Cloning and Expression of Cytosolic Phospholipase A2 (cPLA2) and a Naturally Occurring Variant. Phosphorylation of Ser505 of Recombinant cPLA2 by p42 Mitogen-activated Protein Kinase Results in an Increase in Specific Activity-Reference-Cited by-同舟云学术

Cloning and Expression of Cytosolic Phospholipase A2 (cPLA2) and a Naturally Occurring Variant. Phosphorylation of Ser505 of Recombinant cPLA2 by p42 Mitogen-activated Protein Kinase Results in an Increase in Specific Activity

Published:1996-06-15 Issue:3 Volume:238 Page:690-697
ISSN:0014-2956
Container-title:European Journal of Biochemistry
language:en
Short-container-title:Eur J Biochem

Author:

Gordon Robert D.,Leighton Ian A.,Campbell David G.,Cohen Philip,Creaney Ann,Wilton David C.,Masters David J.,Ritchie Graham A. F.,Mott Richard,Taylor Ian W. F.,Bundell Kenneth R.,Douglas Lynne,Morten John,Needham Maurice

Publisher

Wiley

Subject

Biochemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1996.0690w.x/fullpdf

Reference50 articles.

1. Human cytosolic phospholipase A2 expressed in insect cells is extensively phosphorylated on Ser-505

2. Synthetic peptides as model substrates for the study of the specificity of the polycation-stimulated protein phosphatases

3. Inhibitor-2 functions like a chaperone to fold three expressed isoforms of mammalian protein phosphatase-1 into a conformation with the specificity and regulatory properties of the native enzyme

4. Identification of the sites in MAP kinase kinase-1 phosphorylated by p74raf-1.

5. High-level production of biologically active human cytosolic phospholipase A2 in baculovirus-infected insect cells

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