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Biliverdine
Known as:
Ooecyan
, Biliverdin
, Dehydrobilirubin
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1,3,6,7-Tetramethyl-4,5-dicarboxyethyl-2,8-divinylbilenone. Biosynthesized from hemoglobin as a precursor of bilirubin. Occurs in the bile of…
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National Institutes of Health
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Related topics
Related topics
22 relations
Broader (1)
Bilirubin
Narrower (12)
Biliverdin IX
Biliverdin IX alpha
biliverdin IX delta dimethyl ester
biliverdin XIII alpha dimethyl ester
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In Blood
Process of secretion
agonists
analogs & derivatives
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Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
Review
2010
Review
2010
Targeting heme oxygenase-1 in vascular disease.
W. Durante
Current Drug Targets
2010
Corpus ID: 40052734
Heme oxygenase-1 (HO-1) metabolizes heme to generate carbon monoxide (CO), biliverdin, and iron. Biliverdin is subsequently…
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Highly Cited
2006
Highly Cited
2006
Heme oxygenase-1 inhibits apoptosis in Caco-2 cells via activation of Akt pathway.
J. Busserolles
,
J. Megías
,
M. Terencio
,
M. Alcaraz
International Journal of Biochemistry and Cell…
2006
Corpus ID: 22729971
Highly Cited
2001
Highly Cited
2001
Exacerbation of Chronic Renovascular Hypertension and Acute Renal Failure in Heme Oxygenase-1–Deficient Mice
P. Wiesel
,
Ananddeep Patel
,
+9 authors
M. Perrella
Circulation Research
2001
Corpus ID: 24397885
Abstract— Heme oxygenase (HO) is a cytoprotective enzyme that degrades heme (a potent oxidant) to generate carbon monoxide (a…
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Review
2001
Review
2001
Modulation of heme oxygenase in tissue injury and its implication in protection against gastrointestinal diseases.
Xin Guo
,
V. Shin
,
C. Cho
Life Science
2001
Corpus ID: 3235244
Review
2000
Review
2000
The heme oxygenase–carbon monoxide system: u regulator of hepatobiliary function
M. Suematsu
,
Y. Ishimura
Hepatology
2000
Corpus ID: 39693576
Heme oxygenase (HO) degrades protoheme IX by cleaving its a-methene bridge into carbon monoxide (CO), free divalent iron (Fe21…
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Highly Cited
1998
Highly Cited
1998
The crystal structure of nitrophorin 4 at 1.5 A resolution: transport of nitric oxide by a lipocalin-based heme protein.
John F. Andersen
,
A. Weichsel
,
Celia A. Balfour
,
Donald E. Champagne
,
W. Montfort
Structure
1998
Corpus ID: 19150802
Highly Cited
1988
Highly Cited
1988
In vitro attachment of bilins to apophycocyanin. I. Specific covalent adduct formation at cysteinyl residues involved in phycocyanobilin binding in C-phycocyanin.
D. Arciero
,
D. Bryant
,
A. Glazer
Journal of Biological Chemistry
1988
Corpus ID: 35521841
Expression of cloned alpha and beta subunit genes of Synechococcus sp. PCC7002 C-phycocyanin in Escherichia coli led to the…
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Highly Cited
1980
Highly Cited
1980
Preparation and properties of crystalline biliverdin IX alpha. Simple methods for preparing isomerically homogeneous biliverdin and [14C[biliverdin by using 2,3-dichloro-5,6-dicyanobenzoquinone.
A. Mcdonagh
,
L. Palma
Biochemical Journal
1980
Corpus ID: 10171088
Amorphous isomerically pure biliverdin IX alpha is readily prepared in more than 70% yield by dehydrogenation of bilirubin with 2…
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Highly Cited
1980
Highly Cited
1980
Inhibition of the mutagenicity of amino acid pyrolysis products by hemin and other biological pyrrole pigments.
S. Arimoto
,
Y. Ohara
,
T. Namba
,
T. Negishi
,
H. Hayatsu
Biochemical and Biophysical Research…
1980
Corpus ID: 19185123
Highly Cited
1979
Highly Cited
1979
Purification and properties of heme oxygenase from rat liver microsomes.
T. Yoshida
,
G. Kikuchi
Journal of Biological Chemistry
1979
Corpus ID: 23538632
Heme oxygenase was purified to apparent homogeneity from liver microsomes of rats which had been treated with either cobaltous…
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