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Journal of Muscle Research and Cell Motility (297)
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Young Frado, L.-L., & Craig, R. (1992). Structural changes induced in scallop heavy meromyosin molecules by Ca2+ and ATP. Journal of Muscle Research and Cell Motility, 13(4), 436–446.

Authors 2
  1. Ling-Ling Young Frado (first)
  2. Roger Craig (additional)
References 55 Referenced 13
  1. Adelstein, R. S. &Eisenberg, E. (1980) Regulation and kinetics of the actin-myosin-ATP interaction.Ann. Rev. Biochem. 49, 921–56. (10.1146/annurev.bi.49.070180.004421) / Ann. Rev. Biochem. by R. S. Adelstein (1980)
  2. Ankrett, R. J., Rowe, A. J., Cross, R. A., Kendrick-Jones, J. &Bagshaw, C. R. (1991) A folded (1OS) conformer of myosin from a striated muscle and its implications for regulation of ATPase activity.J. Mol. Biol. 217, 323–35. (10.1016/0022-2836(91)90546-I) / J. Mol. Biol. by R. J. Ankrett (1991)
  3. Bennett, A. J., Patel, N., Wells, C. &Bagshaw, C. R. (1984) 8-analino-1-naphthalenesulphonate, a fluorescent probe for the regulatory light chain binding site of scallop myosin.J. Muscle Res. Cell Motil. 5, 165–82. (10.1007/BF00712154) / J. Muscle Res. Cell Motil. by A. J. Bennett (1984)
  4. Castellani, L., Eliott, Jr, B. W., Winkelmann, D. A., Vibert, P. &Cohen, C. (1987) Myosin binding to actin; structural analysis using myosin fragments.J. Mol. Biol. 196, 955–60. (10.1016/0022-2836(87)90420-7) / J. Mol. Biol. by L. Castellani (1987)
  5. Chantler, P. D. &Szent-Györgyi, A. G. (1978) Spectroscopic studies on invertebrate myosins and light chains.Biochemistry 17, 5440–8. (10.1021/bi00618a018) / Biochemistry by P. D. Chantler (1978)
  6. Collins, J. H., Jakes, R., Kendrick-Jones, J., Leszyk, J., Barouch, W., Theibert, J. L., Spiegel, J. &Szent-Györgyi, A. (1986) Amino acid sequence of myosin essential light chain from the scallop Aequipecten irradians.Biochemistry 25, 7651–6. (10.1021/bi00371a056) / Biochemistry by J. H. Collins (1986)
  7. Craig, R., Szent-Györgyi, A. G., Beese, L., Flicker, P., Vibert, P. &Cohen, C. (1980) Electron microscopy of thin filaments decorated with a Ca2+-regulated myosin.J. Mol. Biol. 140, 35–55. (10.1016/0022-2836(80)90355-1) / J. Mol. Biol. by R. Craig (1980)
  8. Craig, R., Smith, R. &Kendrick-Jones, J. (1983) Light chain phosphorylation controls the conformation of vertebrate non-muscle and smooth muscle myosin molecules.Nature (Lond.)302, 436–9. (10.1038/302436a0) / Nature (Lond.) by R. Craig (1983)
  9. Craig, R., Padrón, R. &Kendrick-Jones, J. (1987) Structural changes accompanying phosphorylation of tarantula muscle myosin filaments.J. Cell Biol. 105, 1319–27. (10.1083/jcb.105.3.1319) / J. Cell Biol. by R. Craig (1987)
  10. Elliott, A. &Offer, G. (1978) Shape and flexibility of the myosin molecule.J. Mol. Biol. 123, 505–19. (10.1016/0022-2836(78)90204-8) / J. Mol. Biol. by A. Elliott (1978)
  11. Flicker, P. F., Wallimann, T. &Vibert, P. (1983) Electron microscopy of scallop myosin: location of regulatory light chains.J. Mol. Biol. 169, 723–41. (10.1016/S0022-2836(83)80167-3) / J. Mol. Biol. by P. F. Flicker (1983)
  12. Frado, L.-L. Y. &Craig, R. (1988) Structural changes induced in scallop HMM by Ca2+ and ATP.Biophys. J. 53, 177a. / Biophys. J. by L.-L. Y. Frado (1988)
  13. Frado, L.-L. Y. &Craig, R. (1989) Structural changes induced in Ca2+-regulated myosin filaments by Ca2+ and ATP.J. Cell Biol. 109, 529–38. (10.1083/jcb.109.2.529) / J. Cell Biol. by L.-L. Y. Frado (1989)
  14. Hardwicke, P. M. D., Wallimann, T. &Szent-Györgyi, A. G. (1983) Light-chain movement and regulation in scallop myosin.Nature (Lond.) 301, 478–82. (10.1038/301478a0) / Nature (Lond.) by P. M. D. Hardwicke (1983)
  15. Hardwicke, P. M. D. &Szent-Györgyi, A. G. (1985) Proximity of regulatory light chains in scallop myosin.J. Mol. Biol. 183, 203–11. (10.1016/0022-2836(85)90213-X) / J. Mol. Biol. by P. M. D. Hardwicke (1985)
  16. Highashihara, M., Frado, L.-L. Y., Craig, R. &Ikebe, M. (1989) Inhibition of conformational change in smooth muscle myosin by a monoclonal antibody against the 17-kDa light chain.J. Biol. Chem. 264, 5218–25. (10.1016/S0021-9258(18)83721-8) / J. Biol. Chem. by M. Highashihara (1989)
  17. Ikebe, M. &Ogihara, S. (1982) Phosphorylation-dependent and ATP-induced changes in structural array in gizzard myosin filament bundles.J. Biochem. (Tokyo) 92, 1973–7. (10.1093/oxfordjournals.jbchem.a134128) / J. Biochem. (Tokyo) by M. Ikebe (1982)
  18. Ikebe, M. &Hartshorne, D. J. (1984) Conformation-dependent proteolysis of smooth-muscle myosin.J. Biol. Chem. 259, 11639–42. (10.1016/S0021-9258(20)71251-2) / J. Biol. Chem. by M. Ikebe (1984)
  19. Ikebe, M., Hinkins, S. &Hartshorne, D. J. (1983) Correlation of enzymatic properties and conformation of smooth muscle myosin.Biochemistry 22, 4580–7. (10.1021/bi00288a036) / Biochemistry by M. Ikebe (1983)
  20. Jackson, A. P., Warriner, K. E., Wells, C. &Bagshaw, C. R. (1986) The actin-activated ATPase of regulated and unregulated scallop heavy meromyosin.FEBS Lett. 197, 154–8. (10.1016/0014-5793(86)80317-9) / FEBS Lett. by A. P. Jackson (1986)
  21. Kendrick-Jones, J. &Scholey, J. M. (1981) Myosin-linked regulatory systems.J. Muscle Res. Cell Motil. 2347–72. (10.1007/BF00711965) / J. Muscle Res. Cell Motil. by J. Kendrick-Jones (1981)
  22. Kendrick-Jones, J., Lehman, W. &Szent-GYörgyi, A. G. (1970) Regulation in molluscan muscles.J. Mol. Biol. 54, 313–26. (10.1016/0022-2836(70)90432-8) / J. Mol. Biol. by J. Kendrick-Jones (1970)
  23. Kendrick-Jones, J., Jakes, R., Tooth, P., Craig, R. &Scholey, J. (1982) Role of the myosin light chain in the regulation of contractile activity. InBasic Biology of Muscles: A Comparative Approach (edited by Twarog, B. M., Levine, R. J. C. & Dewey, M. M.) pp. 255–72. New York: Raven Press. / Basic Biology of Muscles: A Comparative Approach by J. Kendrick-Jones (1982)
  24. Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4.Nature (London) 227, 680–5. (10.1038/227680a0) / Nature (London) by U. K. Laemmli (1970)
  25. Laurent, T. C. &Killander, J. (1964) A theory of gel filtration and its experimental verification.J. Chromatog. 14, 317–30. (10.1016/S0021-9673(00)86637-6) / J. Chromatog. by T. C. Laurent (1964)
  26. Lehman, W. &Szent-Györgyi, A. G. (1975) Regulation of muscular contraction. Distribution of actin control and myosin control in the animal kingdom.J. Gen. Physiol. 66, 1–30. (10.1085/jgp.66.1.1) / J. Gen. Physiol. by W. Lehman (1975)
  27. Lowey, S., Slayter, H. S., Weeds, A. G. &Baker, H. (1969) Substructure of the myosin molecule. I. Subfragments of myosin by enzymic degradation.J. Mol. Biol. 42, 1–29. (10.1016/0022-2836(69)90483-5) / J. Mol. Biol. by S. Lowey (1969)
  28. Margossian, S. S. &Lowey, S. (1982) Preparation of myosin and its subfragments from rabbit skeletal muscle.Methods Enzymol. 85, 55–71. (10.1016/0076-6879(82)85009-X) / Methods Enzymol. by S. S. Margossian (1982)
  29. Matsudaira, P. T. &Burgess, D. R. (1978) SDS microslab linear gradient polyacrylamide gel electrophoresis.Anal. Biochem. 87, 386–96. (10.1016/0003-2697(78)90688-7) / Anal. Biochem. by P. T. Matsudaira (1978)
  30. Onishi, H. &Watanabe, S. (1984) Correlation between the papain digestibility and the conformation of 10S-myosin from chicken gizzard.J. Biochem. (Tokyo) 95, 899–902. (10.1093/oxfordjournals.jbchem.a134685) / J. Biochem. (Tokyo) by H. Onishi (1984)
  31. Schacterle, G. R. &Pollack, R. L. (1973) A simplified method for the quantitative assay of small amounts of protein in biological material.Anal. Biochem. 51, 654–5. (10.1016/0003-2697(73)90523-X) / Anal. Biochem. by G. R. Schacterle (1973)
  32. Sellers, J. R. (1981) Phosphorylation-dependent regulation of Limulus myosin.J. Biol. Chem. 256, 9274–8. (10.1016/S0021-9258(19)52541-8) / J. Biol. Chem. by J. R. Sellers (1981)
  33. Sherry, J. M. F., Gorecka, A., Aksoy, M. O., Dabrowska, A. R. &Hartshorne, D. J. (1978) Roles of calcium and phosphorylation in the regulation of the activity of gizzard myosin.Biochemistry 17, 4411–18. (10.1021/bi00614a009) / Biochemistry by J. M. F. Sherry (1978)
  34. Shpetner, H. (1985) Structural and regulatory properties of scallop heavy meromyosin. PhD Thesis, Brandeis University.
  35. Sobieszek, A. (1977) Vertebrate smooth muscle myosin enzymatic and structural properties. InThe Biochemistry of Smooth Muscle (edited by Stephens, N. L.) pp. 413–43. Baltimore-London-Tokyo: University Park Press. / The Biochemistry of Smooth Muscle by A. Sobieszek (1977)
  36. Spudich, J. A. &Watt, S. (1971) The regulation of rabbit skeletal muscle contraction.J. Biol. Chem. 246, 4866–71. (10.1016/S0021-9258(18)62016-2) / J. Biol. Chem. by J. A. Spudich (1971)
  37. Stafford, W. F., III, Szentkiralyi, E. M. &Szent-GYörgyi, A. G. (1979) Regulatory properties of single-headed fragments of scallop myosin.Biochemistry 18, 5273–80. (10.1021/bi00591a002) / Biochemistry by W. F. Stafford III (1979)
  38. Suzuki, H., Stafford, W. F., III, Slayter, H. S. &Seidel, J. C. (1985) 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, 14 810–17. (10.1016/S0021-9258(17)38644-1) / J. Biol. Chem. by H. Suzuki (1985)
  39. Suzuki, H., Kondo, Y., Carlos, A. D. &Seidel, J. C. (1988) Effects of phosphorylation, MgATP, and ionic strength on the rates of papain degradation of heavy and light chains of smooth muscle heavy meromyosin at the S1-S2 junction.Biol. Chem. 263, 10 974–9. (10.1016/S0021-9258(18)38065-7) / Biol. Chem. by H. Suzuki (1988)
  40. Szent-Györgyi, A. G., Szentkiralyi, E. M. &Kendrick-Jones, J. (1973) The light chains of scallop myosin as regulatory subunits.J. Mol. Biol. 74, 179–203. (10.1016/0022-2836(73)90106-X) / J. Mol. Biol. by A. G. Szent-Györgyi (1973)
  41. Szentkiralyi, E. M. (1984) Tryptic digestion of scallop S1: evidence for a complex between the two light chains and a heavy chain peptide.J. Muscle Res. Cell Motil. 5, 147–64. (10.1007/BF00712153) / J. Muscle Res. Cell Motil. by E. M. Szentkiralyi (1984)
  42. Trybus, K. M. &Lowey, S. (1984) Conformational states of smooth muscle myosin.J. Biol. Chem. 259, 8564–71. (10.1016/S0021-9258(17)39767-3) / J. Biol. Chem. by K. M. Trybus (1984)
  43. Trybus, K. M., Huiatt, T. W. &Lowey, S. (1982) A bent monomeric conformation of myosin from smooth muscle.Proc. Natl. Acad. Sci. USA 79, 6151–5. (10.1073/pnas.79.20.6151) / Proc. Natl. Acad. Sci. USA by K. M. Trybus (1982)
  44. Tyler, J. M. &Branton, D. (1980) Rotary shadowing of extended molecules dried from glycerol.J. Ultrastruct. Res. 71, 95–102. (10.1016/S0022-5320(80)90098-2) / J. Ultrastruct. Res. by J. M. Tyler (1980)
  45. Vibert, P. &Craig, R. (1983) Electron microscopy and image analysis of myosin filaments from scallop striated muscle.J. Mol. Biol. 165, 303–20. (10.1016/S0022-2836(83)80259-9) / J. Mol. Biol. by P. Vibert (1983)
  46. Vibert, P. &Craig, R. (1985) Structural changes that occur in scallop myosin filaments upon activation.J. Cell Biol. 101, 830–7. (10.1083/jcb.101.3.830) / J. Cell Biol. by P. Vibert (1985)
  47. Vibert, P. &Cohen, C. (1988) Domains, motions and regulation in the myosin head.J. Muscle Res. Cell Motil. 9, 296–305. (10.1007/BF01773873) / J. Muscle Res. Cell Motil. by P. Vibert (1988)
  48. Vibert, P. &Castellani, L. (1989) Substructure and accessory proteins in scallop myosin filaments.J. Cell Biol. 109, 539–47. (10.1083/jcb.109.2.539) / J. Cell Biol. by P. Vibert (1989)
  49. Walker, M. &Trinick, J. (1988) Visualization of domains in native and nucleotide-trapped myosin heads by negative staining.J. Muscle Res. Cell Motil. 9, 359–66. (10.1007/BF01773879) / J. Muscle Res. Cell Motil. by M. Walker (1988)
  50. Wallimann, T. &Szent-Györgyi, A. G. (1981) An immunological approach to myosin light-chain function in thick filament linked regulation. 2. Effect of anti-scallop myosin light-chain antibodies. Possible regulatory role for the essential light chain.Biochemistry 20, 1188–97. (10.1021/bi00508a021) / Biochemistry by T. Wallimann (1981)
  51. Wallimann, T., Hardwicke, P. M. D. &Szent-Györgyi, A. G. (1982) Regulatory and essential light-chain interactions in scallop myosin. II. Photochemical cross-linking of regulatory and essential light-chains by heterobifunctional reagents.J. Mol. Biol. 156, 153–73. (10.1016/0022-2836(82)90464-8) / J. Mol. Biol. by T. Wallimann (1982)
  52. Wells, C. &Bagshaw, C. R. (1984) The Ca2+ sensitivity of the actin-activated ATPase of scallop heavy meromyosin.FEBS Lett. 168, 260–4. (10.1016/0014-5793(84)80258-6) / FEBS Lett. by C. Wells (1984)
  53. Wells, C. &Bagshaw, C. R. (1985) Calcium regulation of molluscan myosin ATPase in the absence of actin.Nature (Lond.) 313, 696–7. (10.1038/313696a0) / Nature (Lond.) by C. Wells (1985)
  54. Wells, C., Warriner, K. E. &Bagshaw, C. R. (1985) Fluorescence studies on the nucleotide- and Ca2+-binding domains of molluscan myosin.Biochem. J. 231, 31–8. (10.1042/bj2310031) / Biochem. J. by C. Wells (1985)
  55. Winkelmann, D. A., Almeda, S., Vibert, P. J. &Cohen, C. (1984) A new myosin fragment: visualization of the regulatory domain.Nature (Lond.) 307, 758–60. (10.1038/307758a0) / Nature (Lond.) by D. A. Winkelmann (1984)
Dates
Type When
Created 20 years, 2 months ago (June 17, 2005, 4:21 a.m.)
Deposited 4 years, 1 month ago (July 11, 2021, 7:28 p.m.)
Indexed 1 year, 9 months ago (Nov. 16, 2023, 3:01 p.m.)
Issued 33 years ago (Aug. 1, 1992)
Published 33 years ago (Aug. 1, 1992)
Published Print 33 years ago (Aug. 1, 1992)
Funders 0

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@article{Young_Frado_1992, title={Structural changes induced in scallop heavy meromyosin molecules by Ca2+ and ATP}, volume={13}, ISSN={1573-2657}, url={http://dx.doi.org/10.1007/bf01738038}, DOI={10.1007/bf01738038}, number={4}, journal={Journal of Muscle Research and Cell Motility}, publisher={Springer Science and Business Media LLC}, author={Young Frado, Ling-Ling and Craig, Roger}, year={1992}, month=aug, pages={436–446} }