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213 related items for PubMed ID: 14506265

  • 1. 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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  • 2. Protein kinase C-mediated phosphorylation and calmodulin binding of recombinant myristoylated alanine-rich C kinase substrate (MARCKS) and MARCKS-related protein.
    Verghese GM, Johnson JD, Vasulka C, Haupt DM, Stumpo DJ, Blackshear PJ.
    J Biol Chem; 1994 Mar 25; 269(12):9361-7. PubMed ID: 8132675
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  • 3. Calcium binding and conformational properties of calmodulin complexed with peptides derived from myristoylated alanine-rich C kinase substrate (MARCKS) and MARCKS-related protein (MRP).
    Porumb T, Crivici A, Blackshear PJ, Ikura M.
    Eur Biophys J; 1997 Mar 25; 25(4):239-47. PubMed ID: 9112755
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  • 6. Isolation of the non-myristoylated form of a major substrate of protein kinase C (MARCKS) from bovine brain.
    Manenti S, Sorokine O, Van Dorsselaer A, Taniguchi H.
    J Biol Chem; 1993 Apr 05; 268(10):6878-81. PubMed ID: 8463217
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  • 11. Phosphorylation, high ionic strength, and calmodulin reverse the binding of MARCKS to phospholipid vesicles.
    Kim J, Shishido T, Jiang X, Aderem A, McLaughlin S.
    J Biol Chem; 1994 Nov 11; 269(45):28214-9. PubMed ID: 7961759
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  • 12. Myristoylation-dependent N-terminal cleavage of the myristoylated alanine-rich C kinase substrate (MARCKS) by cellular extracts.
    Braun T, McIlhinney RA, Vergères G.
    Biochimie; 2000 Aug 11; 82(8):705-15. PubMed ID: 11018286
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  • 13. 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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  • 14. Crystal structure of a MARCKS peptide containing the calmodulin-binding domain in complex with Ca2+-calmodulin.
    Yamauchi E, Nakatsu T, Matsubara M, Kato H, Taniguchi H.
    Nat Struct Biol; 2003 Mar 24; 10(3):226-31. PubMed ID: 12577052
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  • 15. Membrane association of the myristoylated alanine-rich C kinase substrate (MARCKS) protein appears to involve myristate-dependent binding in the absence of a myristoyl protein receptor.
    George DJ, Blackshear PJ.
    J Biol Chem; 1992 Dec 05; 267(34):24879-85. PubMed ID: 1332970
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  • 18. Differential expression of MARCKS and other calmodulin-binding protein kinase C substrates in cultured neuroblastoma and glioma cells.
    Rosé SD, Cook HW, Palmer FB, Ridgway ND, Byers DM.
    J Neurochem; 1994 Dec 05; 63(6):2314-23. PubMed ID: 7964753
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  • 20. MARCKS is a natively unfolded protein with an inaccessible actin-binding site: evidence for long-range intramolecular interactions.
    Tapp H, Al-Naggar IM, Yarmola EG, Harrison A, Shaw G, Edison AS, Bubb MR.
    J Biol Chem; 2005 Mar 18; 280(11):9946-56. PubMed ID: 15640140
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