(Q28242181)

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P11, a unique member of the S100 family of calcium-binding proteins, interacts with and inhibits the activity of the 85-kDa cytosolic phospholipase A2

scientific article (publication date: 4 July 1997)

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P11, a unique member of the S100 family of calcium-binding proteins, interacts with and inhibits the activity of the 85-kDa cytosolic phospholipase A2 (English)

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author name string

T Wu

1

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C W Angus

2

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X L Yao

3

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C Logun

4

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J H Shelhamer

5

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language of work or name

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publication date

4 July 1997

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Journal of Biological Chemistry

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272

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27

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17145-53

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Phospholipase A2 enzymes: regulation and physiological role.

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A novel arachidonic acid-selective cytosolic PLA2 contains a Ca(2+)-dependent translocation domain with homology to PKC and GAP

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cPLA2 is phosphorylated and activated by MAP kinase

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Characterization of the promoter for the human 85 kDa cytosolic phospholipase A2 gene

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5'-flanking region surrounding a human cytosolic phospholipase A2 gene

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Identification of a 27 bp 5'-flanking region element responsible for the low level constitutive expression of the human cytosolic phospholipase A2 gene

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Identification of phosphorylation sites of human 85-kDa cytosolic phospholipase A2 expressed in insect cells and present in human monocytes

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The S100 protein family

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Perspectives in S-100 protein biology. Review article

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The S100 protein family: history, function, and expression

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Ca2+-dependent phospholipid- (and membrane-) binding proteins

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Annexin II tetramer: structure and function

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The annexins and exocytosis

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Annexin structure and membrane interactions: a molecular perspective

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10.1074/JBC.272.27.17145

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