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564 related items for PubMed ID: 8908202
1. Thrombin-induced phosphorylation of the myristoylated alanine-rich C kinase substrate (MARCKS) protein in bovine pulmonary artery endothelial cells. Zhao Y, Davis HW. J Cell Physiol; 1996 Nov; 169(2):350-7. PubMed ID: 8908202 [Abstract] [Full Text] [Related]
6. Hydrogen peroxide-induced cytoskeletal rearrangement in cultured pulmonary endothelial cells. Zhao Y, Davis HW. J Cell Physiol; 1998 Mar; 174(3):370-9. PubMed ID: 9462699 [Abstract] [Full Text] [Related]
7. Involvement of the theta-type protein kinase C in translocation of myristoylated alanine-rich C kinase substrate (MARCKS) during myogenesis of chick embryonic myoblasts. Kim SS, Kim JH, Kim HS, Park DE, Chung CH. Biochem J; 2000 Apr 01; 347 Pt 1(Pt 1):139-46. PubMed ID: 10727412 [Abstract] [Full Text] [Related]
8. MARCKS is a major PKC-dependent regulator of calmodulin targeting in smooth muscle. Gallant C, You JY, Sasaki Y, Grabarek Z, Morgan KG. J Cell Sci; 2005 Aug 15; 118(Pt 16):3595-605. PubMed ID: 16046479 [Abstract] [Full Text] [Related]
9. Histamine-induced phosphorylation of the regulatory light chain of myosin II disrupts the barrier integrity of corneal endothelial cells. Srinivas SP, Satpathy M, Guo Y, Anandan V. Invest Ophthalmol Vis Sci; 2006 Sep 15; 47(9):4011-8. PubMed ID: 16936117 [Abstract] [Full Text] [Related]
10. Regulation of endothelial cell gap formation and barrier dysfunction: role of myosin light chain phosphorylation. Garcia JG, Davis HW, Patterson CE. J Cell Physiol; 1995 Jun 15; 163(3):510-22. PubMed ID: 7775594 [Abstract] [Full Text] [Related]
11. The antibody specific for myristoylated alanine-rich C kinase substrate phosphorylated by protein kinase C: activation of protein kinase C in smooth muscle cells in human coronary arteries. Yamamoto H, Matsumura T, Kugiyama K, Oishi Y, Ogata N, Yasue H, Miyamoto E. Arch Biochem Biophys; 1998 Nov 15; 359(2):151-9. PubMed ID: 9808756 [Abstract] [Full Text] [Related]
12. Association between myristoylated alanin-rich C kinase substrate (MARCKS) translocation and cortical granule exocytosis in rat eggs. Eliyahu E, Shtraizent N, Tsaadon A, Shalgi R. Reproduction; 2006 Feb 15; 131(2):221-31. PubMed ID: 16452716 [Abstract] [Full Text] [Related]
13. 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 15; 326(2):193-201. PubMed ID: 8611023 [Abstract] [Full Text] [Related]
14. Thrombin-induced phosphorylation of the regulatory light chain of myosin II in cultured bovine corneal endothelial cells. Satpathy M, Gallagher P, Lizotte-Waniewski M, Srinivas SP. Exp Eye Res; 2004 Oct 15; 79(4):477-86. PubMed ID: 15381032 [Abstract] [Full Text] [Related]
15. Myristoylated alanine-rich C kinase substrate, but not Ca2+/calmodulin-dependent protein kinase II, is the mediator in cortical granules exocytosis. Tsaadon L, Kaplan-Kraicer R, Shalgi R. Reproduction; 2008 May 15; 135(5):613-24. PubMed ID: 18296509 [Abstract] [Full Text] [Related]
16. Thrombin-induced phosphorylation of MARCKS does not alter its interactions with calmodulin or actin. Neltner BS, Zhao Y, Sacks DB, Davis HW. Cell Signal; 2000 Feb 15; 12(2):71-9. PubMed ID: 10679575 [Abstract] [Full Text] [Related]
17. MARCKS phosphorylation by individual protein kinase C isozymes in insect Sf9 cells. Cabell CH, Verghese GM, Rankl NB, Burns DJ, Blackshear PJ. Proc Assoc Am Physicians; 1996 Jan 15; 108(1):37-46. PubMed ID: 8834063 [Abstract] [Full Text] [Related]
18. MARCKS is an actin filament crosslinking protein regulated by protein kinase C and calcium-calmodulin. Hartwig JH, Thelen M, Rosen A, Janmey PA, Nairn AC, Aderem A. Nature; 1992 Apr 16; 356(6370):618-22. PubMed ID: 1560845 [Abstract] [Full Text] [Related]
19. Protein kinase C activation during Ca2+-independent vascular smooth muscle contraction. Throckmorton DC, Packer CS, Brophy CM. J Surg Res; 1998 Jul 15; 78(1):48-53. PubMed ID: 9733617 [Abstract] [Full Text] [Related]
20. Phosphorylation of MARCKS (80-kDa) protein, a major substrate for protein kinase C in oligodendroglial progenitors. Bhat NR. J Neurosci Res; 1991 Oct 15; 30(2):447-54. PubMed ID: 1798060 [Abstract] [Full Text] [Related] Page: [Next] [New Search]