Manenti S - Search Results

1

Affinity purification and characterization of myristoylated alanine-rich protein kinase C substrate (MARCKS) from bovine brain. Comparison of the cytoplasmic and the membrane-bound forms.

Manenti S, Sorokine O, Van Dorsselaer A, Taniguchi H. Manenti S, et al. J Biol Chem. 1992 Nov 5;267(31):22310-5. J Biol Chem. 1992. PMID: 1429582 Free article.

2

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. Taniguchi H, et al. Among authors: manenti s. J Biol Chem. 1994 Jul 15;269(28):18299-302. J Biol Chem. 1994. PMID: 8034575 Free article.

3

A mass spectrometric study on the in vivo posttranslational modification of GAP-43.

Taniguchi H, Suzuki M, Manenti S, Titani K. Taniguchi H, et al. Among authors: manenti s. J Biol Chem. 1994 Sep 9;269(36):22481-4. J Biol Chem. 1994. PMID: 8077193 Free article.

4

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. Manenti S, et al. J Biol Chem. 1994 Mar 18;269(11):8309-13. J Biol Chem. 1994. PMID: 8132554 Free article.

5

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. Manenti S, et al. J Biol Chem. 1993 Apr 5;268(10):6878-81. J Biol Chem. 1993. PMID: 8463217 Free article.

This mass is about 200 Da smaller than that of MARCKS determined by mass spectrometry analysis (Manenti, S., Sorokine, O., Van Dorsselaer, A., and Taniguchi, H. (1992) J. Biol. Chem. 267, 22310-22315), close to the value expected for the change due to N-terminal myr …

This mass is about 200 Da smaller than that of MARCKS determined by mass spectrometry analysis (Manenti, S., Sorokine, O., Van …

6

Interaction of myristoylated alanine-rich protein kinase C substrate (MARCKS) with membrane phospholipids.

Taniguchi H, Manenti S. Taniguchi H, et al. Among authors: manenti s. J Biol Chem. 1993 May 15;268(14):9960-3. J Biol Chem. 1993. PMID: 8486722 Free article.

7

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. Manenti S, et al. J Neurosci Res. 1997 May 1;48(3):259-63. doi: 10.1002/(sici)1097-4547(19970501)48:3<259::aid-jnr8>3.0.co;2-e. J Neurosci Res. 1997. PMID: 9160248

8

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. Vergères G, et al. Among authors: manenti s. J Biol Chem. 1995 Aug 25;270(34):19879-87. doi: 10.1074/jbc.270.34.19879. J Biol Chem. 1995. PMID: 7650001 Free article.

9

Demyristoylation of myristoylated alanine-rich C kinase substrate.

Manenti S, Sorokine O, Van Dorsselaer A, Taniguchi H. Manenti S, et al. Biochem Soc Trans. 1995 Aug;23(3):561-4. doi: 10.1042/bst0230561. Biochem Soc Trans. 1995. PMID: 8566416 No abstract available.

10

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. Manenti S, et al. Biochem J. 1999 Jun 15;340 ( Pt 3)(Pt 3):775-82. Biochem J. 1999. PMID: 10359664 Free PMC article.

The myristoylated alanine-rich C-kinase substrate (MARCKS) purified from brain was recently characterized as a proline-directed kinase(s) substrate in vivo [Taniguchi, Manenti, Suzuki and Titani (1994) J. Biol. Chem. 269, 18299-18302]. ...

The myristoylated alanine-rich C-kinase substrate (MARCKS) purified from brain was recently characterized as a proline-directed kinase(s …

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