Properties of human kidney heme oxygenase: Inhibition by synthetic heme analogues and metalloporphyrins-Reference-Cited by-同舟云学术

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Properties of human kidney heme oxygenase: Inhibition by synthetic heme analogues and metalloporphyrins

Published:1988-12 Issue:2 Volume:157 Page:480-487
ISSN:0006-291X
Container-title:Biochemical and Biophysical Research Communications
language:en
Short-container-title:Biochemical and Biophysical Research Communications

Author:

Martasek Pavel,Solangi Karim,Goodman Alvin I.,Levere Richard D.,Chernick Richard J.,Abraham Nader G.

Funder

National Institutes of Health

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry,Biophysics

Reference30 articles.

1. Reduced nicotinamide adenine dinucleotide phosphate dependent biliverdin reductase. Partial purification and characterization

2. Purification and properties of bovine spleen heme oxygenase. Amino acid composition and sites of action of inhibitors of heme oxidation.

3. Tin-protoporphyrin suppression of hyperbilirubinemia in mutant mice with severe hemolytic anemia

4. Inducible heme oxygenase in the kidney: a model for the homeostatic control of hemoglobin catabolism

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1. Reciprocal regulation of carbon monoxide metabolism and the circadian clock;Nature Structural & Molecular Biology;2016-11-28

2. Heme Oxygenase-1 in Kidney Health and Disease;Antioxidants & Redox Signaling;2016-07-20

3. Metalloporphyrins – An Update;Frontiers in Pharmacology;2012

4. Mutations of human cytochrome P450 reductase differentially modulate heme oxygenase-1 activity and oligomerization;Archives of Biochemistry and Biophysics;2011-09

5. Measurement of Membrane-Bound Human Heme Oxygenase-1 Activity Using a Chemically Defined Assay System;Drug Metabolism and Disposition;2009-01-08

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