151 related articles for article (PubMed ID: 10631796)
1. Protein myristoylation in protein-lipid and protein-protein interactions.
Taniguchi H
Biophys Chem; 1999 Dec; 82(2-3):129-37. PubMed ID: 10631796
[TBL] [Abstract][Full Text] [Related]
2. Myristoylation-dependent and electrostatic interactions exert independent effects on the membrane association of the myristoylated alanine-rich protein kinase C substrate protein in intact cells.
Swierczynski SL; Blackshear PJ
J Biol Chem; 1996 Sep; 271(38):23424-30. PubMed ID: 8798548
[TBL] [Abstract][Full Text] [Related]
3. 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; 82(8):705-15. PubMed ID: 11018286
[TBL] [Abstract][Full Text] [Related]
4. The myristoyl moiety of myristoylated alanine-rich C kinase substrate (MARCKS) and MARCKS-related protein is embedded in the membrane.
Vergères G; Manenti S; Weber T; Stürzinger C
J Biol Chem; 1995 Aug; 270(34):19879-87. PubMed ID: 7650001
[TBL] [Abstract][Full Text] [Related]
5. Identification of the calmodulin-binding domain of neuron-specific protein kinase C substrate protein CAP-22/NAP-22. Direct involvement of protein myristoylation in calmodulin-target protein interaction.
Takasaki A; Hayashi N; Matsubara M; Yamauchi E; Taniguchi H
J Biol Chem; 1999 Apr; 274(17):11848-53. PubMed ID: 10207003
[TBL] [Abstract][Full Text] [Related]
6. The myristoyl-electrostatic switch: a modulator of reversible protein-membrane interactions.
McLaughlin S; Aderem A
Trends Biochem Sci; 1995 Jul; 20(7):272-6. PubMed ID: 7667880
[TBL] [Abstract][Full Text] [Related]
7. 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; 278(49):48898-902. PubMed ID: 14506265
[TBL] [Abstract][Full Text] [Related]
8. Demyristoylation of the major substrate of protein kinase C (MARCKS) by the cytoplasmic fraction of brain synaptosomes.
Manenti S; Sorokine O; Van Dorsselaer A; Taniguchi H
J Biol Chem; 1994 Mar; 269(11):8309-13. PubMed ID: 8132554
[TBL] [Abstract][Full Text] [Related]
9. Myristoylation does not modulate the properties of MARCKS-related protein (MRP) in solution.
Schleiff E; Schmitz A; McIlhinney RA; Manenti S; Vergères G
J Biol Chem; 1996 Oct; 271(43):26794-802. PubMed ID: 8900160
[TBL] [Abstract][Full Text] [Related]
10. Overexpression of the myristoylated alanine-rich C-kinase substrate inhibits cell adhesion to extracellular matrix components.
Spizz G; Blackshear PJ
J Biol Chem; 2001 Aug; 276(34):32264-73. PubMed ID: 11413143
[TBL] [Abstract][Full Text] [Related]
11. A mouse brain cDNA encodes a novel protein with the protein kinase C phosphorylation site domain common to MARCKS.
Umekage T; Kato K
FEBS Lett; 1991 Jul; 286(1-2):147-51. PubMed ID: 1864362
[TBL] [Abstract][Full Text] [Related]
12. Cross-talk unfolded: MARCKS proteins.
Arbuzova A; Schmitz AA; Vergères G
Biochem J; 2002 Feb; 362(Pt 1):1-12. PubMed ID: 11829734
[TBL] [Abstract][Full Text] [Related]
13. Binding of MARCKS (myristoylated alanine-rich C kinase substrate)-related protein (MRP) to vesicular phospholipid membranes.
Vergères G; Ramsden JJ
Biochem J; 1998 Feb; 330 ( Pt 1)(Pt 1):5-11. PubMed ID: 9461483
[TBL] [Abstract][Full Text] [Related]
14. Interactions controlling the membrane binding of basic protein domains: phenylalanine and the attachment of the myristoylated alanine-rich C-kinase substrate protein to interfaces.
Victor K; Jacob J; Cafiso DS
Biochemistry; 1999 Sep; 38(39):12527-36. PubMed ID: 10504221
[TBL] [Abstract][Full Text] [Related]
15. The role of myristoylated protein kinase C substrates in intracellular signaling pathways in macrophages.
Aderem A
Curr Top Microbiol Immunol; 1992; 181():189-207. PubMed ID: 1424780
[No Abstract] [Full Text] [Related]
16. Analogous structural motifs in myelin basic protein and in MARCKS.
Harauz G; Ishiyama N; Bates IR
Mol Cell Biochem; 2000 Jun; 209(1-2):155-63. PubMed ID: 10942213
[TBL] [Abstract][Full Text] [Related]
17. 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; 63(6):2314-23. PubMed ID: 7964753
[TBL] [Abstract][Full Text] [Related]
18. MARCKS, a major protein kinase C substrate, assumes non-helical conformations both in solution and in complex with Ca2+-calmodulin.
Matsubara M; Yamauchi E; Hayashi N; Taniguchi H
FEBS Lett; 1998 Jan; 421(3):203-7. PubMed ID: 9468306
[TBL] [Abstract][Full Text] [Related]
19. 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; 277(16):14068-76. PubMed ID: 11825894
[TBL] [Abstract][Full Text] [Related]
20. Binding of myristoylated alanine-rich protein kinase C substrate to phosphoinositides attenuates the phosphorylation by protein kinase C.
Seki K; Sheu FS; Huang KP
Arch Biochem Biophys; 1996 Feb; 326(2):193-201. PubMed ID: 8611023
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]