Crossref journal-article
Springer Science and Business Media LLC
Nature (297)
Bibliography

Woodhead, J. L., Zhao, F.-Q., Craig, R., Egelman, E. H., Alamo, L., & Padrón, R. (2005). Atomic model of a myosin filament in the relaxed state. Nature, 436(7054), 1195–1199.

Authors 6
  1. John L. Woodhead (first)
  2. Fa-Qing Zhao (additional)
  3. Roger Craig (additional)
  4. Edward H. Egelman (additional)
  5. Lorenzo Alamo (additional)
  6. Raúl Padrón (additional)
References 30 Referenced 322
  1. Geeves, M. A. & Holmes, K. C. Structural mechanism of muscle contraction. Annu. Rev. Biochem. 68, 687–728 (1999) (10.1146/annurev.biochem.68.1.687) / Annu. Rev. Biochem. by MA Geeves (1999)
  2. Lehman, W. & Szent-Györgyi, A. G. Regulation of muscular contraction. Distribution of actin control and myosin control in the animal kingdom. J. Gen. Physiol. 66, 1–30 (1975) (10.1085/jgp.66.1.1) / J. Gen. Physiol. by W Lehman (1975)
  3. Wendt, T., Taylor, D., Trybus, K. M. & Taylor, K. Three-dimensional image reconstruction of dephosphorylated smooth muscle heavy meromyosin reveals asymmetry in the interaction between myosin heads and placement of subfragment 2. Proc. Natl Acad. Sci. USA 98, 4361–4366 (2001) (10.1073/pnas.071051098) / Proc. Natl Acad. Sci. USA by T Wendt (2001)
  4. Craig, R. & Padrón, R. in Myology (eds Engel, A. G. & Franzini-Armstrong, C.) 129–166 (McGraw-Hill, New York, 2004) / Myology by R Craig (2004)
  5. Huxley, H. E. & Brown, W. The low-angle x-ray diagram of vertebrate striated muscle and its behaviour during contraction and rigor. J. Mol. Biol. 30, 383–434 (1967) (10.1016/S0022-2836(67)80046-9) / J. Mol. Biol. by HE Huxley (1967)
  6. Wray, J. S., Vibert, P. J. & Cohen, C. Diversity of cross-bridge configurations in invertebrate muscles. Nature 257, 561–564 (1975) (10.1038/257561a0) / Nature by JS Wray (1975)
  7. Crowther, R. A., Padrón, R. & Craig, R. Arrangement of the heads of myosin in relaxed thick filaments from tarantula muscle. J. Mol. Biol. 184, 429–439 (1985) (10.1016/0022-2836(85)90292-X) / J. Mol. Biol. by RA Crowther (1985)
  8. Offer, G., Knight, P. J., Burgess, S. A., Alamo, L. & Padrón, R. A new model for the surface arrangement of myosin molecules in tarantula thick filaments. J. Mol. Biol. 298, 239–260 (2000) (10.1006/jmbi.2000.3664) / J. Mol. Biol. by G Offer (2000)
  9. Stewart, M., Kensler, R. W. & Levine, R. J. Three-dimensional reconstruction of thick filaments from Limulus and scorpion muscle. J. Cell Biol. 101, 402–411 (1985) (10.1083/jcb.101.2.402) / J. Cell Biol. by M Stewart (1985)
  10. Stewart, M. & Kensler, R. W. Arrangement of myosin heads in relaxed thick filaments from frog skeletal muscle. J. Mol. Biol. 192, 831–851 (1986) (10.1016/0022-2836(86)90032-X) / J. Mol. Biol. by M Stewart (1986)
  11. Vibert, P. Helical reconstruction of frozen-hydrated scallop myosin filaments. J. Mol. Biol. 223, 661–671 (1992) (10.1016/0022-2836(92)90982-P) / J. Mol. Biol. by P Vibert (1992)
  12. Eakins, F., AL-Khayat, H. A., Kensler, R. W., Morris, E. P. & Squire, J. M. 3D Structure of fish muscle myosin filaments. J. Struct. Biol. 137, 154–163 (2002) (10.1006/jsbi.2002.4453) / J. Struct. Biol. by F Eakins (2002)
  13. Egelman, E. H. A robust algorithm for the reconstruction of helical filaments using single-particle methods. Ultramicroscopy 85, 225–234 (2000) (10.1016/S0304-3991(00)00062-0) / Ultramicroscopy by EH Egelman (2000)
  14. Wray, J. S. Structure of the backbone in myosin filaments of muscle. Nature 277, 37–40 (1979) (10.1038/277037a0) / Nature by JS Wray (1979)
  15. Liu, J., Wendt, T., Taylor, D. & Taylor, K. Refined model of the 10S conformation of smooth muscle myosin by cryo-electron microscopy 3D image reconstruction. J. Mol. Biol. 329, 963–972 (2003) (10.1016/S0022-2836(03)00516-3) / J. Mol. Biol. by J Liu (2003)
  16. Burgess, S. A., Walker, M. L., White, H. D. & Trinick, J. Flexibility within myosin heads revealed by negative stain and single-particle analysis. J. Cell Biol. 139, 675–681 (1997) (10.1083/jcb.139.3.675) / J. Cell Biol. by SA Burgess (1997)
  17. Suzuki, H., Stafford, W. F. III, Slayter, H. S. & Seidel, J. C. A conformational transition in gizzard heavy meromyosin involving the head-tail junction, resulting in changes in sedimentation coefficient, ATPase activity, and orientation of heads. J. Biol. Chem. 260, 14810–14817 (1985) (10.1016/S0021-9258(17)38644-1) / J. Biol. Chem. by H Suzuki (1985)
  18. Burgess, S. A. et al. Structure of smooth muscle myosin in the switched-off state. Biophys. J. 82, 356a (2002) (10.1016/S0006-3495(02)75539-2) / Biophys. J. by SA Burgess (2002)
  19. Jung, H. et al. Comparative studies of the folded structures of scallop striated and vertebrate smooth muscle myosins. Biophys. J. 86, 403a (2004) / Biophys. J. by H Jung (2004)
  20. Stafford, W. F. et al. Calcium-dependent structural changes in scallop heavy meromyosin. J. Mol. Biol. 307, 137–147 (2001) (10.1006/jmbi.2000.4490) / J. Mol. Biol. by WF Stafford (2001)
  21. Trybus, K. M., Freyzon, Y., Faust, L. Z. & Sweeney, H. L. Spare the rod, spoil the regulation: necessity for a myosin rod. Proc. Natl Acad. Sci. USA 94, 48–52 (1997) (10.1073/pnas.94.1.48) / Proc. Natl Acad. Sci. USA by KM Trybus (1997)
  22. Rovner, A. S. A long, weakly charged actin-binding loop is required for phosphorylation-dependent regulation of smooth muscle myosin. J. Biol. Chem. 273, 27939–27944 (1998) (10.1074/jbc.273.43.27939) / J. Biol. Chem. by AS Rovner (1998)
  23. Trybus, K. M., Naroditskaya, V. & Sweeney, H. L. The light chain-binding domain of the smooth muscle myosin heavy chain is not the only determinant of regulation. J. Biol. Chem. 273, 18423–18428 (1998) (10.1074/jbc.273.29.18423) / J. Biol. Chem. by KM Trybus (1998)
  24. Sellers, J. R. Phosphorylation-dependent regulation of Limulus myosin. J. Biol. Chem. 256, 9274–9278 (1981) (10.1016/S0021-9258(19)52541-8) / J. Biol. Chem. by JR Sellers (1981)
  25. Sellers, J. R. Regulation of cytoplasmic and smooth muscle myosin. Curr. Opin. Cell Biol. 3, 98–104 (1991) (10.1016/0955-0674(91)90171-T) / Curr. Opin. Cell Biol. by JR Sellers (1991)
  26. Craig, R., Padrón, R. & Kendrick-Jones, J. Structural changes accompanying phosphorylation of tarantula muscle myosin filaments. J. Cell Biol. 105, 1319–1327 (1987) (10.1083/jcb.105.3.1319) / J. Cell Biol. by R Craig (1987)
  27. Levine, R. J., Kensler, R. W., Yang, Z., Stull, J. T. & Sweeney, H. L. Myosin light chain phosphorylation affects the structure of rabbit skeletal muscle thick filaments. Biophys. J. 71, 898–907 (1996) (10.1016/S0006-3495(96)79293-7) / Biophys. J. by RJ Levine (1996)
  28. Hidalgo, C., Padrón, R., Horowitz, R., Zhao, F. Q. & Craig, R. Purification of native myosin filaments from muscle. Biophys. J. 81, 2817–2826 (2001) (10.1016/S0006-3495(01)75923-1) / Biophys. J. by C Hidalgo (2001)
  29. 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) (10.1006/jsbi.1996.0030) / J. Struct. Biol. by J Frank (1996)
  30. Pettersen, E. F. et al. UCSF Chimera–a visualization system for exploratory research and analysis. J. Comput. Chem. 25, 1605–1612 (2004) (10.1002/jcc.20084) / J. Comput. Chem. by EF Pettersen (2004)
Dates
Type When
Created 20 years ago (Aug. 24, 2005, 2:48 p.m.)
Deposited 2 years, 3 months ago (May 18, 2023, 1:48 p.m.)
Indexed 3 days, 3 hours ago (Aug. 21, 2025, 2:21 p.m.)
Issued 20 years ago (Aug. 1, 2005)
Published 20 years ago (Aug. 1, 2005)
Published Print 20 years ago (Aug. 1, 2005)
Funders 0

None

@article{Woodhead_2005, title={Atomic model of a myosin filament in the relaxed state}, volume={436}, ISSN={1476-4687}, url={http://dx.doi.org/10.1038/nature03920}, DOI={10.1038/nature03920}, number={7054}, journal={Nature}, publisher={Springer Science and Business Media LLC}, author={Woodhead, John L. and Zhao, Fa-Qing and Craig, Roger and Egelman, Edward H. and Alamo, Lorenzo and Padrón, Raúl}, year={2005}, month=aug, pages={1195–1199} }