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Journal of Biological Chemistry, ISSN 0021-9258, 2017, Volume 292, Issue 32, pp. 13205 - 13229
Mammals incorporate a major proportion of absorbed iron as heme, which is catabolized by the heme oxygenase 1 (HO1)-NADPH-cytochrome P450 reductase (CPR)... 
TRANSPORT | POLY(C)-BINDING PROTEINS | MECHANISM | CARBON-MONOXIDE | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | KH DOMAINS | BINDING-PROTEIN | ABSORPTION | IDENTIFICATION | EXPRESSION | Heme Oxygenase-1 - chemistry | RNA-Binding Proteins - genetics | Heme Oxygenase-1 - metabolism | NADPH-Ferrihemoprotein Reductase - genetics | Heme - metabolism | NADPH-Ferrihemoprotein Reductase - antagonists & inhibitors | Transcription Factors - chemistry | Humans | Protein Multimerization | NADPH-Ferrihemoprotein Reductase - chemistry | Heme Oxygenase (Decyclizing) - chemistry | Recombinant Fusion Proteins - metabolism | Heme Oxygenase-1 - genetics | Biological Transport | RNA Interference | Gene Deletion | Protein Interaction Domains and Motifs | Heme Oxygenase (Decyclizing) - metabolism | Binding Sites | Heme Oxygenase (Decyclizing) - genetics | Binding, Competitive | Cell Line | NADPH-Ferrihemoprotein Reductase - metabolism | Metalloporphyrins - metabolism | RNA-Binding Proteins - chemistry | Recombinant Fusion Proteins - chemistry | Transcription Factors - genetics | Heme Oxygenase-1 - antagonists & inhibitors | Iron - metabolism | Protein Transport | Transcription Factors - metabolism | Structural Homology, Protein | Mutation | RNA-Binding Proteins - metabolism | Amino Acid Substitution | heme oxygenase | iron metabolism | protein interaction | heme | iron chaperone | protein | PCBP2 | iron | Cell Biology
Journal Article
Journal Article
Journal Article
Current opinion in chemical biology, ISSN 1367-5931, 2014, Volume 19, Issue 1, pp. 34 - 41
Journal Article
The Journal of biological chemistry, ISSN 1083-351X, 2018, Volume 293, Issue 43, pp. 16778 - 16790
Cytochromes c are ubiquitous proteins, essential for life in most organisms. Their distinctive characteristic is the covalent attachment of heme to their... 
post-translational modification (PTM) | CHAPERONE CCME | cytochrome c maturation | BACTERIA | APOCYTOCHROME-C | heme | NMR-SPECTROSCOPY | BIOCHEMISTRY & MOLECULAR BIOLOGY | CcmE | ESCHERICHIA-COLI | TRAFFICKING | CcmC | protein-protein interactions | BIOGENESIS SYSTEM | PATHWAY | nuclear magnetic resonance (NMR) | Gram-negative bacteria | System I | cytochrome c | BINDING SITE | LIGATION COMPLEX | Apoproteins - chemistry | Hemeproteins - genetics | Heme - metabolism | Crystallography, X-Ray | Cytochromes c - genetics | Cytochromes c - chemistry | Heme - chemistry | Heme - genetics | Hemeproteins - chemistry | Escherichia coli - metabolism | Membrane Proteins - metabolism | Protein Interaction Domains and Motifs | Escherichia coli - growth & development | Binding Sites | Apoproteins - metabolism | Bacterial Outer Membrane Proteins - genetics | Mutagenesis, Site-Directed | Hemeproteins - metabolism | Membrane Proteins - genetics | Cytochromes c - metabolism | Bacterial Outer Membrane Proteins - chemistry | Escherichia coli Proteins - metabolism | Bacterial Outer Membrane Proteins - metabolism | Membrane Proteins - chemistry | Escherichia coli - genetics | Apoproteins - genetics | Escherichia coli Proteins - genetics | Protein Conformation | Escherichia coli Proteins - chemistry | Amino Acid Substitution | Index Medicus | Bioenergetics
Journal Article
Nature (London), ISSN 1476-4687, 2011, Volume 477, Issue 7363, pp. 225 - 228
Journal Article
Proceedings of the National Academy of Sciences - PNAS, ISSN 1091-6490, 2019, Volume 116, Issue 7, pp. 2672 - 2680
Heart disease is the leading cause of death worldwide. A key pathogenic factor in the development of lethal heart failure is loss of terminally differentiated... 
Mitochondria | Iron | Heart injury | Ferroptos | Cell death | ferroptosis | cell death | mitochondria | MULTIDISCIPLINARY SCIENCES | HEART-FAILURE | ISCHEMIA | MECHANISMS | CELL-DEATH | NRF2 | ANTIOXIDANT | DISEASE | DOXORUBICIN CARDIOTOXICITY | iron | TRANSCRIPTION FACTOR | heart injury | Up-Regulation | Heme Oxygenase-1 - metabolism | Heme - metabolism | Mitochondria, Heart - metabolism | Mitochondria, Heart - enzymology | Cardiomyopathies - prevention & control | Mitochondria, Heart - drug effects | Iron - metabolism | Doxorubicin - toxicity | Mice, Knockout | Heme Oxygenase-1 - genetics | Animals | Reperfusion Injury - prevention & control | Myocytes, Cardiac - metabolism | NF-E2-Related Factor 2 - genetics | Mice | Lipid Peroxidation | Doxorubicin - pharmacology | Apoptosis | Cardiomyopathies - chemically induced | Prevention | Cardiomyopathy | Health aspects | Heart diseases | Animal models | Membranes | Razoxane | Lipid peroxidation | Lipids | Zinc protoporphyrin IX | Doxorubicin | Gene sequencing | Degradation | Antioxidants | FADD protein | Lipid membranes | Reperfusion | Protoporphyrin | Ischemia | Heme | Chelation | Damage | Peroxidation | Heart failure | Mortality | Heme oxygenase (decyclizing) | Cardiomyocytes | Ribonucleic acid--RNA | Coronary artery disease | Zinc | Oxygenase | Cardiovascular diseases | Protoporphyrin IX | Index Medicus | Biological Sciences | PNAS Plus
Journal Article