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. 1973 Jul 1;58(1):230–237. doi: 10.1083/jcb.58.1.230

MICROFILAMENTS IN CHAOS CAROLINENSIS

Membrane Association, Distribution, and Heavy Meromyosin Binding in the Glycerinated Cell

Lucy T Comly 1
PMCID: PMC2109023  PMID: 4125372

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Abercrombie M., Heaysman J. E., Pegrum S. M. The locomotion of fibroblasts in culture. IV. Electron microscopy of the leading lamella. Exp Cell Res. 1971 Aug;67(2):359–367. doi: 10.1016/0014-4827(71)90420-4. [DOI] [PubMed] [Google Scholar]
  2. Adelman M. R., Taylor E. W. Further purification and characterization of slime mold myosin and slime mold actin. Biochemistry. 1969 Dec;8(12):4976–4988. doi: 10.1021/bi00840a047. [DOI] [PubMed] [Google Scholar]
  3. Adelman M. R., Taylor E. W. Isolation of an actomyosin-like protein complex from slime mold plasmodium and the separation of the complex into actin- and myosin-like fractions. Biochemistry. 1969 Dec;8(12):4964–4975. doi: 10.1021/bi00840a046. [DOI] [PubMed] [Google Scholar]
  4. Bruce D. L., Marshall J. M., Jr Some ionic and bioelectric properties of the ameba Chaos chaos. J Gen Physiol. 1965 Sep;49(1):151–178. doi: 10.1085/jgp.49.1.151. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Cloney R. A. Cytoplasmic filaments and cell movements: epidermal cells during ascidian metamorphosis. J Ultrastruct Res. 1966 Feb;14(3):300–328. doi: 10.1016/s0022-5320(66)80051-5. [DOI] [PubMed] [Google Scholar]
  6. Eisenberg E., Moos C. The interaction of actin with myosin and heavy meromyosin in solution at low ionic strength. J Biol Chem. 1967 Jun 25;242(12):2945–2951. [PubMed] [Google Scholar]
  7. Eisenberg E., Weihing R. R. Effect of skeletal muscle native tropomyosin on the interaction of amoeba actin with heavy meromyosin. Nature. 1970 Dec 12;228(5276):1092–1093. doi: 10.1038/2281092a0. [DOI] [PubMed] [Google Scholar]
  8. Hatano S., Oosawa F. Extraction of an actin-like protein from the plasmodium of a myxomycete and its interaction with myosin A from rabbit striated muscle. J Cell Physiol. 1966 Oct;68(2):197–202. doi: 10.1002/jcp.1040680214. [DOI] [PubMed] [Google Scholar]
  9. Hatano S., Oosawa F. Isolation and characterization of plasmodium actin. Biochim Biophys Acta. 1966 Oct 31;127(2):488–498. doi: 10.1016/0304-4165(66)90402-8. [DOI] [PubMed] [Google Scholar]
  10. Hatano S., Tazawa M. Isolation, purification and characterization of byosin B from myxomycete plasmodium. Biochim Biophys Acta. 1968 Apr 9;154(3):507–519. doi: 10.1016/0005-2795(68)90011-1. [DOI] [PubMed] [Google Scholar]
  11. Ishikawa H., Bischoff R., Holtzer H. Formation of arrowhead complexes with heavy meromyosin in a variety of cell types. J Cell Biol. 1969 Nov;43(2):312–328. [PMC free article] [PubMed] [Google Scholar]
  12. LOWEY S., COHEN C. Studies on the structure of myosin. J Mol Biol. 1962 Apr;4:293–308. doi: 10.1016/s0022-2836(62)80007-2. [DOI] [PubMed] [Google Scholar]
  13. Moore P. B., Huxley H. E., DeRosier D. J. Three-dimensional reconstruction of F-actin, thin filaments and decorated thin filaments. J Mol Biol. 1970 Jun 14;50(2):279–295. doi: 10.1016/0022-2836(70)90192-0. [DOI] [PubMed] [Google Scholar]
  14. NACHMIAS V. T. FIBRILLAR STRUCTURES IN THE CYTOPLASM OF CHAOS CHAOS. J Cell Biol. 1964 Oct;23:183–188. doi: 10.1083/jcb.23.1.183. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Nachmias V. T. Electron microscope observations on myosin from Physarum polycephalum. J Cell Biol. 1972 Mar;52(3):648–663. doi: 10.1083/jcb.52.3.648. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Nachmias V. T. Further electron microscope studies on fibrillar organization of the ground cytoplasm of Chaos chaos. J Cell Biol. 1968 Jul;38(1):40–50. doi: 10.1083/jcb.38.1.40. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Nachmias V. T., Huxley H. E. Electron microscope observations on actomyosin and actin preparations from Physarum polycephalum, and on their interaction with heavy meromyosin subfragment I from muscle myosin. J Mol Biol. 1970 May 28;50(1):83–90. doi: 10.1016/0022-2836(70)90105-1. [DOI] [PubMed] [Google Scholar]
  18. Nachmias V. T., Ingram W. C. Actomyosin from Physarum polycephalum: electron microscopy of myosin-enriched preparations. Science. 1970 Nov 13;170(3959):743–745. doi: 10.1126/science.170.3959.743. [DOI] [PubMed] [Google Scholar]
  19. Nachmias V. Filament formation by purified Physarum myosin. Proc Natl Acad Sci U S A. 1972 Aug;69(8):2011–2014. doi: 10.1073/pnas.69.8.2011. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Perry M. M., John H. A., Thomas N. S. Actin-like filaments in the cleavage furrow of newt egg. Exp Cell Res. 1971 Mar;65(1):249–253. doi: 10.1016/s0014-4827(71)80075-7. [DOI] [PubMed] [Google Scholar]
  21. Pollard T. D., Ito S. Cytoplasmic filaments of Amoeba proteus. I. The role of filaments in consistency changes and movement. J Cell Biol. 1970 Aug;46(2):267–289. doi: 10.1083/jcb.46.2.267. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Pollard T. D., Korn E. D. Filaments of Amoeba proteus. II. Binding of heavy meromyosin by thin filaments in motile cytoplasmic extracts. J Cell Biol. 1971 Jan;48(1):216–219. doi: 10.1083/jcb.48.1.216. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Pollard T. D., Shelton E., Weihing R. R., Korn E. D. Ultrastructural characterization of F-actin isolated from Acanthamoeba castellanii and identification of cytoplasmic filaments as F-actin by reaction with rabbit heavy meromyosin. J Mol Biol. 1970 May 28;50(1):91–97. doi: 10.1016/0022-2836(70)90106-3. [DOI] [PubMed] [Google Scholar]
  24. REYNOLDS E. S. The use of lead citrate at high pH as an electron-opaque stain in electron microscopy. J Cell Biol. 1963 Apr;17:208–212. doi: 10.1083/jcb.17.1.208. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Spooner B. S., Yamada K. M., Wessells N. K. Microfilaments and cell locomotion. J Cell Biol. 1971 Jun;49(3):595–613. doi: 10.1083/jcb.49.3.595. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Tilney L. G., Mooseker M. Actin in the brush-border of epithelial cells of the chicken intestine. Proc Natl Acad Sci U S A. 1971 Oct;68(10):2611–2615. doi: 10.1073/pnas.68.10.2611. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Weihing R. R., Korn E. D. Acanthamoeba actin. Isolation and properties. Biochemistry. 1971 Feb 16;10(4):590–600. doi: 10.1021/bi00780a008. [DOI] [PubMed] [Google Scholar]
  28. Weihing R. R., Korn E. D. Ameba actin: the presence of 3-methylhistidine. Biochem Biophys Res Commun. 1969 Jun 27;35(6):906–912. doi: 10.1016/0006-291x(69)90710-4. [DOI] [PubMed] [Google Scholar]
  29. Weihing R. R., Korn E. D. Epsilon-N-dimethyllysine in amoeba actin. Nature. 1970 Sep 19;227(5264):1263–1264. doi: 10.1038/2271263a0. [DOI] [PubMed] [Google Scholar]
  30. Woolley D. E. An actin-like protein from amoebae of dictyostelium discoideum. Arch Biochem Biophys. 1972 Jun;150(2):519–530. doi: 10.1016/0003-9861(72)90070-7. [DOI] [PubMed] [Google Scholar]

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