Article
Glucocorticoid-induced leucine zipper (GILZ)/NF-kappaB interaction: role of GILZ homo-dimerization and C-terminal domain.
Nucleic acids research - 1 Jan 2007
Di Marco Barbara, Massetti Michela, Bruscoli Stefano, Macchiarulo Antonio, Di Virgilio Rosa, Velardi Enrico, Donato Valerio, Migliorati Graziella, Riccardi Carlo
Abstract excerpt
Glucocorticoid-induced leucine zipper (GILZ) is a 137 amino acid protein, rapidly induced by treatment with glucocorticoids (GC), characterized by a leucine zipper (LZ) domain (76-97 amino acids), an N-terminal domain (1-75 amino acids) and a C-terminal PER domain (98-137 amino acids) rich in proline and glutamic acid residues. We have previously shown that GILZ binds to and inhibits NF-kappaB activity. In the...
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