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Journal Abstract Search

184 related items for PubMed ID: 2141027

  • 1. Regulation of the actin-activated ATPase activity of Acanthamoeba myosin II by copolymerization with phosphorylated and dephosphorylated peptides derived from the carboxyl-terminal end of the heavy chain.
    Ganguly C, Atkinson MA, Attri AK, Sathyamoorthy V, Bowers B, Korn ED.
    J Biol Chem; 1990 Jun 15; 265(17):9993-8. PubMed ID: 2141027
    [Abstract] [Full Text] [Related]

  • 2. Cooperative dependence of the actin-activated Mg2+-ATPase activity of Acanthamoeba myosin II on the extent of filament phosphorylation.
    Atkinson MA, Lambooy PK, Korn ED.
    J Biol Chem; 1989 Mar 05; 264(7):4127-32. PubMed ID: 2521858
    [Abstract] [Full Text] [Related]

  • 3. Filament formation and actin-activated ATPase activity are abolished by proteolytic removal of a small peptide from the tip of the tail of the heavy chain of Acanthamoeba myosin II.
    Kuznicki J, Côté GP, Bowers B, Korn ED.
    J Biol Chem; 1985 Feb 10; 260(3):1967-72. PubMed ID: 3155741
    [Abstract] [Full Text] [Related]

  • 4. Functional consequences of the proteolytic removal of regulatory serines from the nonhelical tailpiece of Acanthamoeba myosin II.
    Sathyamoorthy V, Atkinson MA, Bowers B, Korn ED.
    Biochemistry; 1990 Apr 17; 29(15):3793-7. PubMed ID: 2160267
    [Abstract] [Full Text] [Related]

  • 5. Regulation of the actin-activated ATPase and in vitro motility activities of monomeric and filamentous Acanthamoeba myosin II.
    Ganguly C, Baines IC, Korn ED, Sellers J.
    J Biol Chem; 1992 Oct 15; 267(29):20900-4. PubMed ID: 1400404
    [Abstract] [Full Text] [Related]

  • 6. Limited tryptic digestion of Acanthamoeba myosin IA abolishes regulation of actin-activated ATPase activity by heavy chain phosphorylation.
    Lynch TJ, Brzeska H, Korn ED.
    J Biol Chem; 1987 Oct 05; 262(28):13842-9. PubMed ID: 2958454
    [Abstract] [Full Text] [Related]

  • 7. The effect of actin and phosphorylation on the tryptic cleavage pattern of Acanthamoeba myosin IA.
    Brzeska H, Lynch TJ, Korn ED.
    J Biol Chem; 1989 Jun 15; 264(17):10243-50. PubMed ID: 2524493
    [Abstract] [Full Text] [Related]

  • 8. Localization of the actin-binding sites of Acanthamoeba myosin IB and effect of limited proteolysis on its actin-activated Mg2+-ATPase activity.
    Brzeska H, Lynch TJ, Korn ED.
    J Biol Chem; 1988 Jan 05; 263(1):427-35. PubMed ID: 2961746
    [Abstract] [Full Text] [Related]

  • 9. A structural difference between filaments of phosphorylated and dephosphorylated Acanthamoeba myosin II revealed by electric birefringence.
    Rau DC, Ganguly C, Korn ED.
    J Biol Chem; 1993 Mar 05; 268(7):4612-24. PubMed ID: 8444836
    [Abstract] [Full Text] [Related]

  • 10. Enzymatic activity and filament assembly of Acanthamoeba myosin II are regulated by adjacent domains at the end of the tail.
    Atkinson MA, Appella E, Corigliano-Murphy MA, Korn ED.
    FEBS Lett; 1988 Jul 18; 234(2):435-8. PubMed ID: 2968922
    [Abstract] [Full Text] [Related]

  • 11. Purification and characterization of a third isoform of myosin I from Acanthamoeba castellanii.
    Lynch TJ, Brzeska H, Miyata H, Korn ED.
    J Biol Chem; 1989 Nov 15; 264(32):19333-9. PubMed ID: 2530229
    [Abstract] [Full Text] [Related]

  • 12. Limited proteolysis reveals a structural difference in the globular head domains of dephosphorylated and phosphorylated Acanthamoeba myosin II.
    Ganguly C, Martin B, Bubb M, Korn ED.
    J Biol Chem; 1992 Oct 15; 267(29):20905-8. PubMed ID: 1400405
    [Abstract] [Full Text] [Related]

  • 13. Supramolecular regulation of the actin-activated ATPase activity of filaments of Acanthamoeba Myosin II.
    Kuznicki J, Albanesi JP, Côté GP, Korn ED.
    J Biol Chem; 1983 May 25; 258(10):6011-4. PubMed ID: 6222038
    [Abstract] [Full Text] [Related]

  • 14.
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  • 15. Structure-function studies on Acanthamoeba myosins IA, IB, and II.
    Korn ED, Atkinson MA, Brzeska H, Hammer JA, Jung G, Lynch TJ.
    J Cell Biochem; 1988 Jan 25; 36(1):37-50. PubMed ID: 3277984
    [Abstract] [Full Text] [Related]

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  • 17. Acanthamoeba cofactor protein is a heavy chain kinase required for actin activation of the Mg2+-ATPase activity of Acanthamoeba myosin I.
    Maruta H, Korn ED.
    J Biol Chem; 1977 Dec 10; 252(23):8329-32. PubMed ID: 144730
    [Abstract] [Full Text] [Related]

  • 18. The localization and sequence of the phosphorylation sites of Acanthamoeba myosins I. An improved method for locating the phosphorylated amino acid.
    Brzeska H, Lynch TJ, Martin B, Korn ED.
    J Biol Chem; 1989 Nov 15; 264(32):19340-8. PubMed ID: 2530230
    [Abstract] [Full Text] [Related]

  • 19. Proteolytic separation of the actin-activatable ATPase site from the phosphorylation site on the heavy chain of Acanthamoeba myosin IA.
    Maruta H, Korn ED.
    J Biol Chem; 1981 Jan 10; 256(1):503-6. PubMed ID: 6108957
    [Abstract] [Full Text] [Related]

  • 20. Nucleotides increase the internal flexibility of filaments of dephosphorylated Acanthamoeba myosin II.
    Redowicz MJ, Korn ED, Rau DC.
    J Biol Chem; 1996 May 24; 271(21):12401-7. PubMed ID: 8647844
    [Abstract] [Full Text] [Related]

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