226 related articles for article (PubMed ID: 8550618)
1. Protein kinase C-mediated phosphorylation of the myristoylated alanine-rich C-kinase substrate protects it from specific proteolytic cleavage.
Spizz G; Blackshear PJ
J Biol Chem; 1996 Jan; 271(1):553-62. PubMed ID: 8550618
[TBL] [Abstract][Full Text] [Related]
2. Specific proteolytic cleavage of the myristoylated alanine-rich C kinase substrate between Asn 147 and Glu 148 also occurs in brain.
Manenti S; Taniguchi H; Sorokine O; Van Dorsselaer A; Darbon JM
J Neurosci Res; 1997 May; 48(3):259-63. PubMed ID: 9160248
[TBL] [Abstract][Full Text] [Related]
3. Identification and characterization of cathepsin B as the cellular MARCKS cleaving enzyme.
Spizz G; Blackshear PJ
J Biol Chem; 1997 Sep; 272(38):23833-42. PubMed ID: 9295331
[TBL] [Abstract][Full Text] [Related]
4. 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]
5. Specificity of the high affinity interaction of protein kinase C with a physiological substrate, myristoylated alanine-rich protein kinase C substrate.
Fujise A; Mizuno K; Ueda Y; Osada S; Hirai S; Takayanagi A; Shimizu N; Owada MK; Nakajima H; Ohno S
J Biol Chem; 1994 Dec; 269(50):31642-8. PubMed ID: 7989336
[TBL] [Abstract][Full Text] [Related]
6. Membrane association of the myristoylated alanine-rich C kinase substrate (MARCKS) protein. Mutational analysis provides evidence for complex interactions.
Swierczynski SL; Blackshear PJ
J Biol Chem; 1995 Jun; 270(22):13436-45. PubMed ID: 7768946
[TBL] [Abstract][Full Text] [Related]
7. Phosphorylation of the myristoylated protein kinase C substrate MARCKS by the cyclin E-cyclin-dependent kinase 2 complex in vitro.
Manenti S; Yamauchi E; Sorokine O; Knibiehler M; Van Dorsselaer A; Taniguchi H; Ducommun B; Darbon JM
Biochem J; 1999 Jun; 340 ( Pt 3)(Pt 3):775-82. PubMed ID: 10359664
[TBL] [Abstract][Full Text] [Related]
8. Phosphorylation-regulated calmodulin binding to a prominent cellular substrate for protein kinase C.
Graff JM; Young TN; Johnson JD; Blackshear PJ
J Biol Chem; 1989 Dec; 264(36):21818-23. PubMed ID: 2557340
[TBL] [Abstract][Full Text] [Related]
9. Protein kinase C substrate and inhibitor characteristics of peptides derived from the myristoylated alanine-rich C kinase substrate (MARCKS) protein phosphorylation site domain.
Graff JM; Rajan RR; Randall RR; Nairn AC; Blackshear PJ
J Biol Chem; 1991 Aug; 266(22):14390-8. PubMed ID: 1650359
[TBL] [Abstract][Full Text] [Related]
10. 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]
11. Neuroanatomical development in the absence of PKC phosphorylation of the myristoylated alanine-rich C-kinase substrate (MARCKS) protein.
Scarlett CO; Blackshear PJ
Brain Res Dev Brain Res; 2003 Aug; 144(1):25-42. PubMed ID: 12888215
[TBL] [Abstract][Full Text] [Related]
12. 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; 267(34):24879-85. PubMed ID: 1332970
[TBL] [Abstract][Full Text] [Related]
13. 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; 25(4):239-47. PubMed ID: 9112755
[TBL] [Abstract][Full Text] [Related]
14. Myristoylated alanine-rich C kinase substrate (MARCKS), a major protein kinase C substrate, is an in vivo substrate of proline-directed protein kinase(s). A mass spectroscopic analysis of the post-translational modifications.
Taniguchi H; Manenti S; Suzuki M; Titani K
J Biol Chem; 1994 Jul; 269(28):18299-302. PubMed ID: 8034575
[TBL] [Abstract][Full Text] [Related]
15. 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; 269(12):9361-7. PubMed ID: 8132675
[TBL] [Abstract][Full Text] [Related]
16. Ca2+ x calmodulin prevents myristoylated alanine-rich kinase C substrate protein phosphorylation by protein kinase Cs in C6 rat glioma cells.
Chakravarthy BR; Isaacs RJ; Morley P; Whitfield JF
J Biol Chem; 1995 Oct; 270(42):24911-6. PubMed ID: 7559616
[TBL] [Abstract][Full Text] [Related]
17. Adducin is an in vivo substrate for protein kinase C: phosphorylation in the MARCKS-related domain inhibits activity in promoting spectrin-actin complexes and occurs in many cells, including dendritic spines of neurons.
Matsuoka Y; Li X; Bennett V
J Cell Biol; 1998 Jul; 142(2):485-97. PubMed ID: 9679146
[TBL] [Abstract][Full Text] [Related]
18. 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; 347 Pt 1(Pt 1):139-46. PubMed ID: 10727412
[TBL] [Abstract][Full Text] [Related]
19. 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]
20. Characterization of the phosphatidylserine-binding region of rat MARCKS (myristoylated, alanine-rich protein kinase C substrate). Its regulation through phosphorylation of serine 152.
Nakaoka T; Kojima N; Ogita T; Tsuji S
J Biol Chem; 1995 May; 270(20):12147-51. PubMed ID: 7744864
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
