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cobaltiprotoporphyrin

Known as: cobalt protoporphyrin, cobalt protoporphyrin IX 
 
National Institutes of Health

Papers overview

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Highly Cited
2009
Highly Cited
2009
We examined our hypothesis that heme-oxygenase-1 (HO-1)-derived carbon monoxide (CO) inhibits the release of high-mobility group… Expand
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Highly Cited
2008
Highly Cited
2008
OBJECTIVE—We hypothesized that the induction of heme oxygenase (HO)-1 and increased HO activity, which induces arterial… Expand
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Highly Cited
2007
Highly Cited
2007
Heme oxygenase-1 (HO-1, encoded by HMOX1) dampens inflammatory reactions via the catabolism of heme into CO, Fe, and biliverdin… Expand
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Highly Cited
2006
Highly Cited
2006
Heme oxygenase (HO) catalyzes the conversion of heme to biliverdin with the release of iron and carbon monoxide. HO‐1 is highly… Expand
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Highly Cited
2006
Highly Cited
2006
Up-regulation of heme oxygenase (HO-1) by either cobalt protoporphyrin (CoPP) or human gene transfer improves vascular and renal… Expand
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Highly Cited
2005
Highly Cited
2005
Heme oxygenase-1 (HO-1) is an intracellular enzyme that degrades heme and inhibits immune responses and inflammation in vivo. In… Expand
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Highly Cited
2005
Highly Cited
2005
Increased heme oxygenase (HO)-1 activity attenuates endothelial cell apoptosis and decreases superoxide anion (O2-) formation in… Expand
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Highly Cited
2004
Highly Cited
2004
Heme oxygenase‐1 (HO‐1) degrades heme into iron, biliverdin, and carbon monoxide (CO). HO‐ 1 expression can be used… Expand
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Highly Cited
2004
Highly Cited
2004
Background—Heme oxygenase-1 (HO-1) is a stress-response enzyme implicated in cardioprotection. To explore whether HO-1 has a role… Expand
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Highly Cited
1999
Highly Cited
1999
We examined the effects of upregulation of heme oxygenase-1 (HO-1) in steatotic rat liver models of ex vivo cold ischemia… Expand
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