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.-Reference-Cited by-同舟云学术

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.

Published:1992-11 Issue:31 Volume:267 Page:22310-22315
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Manenti S,Sorokine O,Van Dorsselaer A,Taniguchi H

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference31 articles.

1. The role of protein kinase C in cell surface signal transduction and tumour promotion

2. Studies and Perspectives of Protein Kinase C

3. The 87-kDa protein, a major specific substrate for protein kinase C: purification from bovine brain and characterization.

4. Widespread occurrence of "87 kDa," a major specific substrate for protein kinase C.

5. SEQUENCES OF INTEREST: Molecular Cloning, Sequence, and Expression of a cDNA Encoding the Chicken Myristoylated Alanine-Rich C Kinase Substrate (MARCKS)

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