Taniguchi H - 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. Among authors: taniguchi h. 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. 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. 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. Among authors: taniguchi h. 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. Among authors: taniguchi h. 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 Dorsselaer, A …

6

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

Taniguchi H, Manenti S. Taniguchi H, et al. 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. Among authors: taniguchi h. 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

Demyristoylation of myristoylated alanine-rich C kinase substrate.

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

9

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. Among authors: taniguchi h. Biochem J. 1999 Jun 15;340 ( Pt 3)(Pt 3):775-82. Biochem J. 1999. PMID: 10359664 Free PMC article.

10

The C-terminal conserved domain of MARCKS is phosphorylated in vivo by proline-directed protein kinase. Application of ion trap mass spectrometry to the determination of protein phosphorylation sites.

Yamauchi E, Kiyonami R, Kanai M, Taniguchi H. Yamauchi E, et al. Among authors: taniguchi h. J Biol Chem. 1998 Feb 20;273(8):4367-71. doi: 10.1074/jbc.273.8.4367. J Biol Chem. 1998. PMID: 9468486 Free article.

We have previously shown that MARCKS purified from bovine brain is phosphorylated not only by protein kinase C but also by so-called proline-directed protein kinases in the well conserved N-terminal half of the molecule (Taniguchi, H., Manenti, S., Suzuki, M., and T …

We have previously shown that MARCKS purified from bovine brain is phosphorylated not only by protein kinase C but also by so-called proline …

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