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heme oxidation
Known as:
haem oxidation
The chemical reactions and pathways resulting in the loss of electrons from one or more atoms in heme. [GOC:mah]
National Institutes of Health
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Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
Review
2016
Review
2016
BACH1, the master regulator gene: A novel candidate target for cancer therapy.
Sadaf Davudian
,
B. Mansoori
,
Neda Shajari
,
A. Mohammadi
,
B. Baradaran
Gene
2016
Corpus ID: 28226515
Highly Cited
2009
Highly Cited
2009
Design and engineering of an O(2) transport protein
R. Koder
,
J. L. Ross Anderson
,
Lee A. Solomon
,
K. Reddy
,
C. Moser
,
P. Dutton
Nature
2009
Corpus ID: 4366003
The principles of natural protein engineering are obscured by overlapping functions and complexity accumulated through natural…
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Review
2003
Review
2003
The heme oxygenase system: its role in liver inflammation.
C. Wunder
,
R. Potter
Current drug targets. Cardiovascular…
2003
Corpus ID: 22592783
Heme Oxygenase is the rate-limiting enzyme in the degradation of heme into carbon monoxide (CO), iron and bilirubin. To date…
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Highly Cited
2003
Highly Cited
2003
How cytochromes with different folds control heme redox potentials.
J. Mao
,
K. Hauser
,
M. Gunner
Biochemistry
2003
Corpus ID: 14098245
The electrochemical midpoint potentials (E(m)'s) of 13 cytochromes, in globin (c, c(2), c(551), c(553)), four-helix bundle (c', b…
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Highly Cited
1998
Highly Cited
1998
Evidence for Heme-mediated Redox Regulation of Human Cystathionine β-Synthase Activity*
S. Taoka
,
Sunil Ohja
,
X. Shan
,
W. Kruger
,
R. Banerjee
Journal of Biological Chemistry
1998
Corpus ID: 39790237
Human cystathionine β-synthase catalyzes the first step in the catabolic removal of the toxic metabolite, homocysteine. It is…
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Review
1995
Review
1995
Nitric oxide (NO) protects against cellular damage by reactive oxygen species.
D. Wink
,
J. Cook
,
R. Pacelli
,
J. Liebmann
,
M. Krishna
,
J. Mitchell
Toxicology Letters
1995
Corpus ID: 32573507
Highly Cited
1987
Highly Cited
1987
Dual control mechanism for heme oxygenase: tin(IV)-protoporphyrin potently inhibits enzyme activity while markedly increasing content of enzyme protein in liver.
M. Sardana
,
A. Kappas
Proceedings of the National Academy of Sciences…
1987
Corpus ID: 8688977
Tin(IV)-protoporphyrin (Sn-protoporphyrin) potently inhibits heme degradation to bile pigments in vitro and in vivo, a property…
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Highly Cited
1981
Highly Cited
1981
Prevention of neonatal hyperbilirubinemia by tin protoporphyrin IX, a potent competitive inhibitor of heme oxidation.
G. Drummond
,
A. Kappas
Proceedings of the National Academy of Sciences…
1981
Corpus ID: 9930746
The effects of various metalloporphyrins on hepatic heme oxygenase (EC 1.14.99.3) activity were examined in order to identify…
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Highly Cited
1976
Highly Cited
1976
Studies on the mechanism of induction of haem oxygenase by cobalt and other metal ions.
M. Maines
,
A. Kappas
Biochemical Journal
1976
Corpus ID: 38473126
Cobalt ions (Co2+) are potent inducers of haem oxygenase in liver and inhibit microsomal drug oxidation probably by depleting…
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Highly Cited
1974
Highly Cited
1974
Cobalt induction of hepatic heme oxygenase; with evidence that cytochrome P-450 is not essential for this enzyme activity.
M. Maines
,
A. Kappas
Proceedings of the National Academy of Sciences…
1974
Corpus ID: 7998312
Treatment of rats in vivo with cobalt chloride stimulated heme oxidation by hepatic microsomes to levels up to 800% above…
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