Department of Urology
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Biliverdin reductase, a novel regulator for induction of activating transcription factor-2 and heme oxygenase-1.
The Journal of biological chemistry May, 2004 | Pubmed ID: 14988408
Small interference RNA-mediated gene silencing of human biliverdin reductase, but not that of heme oxygenase-1, attenuates arsenite-mediated induction of the oxygenase and increases apoptosis in 293A kidney cells.
The Journal of biological chemistry Apr, 2005 | Pubmed ID: 15741166
Human biliverdin reductase, a previously unknown activator of protein kinase C betaII.
The Journal of biological chemistry Mar, 2007 | Pubmed ID: 17227757
Regulation of TNF-alpha-activated PKC-zeta signaling by the human biliverdin reductase: identification of activating and inhibitory domains of the reductase.
FASEB journal : official publication of the Federation of American Societies for Experimental Biology Dec, 2007 | Pubmed ID: 17639074
Human biliverdin reductase is an ERK activator; hBVR is an ERK nuclear transporter and is required for MAPK signaling.
Proceedings of the National Academy of Sciences of the United States of America May, 2008 | Pubmed ID: 18463290
Human biliverdin reductase suppresses Goodpasture antigen-binding protein (GPBP) kinase activity: the reductase regulates tumor necrosis factor-alpha-NF-kappaB-dependent GPBP expression.
The Journal of biological chemistry Apr, 2010 | Pubmed ID: 20177069
Characterization of the human biliverdin reductase gene structure and regulatory elements: promoter activity is enhanced by hypoxia and suppressed by TNF-alpha-activated NF-kappaB.
FASEB journal : official publication of the Federation of American Societies for Experimental Biology Sep, 2010 | Pubmed ID: 20410444
Formation of ternary complex of human biliverdin reductase-protein kinase Cδ-ERK2 protein is essential for ERK2-mediated activation of Elk1 protein, nuclear factor-κB, and inducible nitric-oxidase synthase (iNOS).
The Journal of biological chemistry Jan, 2012 | Pubmed ID: 22065579
The human biliverdin reductase-based peptide fragments and biliverdin regulate protein kinase Cδ activity: the peptides are inhibitors or substrate for the protein kinase C.
The Journal of biological chemistry Jul, 2012 | Pubmed ID: 22584576
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