversity, Cell 99, 757-768.
    • (1999) Cell , vol.99 , pp. 757-768
    • Chen, L.1    Sigler, P.B.2
  • 4
    • 0028027055 scopus 로고
    • Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy
    • Chen, S., Roseman, A. M., Hunter, A. S., Wood, S. P., Burston, S. G., Ranson, N. A., Clarke, A. R., and Saibil, H. R. (1994) Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy, Nature 371, 261-264.
    • (1994) Nature , vol.371 , pp. 261-264
    • Chen, S.1    Roseman, A.M.2    Hunter, A.S.3    Wood, S.P.4    Burston, S.G.5    Ranson, N.A.6    Clarke, A.R.7    Saibil, H.R.8
  • 5
    • 0034972451 scopus 로고    scopus 로고
    • Structural changes in GroEL effected by binding a denatured protein substrate
    • in press
    • Falke, S., Fisher, M. T., and Gogol, E. P. (2001) Structural changes in GroEL effected by binding a denatured protein substrate, J. Mol. Biol., in press.
    • (2001) J. Mol. Biol.
    • Falke, S.1    Fisher, M.T.2    Gogol, E.P.3
  • 6
    • 0026741821 scopus 로고
    • Promotion of the in vitro renaturation of dodecameric glutamine synthetase from Escherichia coli in the presence of GroEL (Chaperonin-60) and ATP
    • Fisher, M. T. (1992) Promotion of the in vitro renaturation of dodecameric glutamine synthetase from Escherichia coli in the presence of GroEL (Chaperonin-60) and ATP, Biochemistry 31, 3955-3963.
    • (1992) Biochemistry , vol.31 , pp. 3955-3963
    • Fisher, M.T.1
  • 7
    • 0028242347 scopus 로고
    • On the assembly of dodecameric glutamine synthetase from stable chaperonin complexes
    • Fisher, M. T. (1993) On the assembly of dodecameric glutamine synthetase from stable chaperonin complexes, J. Biol. Chem. 269, 13629-13636.
    • (1993) J. Biol. Chem. , vol.269 , pp. 13629-13636
    • Fisher, M.T.1
  • 8
    • 0029975088 scopus 로고    scopus 로고
    • SPIDER and WEB: Processing and visualization of images in 3D electron microsocpy and other fields
    • Frank, J., Radermacher, M., Penczek, P., Zhu, J., Li, Y., Ladjadj, M., and Leith, A. (1996) SPIDER and WEB: Processing and visualization of images in 3D electron microsocpy and other fields, J. Struct. Biol. 116, 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
  • 9
    • 0020920066 scopus 로고
    • Direct three-dimensional reconstruction for macromolecular complexes from electron micrographs
    • Harauz, G., and Ottensmeyer, F. P. (1984) Direct three-dimensional reconstruction for macromolecular complexes from electron micrographs, Ultramicroscopy 12, 309-320.
    • (1984) Ultramicroscopy , vol.12 , pp. 309-320
    • Harauz, G.1    Ottensmeyer, F.P.2
  • 10
    • 0027092285 scopus 로고
    • Chaperonin-mediated protein folding: GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavity
    • Langer, T., Pfeifer, G., Martin, J., Baumeister, W., and Hartl, F. (1992) Chaperonin-mediated protein folding: GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavity, EMBO J. 11, 4757-4765.
    • (1992) EMBO J. , vol.11 , pp. 4757-4765
    • Langer, T.1    Pfeifer, G.2    Martin, J.3    Baumeister, W.4    Hartl, F.5
  • 11
    • 0030902005 scopus 로고    scopus 로고
    • Symmetric GroEL-GroES complexes can contain substrate simultaneously in both GroEL rings
    • Llorca, O., Marco, S., Carrascso, J., and Valpuesta, J. M. (1997) Symmetric GroEL-GroES complexes can contain substrate simultaneously in both GroEL rings, FEBS Lett. 405, 195-199.
    • (1997) FEBS Lett. , vol.405 , pp. 195-199
    • Llorca, O.1    Marco, S.2    Carrascso, J.3    Valpuesta, J.M.4
  • 12
    • 0028393194 scopus 로고
    • The ribosome at improved resolution: New techniques for merging and orientation refinement in 3D cryoelectron microscopy of biological particles
    • Penczek, P., Grassucci, R. A., and Frank, J. (1994) The ribosome at improved resolution: New techniques for merging and orientation refinement in 3D cryoelectron microscopy of biological particles, Ultramicroscopy 53, 251-270.
    • (1994) Ultramicroscopy , vol.53 , pp. 251-270
    • Penczek, P.1    Grassucci, R.A.2    Frank, J.3
  • 13
    • 0026521233 scopus 로고
    • Three-dimensional reconstruction of single particles embedded in ice
    • Penczek, P., Radermacher, M., and Frank, J. (1992) Three-dimensional reconstruction of single particles embedded in ice, Ultramicroscopy 40, 33-53.
    • (1992) Ultramicroscopy , vol.40 , pp. 33-53
    • Penczek, P.1    Radermacher, M.2    Frank, J.3
  • 14
    • 0030198739 scopus 로고    scopus 로고
    • A common-lines based method for determining orientations for N > 3 particle projections simultaneously
    • Penczek, P. A., Zhu, J., and Frank, J. (1996) A common-lines based method for determining orientations for N > 3 particle projections simultaneously, Ultramicroscopy 63, 205-218.
    • (1996) Ultramicroscopy , vol.63 , pp. 205-218
    • Penczek, P.A.1    Zhu, J.2    Frank, J.3
  • 15
    • 0030592538 scopus 로고    scopus 로고
    • The chaperonin ATPase cycle: Mechanism of allosteric switching and movements of substrate-binding domains in GroEL
    • Roseman, A. M., Chen, S., White, H., Braig, K., and Saibil, H. R. (1996) The chaperonin ATPase cycle: Mechanism of allosteric switching and movements of substrate-binding domains in GroEL, Cell 87, 241-251.
    • (1996) Cell , vol.87 , pp. 241-251
    • Roseman, A.M.1    Chen, S.2    White, H.3    Braig, K.4    Saibil, H.R.5
  • 18
    • 0000457986 scopus 로고
    • Three-dimensional reconstruction with unknown angular relationships
    • Electron Microscopy Foundation, Budapest
    • van Heel, M. (1984) Three-dimensional reconstruction with unknown angular relationships. In Proceedings of the 8th European Congress on Electron Microscopy, pp. 1347-1348, Electron Microscopy Foundation, Budapest.
    • (1984) Proceedings of the 8th European Congress on Electron Microscopy , pp. 1347-1348
    • Van Heel, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.