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Journal Abstract Search

209 related items for PubMed ID: 12097325

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  • 2. The effector domain of myristoylated alanine-rich C kinase substrate binds strongly to phosphatidylinositol 4,5-bisphosphate.
    Wang J, Arbuzova A, Hangyás-Mihályné G, McLaughlin S.
    J Biol Chem; 2001 Feb 16; 276(7):5012-9. PubMed ID: 11053422
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  • 3. Membrane binding of peptides containing both basic and aromatic residues. Experimental studies with peptides corresponding to the scaffolding region of caveolin and the effector region of MARCKS.
    Arbuzova A, Wang L, Wang J, Hangyás-Mihályné G, Murray D, Honig B, McLaughlin S.
    Biochemistry; 2000 Aug 22; 39(33):10330-9. PubMed ID: 10956022
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  • 6. Binding of peptides with basic and aromatic residues to bilayer membranes: phenylalanine in the myristoylated alanine-rich C kinase substrate effector domain penetrates into the hydrophobic core of the bilayer.
    Zhang W, Crocker E, McLaughlin S, Smith SO.
    J Biol Chem; 2003 Jun 13; 278(24):21459-66. PubMed ID: 12670959
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  • 8. Reversible - through calmodulin - electrostatic interactions between basic residues on proteins and acidic lipids in the plasma membrane.
    McLaughlin S, Hangyás-Mihályné G, Zaitseva I, Golebiewska U.
    Biochem Soc Symp; 2005 Jun 13; (72):189-98. PubMed ID: 15649142
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  • 9. Myristoylated alanine-rich C kinase substrate (MARCKS) sequesters spin-labeled phosphatidylinositol 4,5-bisphosphate in lipid bilayers.
    Rauch ME, Ferguson CG, Prestwich GD, Cafiso DS.
    J Biol Chem; 2002 Apr 19; 277(16):14068-76. PubMed ID: 11825894
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  • 10. Kinetics of interaction of the myristoylated alanine-rich C kinase substrate, membranes, and calmodulin.
    Arbuzova A, Wang J, Murray D, Jacob J, Cafiso DS, McLaughlin S.
    J Biol Chem; 1997 Oct 24; 272(43):27167-77. PubMed ID: 9341159
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  • 11. Myristoylated alanine-rich C kinase substrate (MARCKS) produces reversible inhibition of phospholipase C by sequestering phosphatidylinositol 4,5-bisphosphate in lateral domains.
    Glaser M, Wanaski S, Buser CA, Boguslavsky V, Rashidzada W, Morris A, Rebecchi M, Scarlata SF, Runnels LW, Prestwich GD, Chen J, Aderem A, Ahn J, McLaughlin S.
    J Biol Chem; 1996 Oct 18; 271(42):26187-93. PubMed ID: 8824266
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  • 12. Location of the myristoylated alanine-rich C-kinase substrate (MARCKS) effector domain in negatively charged phospholipid bicelles.
    Ellena JF, Burnitz MC, Cafiso DS.
    Biophys J; 2003 Oct 18; 85(4):2442-8. PubMed ID: 14507707
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  • 18. Direct involvement of protein myristoylation in myristoylated alanine-rich C kinase substrate (MARCKS)-calmodulin interaction.
    Matsubara M, Titani K, Taniguchi H, Hayashi N.
    J Biol Chem; 2003 Dec 05; 278(49):48898-902. PubMed ID: 14506265
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  • 20. Interaction between actin and the effector peptide of MARCKS-related protein. Identification of functional amino acid segments.
    Wohnsland F, Schmitz AA, Steinmetz MO, Aebi U, Vergéres G.
    J Biol Chem; 2000 Jul 07; 275(27):20873-9. PubMed ID: 10748210
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