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1. Full Text Hepcidin and disorders of iron metabolism
by Ganz, Tomas and Nemeth, Elizabeta
Annual review of medicine, ISSN 0066-4219, 02/2011, Volume 62, Issue 1, pp. 347 - 360
iron overload | inflammation | anemia | Neoplasms - metabolism | Antimicrobial Cationic Peptides - antagonists & inhibitors | Antimicrobial Cationic Peptides - agonists | Humans | Iron Metabolism Disorders - drug therapy | Male | Hepatocytes - metabolism | Antimicrobial Cationic Peptides - metabolism | Iron - metabolism | Iron, Dietary - metabolism | Anemia - metabolism | Inflammation - metabolism | Animals | Cation Transport Proteins - metabolism | Hepcidins | Iron Metabolism Disorders - metabolism | Female | Mice | Transferrin - metabolism | Interleukin-6 - metabolism | Aging - metabolism | Kidney Diseases - metabolism | Care and treatment | Anemia | Physiological aspects | Metabolic diseases | Iron in the body | Diagnosis | Peptide hormones | Pathology | Iron | Hormones | Peptides | Liver | Index Medicus
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2. Full Text Depletion of stromal cells expressing fibroblast activation protein-α from skeletal muscle and bone marrow results in cachexia and anemia
by Roberts, Edward W and Deonarine, Andrew and Jones, James O and Denton, Alice E and Feig, Christine and Lyons, Scott K and Espeli, Marion and Kraman, Matthew and McKenna, Brendan and Wells, Richard J.B and Zhao, Qi and Caballero, Otavia L and Larder, Rachel and Coll, Anthony P and O'Rahilly, Stephen and Brindle, Kevin M and Teichmann, Sarah A and Tuveson, David A and Fearon, Douglas T
The Journal of experimental medicine, ISSN 0022-1007, 06/2013, Volume 210, Issue 6, pp. 1137 - 1151
Immunology | Life Sciences & Biomedicine | Medicine, Research & Experimental | Science & Technology | Research & Experimental Medicine | Neoplasms - metabolism | Follistatin - genetics | Lymphopoiesis - genetics | Follistatin - metabolism | Anemia - pathology | Muscle, Skeletal - metabolism | Mice, Transgenic - metabolism | Muscle, Skeletal - cytology | Adipose Tissue - metabolism | Anemia - genetics | Chemokine CXCL12 - genetics | Neoplasms - genetics | Bone Marrow - metabolism | Gelatinases - metabolism | Serine Endopeptidases - genetics | Membrane Proteins - metabolism | Cachexia - metabolism | Cell Lineage - genetics | Erythropoiesis - genetics | Muscular Disorders, Atrophic - metabolism | Cachexia - genetics | Membrane Proteins - genetics | Mice, Inbred C57BL | Stromal Cells - metabolism | Mice, Transgenic - genetics | Muscular Disorders, Atrophic - genetics | Hematopoiesis - genetics | Transcriptome - genetics | Pancreas - metabolism | Anemia - metabolism | Animals | Chemokine CXCL12 - metabolism | Gelatinases - genetics | Cachexia - pathology | Mice | Serine Endopeptidases - metabolism | Stromal Cells - cytology | Index Medicus | 307
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3. Full Text Heme regulates gene expression by triggering Crm1-dependent nuclear export of Bach1
by Sun, Jiying and Yoshida, Minoru and Igarashi, Kazuhiko and Hira, Shusuke and Tashiro, Satoshi and Suzuki, Hiroshi and Yamazaki, Chikara and Zenke, Yukari and Ikeda-Saito, Masao
The EMBO journal, ISSN 0261-4189, 07/2004, Volume 23, Issue 13, pp. 2544 - 2553
heme oxygenase | Maf | globin | heme | oxidative stress | Globin | Oxidative stress | Heme | Heme oxygenase | Biochemistry & Molecular Biology | Life Sciences & Biomedicine | Science & Technology | Cell Biology | Immunohistochemistry | Heme - metabolism | Transcription Factors - chemistry | Humans | Leucine Zippers | Molecular Sequence Data | Globins - metabolism | Recombinant Fusion Proteins - metabolism | DNA-Binding Proteins - metabolism | Cell Nucleus - metabolism | Chromatin Immunoprecipitation | Heme Oxygenase-1 | Transcription, Genetic | Active Transport, Cell Nucleus | Hemin - pharmacology | Heme Oxygenase (Decyclizing) - metabolism | Dimerization | Heme Oxygenase (Decyclizing) - genetics | Genes, Reporter | Repressor Proteins - metabolism | Fibroblasts - metabolism | Amino Acid Sequence | Cell Line | Green Fluorescent Proteins - metabolism | Zinc Fingers | Gene Expression Regulation | Glutathione Transferase - metabolism | Alanine - metabolism | Nuclear Proteins - metabolism | Recombinant Fusion Proteins - chemistry | Transcription Factors - genetics | Fanconi Anemia Complementation Group Proteins | Amino Acid Motifs | MafK Transcription Factor | Membrane Proteins | Transcription Factors - metabolism | Karyopherins - metabolism | Escherichia coli - genetics | Plasmids | Fibroblasts - drug effects | Erythroid-Specific DNA-Binding Factors | Spectrophotometry | Basic-Leucine Zipper Transcription Factors | Amino Acid Substitution | Receptors, Cytoplasmic and Nuclear - metabolism | Index Medicus
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4. Full Text On-demand erythrocyte disposal and iron recycling requires transient macrophages in the liver
by Theurl, Igor and Hilgendorf, Ingo and Nairz, Manfred and Tymoszuk, Piotr and Haschka, David and Asshoff, Malte and He, Shun and Gerhardt, Louisa M. S and Holderried, Tobias A. W and Seifert, Markus and Sopper, Sieghart and Fenn, Ashley M and Anzai, Atsushi and Rattik, Sara and McAlpine, Cameron and Theurl, Milan and Wieghofer, Peter and Iwamoto, Yoshiko and Weber, Georg F and Harder, Nina K and Chousterman, Benjamin G and Arvedson, Tara L and McKee, Mary and Wang, Fudi and Lutz, Oliver M. D and Rezoagli, Emanuele and Babitt, Jodie L and Berra, Lorenzo and Prinz, Marco and Nahrendorf, Matthias and Weiss, Guenter and Weissleder, Ralph and Lin, Herbert Y and Swirski, Filip K
Nature medicine, ISSN 1078-8956, 08/2016, Volume 22, Issue 8, pp. 945 - 951
Biochemistry & Molecular Biology | Life Sciences & Biomedicine | Medicine, Research & Experimental | Science & Technology | Cell Biology | Research & Experimental Medicine | Anemia, Sickle Cell | Granulocyte-Macrophage Colony-Stimulating Factor - metabolism | Monocytes - cytology | Monocytes - metabolism | Hepatocytes - metabolism | Cation Transport Proteins - metabolism | Antigens, Ly - metabolism | Erythrocytes - cytology | Cell Differentiation | Kupffer Cells - metabolism | Membrane Proteins - metabolism | Disease Models, Animal | Spleen | Kupffer Cells - cytology | Anemia | Liver - metabolism | Inflammation | Macrophage Colony-Stimulating Factor - metabolism | Anemia, Hemolytic | Macrophages - cytology | Iron - metabolism | Macrophages - metabolism | Animals | NF-E2-Related Factor 2 - metabolism | Erythrocytes - metabolism | Mice | Biological research | Nutrient interactions | Biological transport | Erythrocytes | Physiological aspects | Research | Biology, Experimental | Proteins | Oxygen | Iron | Liver | Index Medicus
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5. Full Text Mechanism of Ubiquitination and Deubiquitination in the Fanconi Anemia Pathway
by van Twest, Sylvie and Murphy, Vincent J and Hodson, Charlotte and Tan, Winnie and Swuec, Paolo and O’Rourke, Julienne J and Heierhorst, Jörg and Crismani, Wayne and Deans, Andrew J
Molecular cell, ISSN 1097-2765, 01/2017, Volume 65, Issue 2, pp. 247 - 259
core complex | RING E3 | Fanconi anemia | FANCD2 | deubiquitination | FANCB | enzyme mechanism | monoubiquitination | DNA repair | Biochemistry & Molecular Biology | Life Sciences & Biomedicine | Science & Technology | Cell Biology | Fanconi Anemia Complementation Group D2 Protein - genetics | Fanconi Anemia - metabolism | Humans | Multiprotein Complexes | Protein Multimerization | Substrate Specificity | Fanconi Anemia Complementation Group A Protein - metabolism | DNA-Binding Proteins - metabolism | Fanconi Anemia Complementation Group Proteins - metabolism | Ubiquitination | Transfection | Time Factors | Fanconi Anemia - genetics | Ubiquitin-Specific Proteases - metabolism | Recombinant Proteins - metabolism | Cell Line | Fanconi Anemia Complementation Group Proteins - genetics | Nuclear Proteins - metabolism | Fanconi Anemia Complementation Group G Protein - metabolism | DNA - metabolism | Inhibitor of Differentiation Protein 2 - metabolism | DNA - genetics | Fanconi Anemia Complementation Group C Protein - metabolism | Fanconi Anemia Complementation Group D2 Protein - metabolism | Protein Binding | Fanconi Anemia Complementation Group L Protein - metabolism | Fanconi Anemia Complementation Group E Protein - metabolism | Ubiquitin | Chemotherapy | Ligases | Genomics | Research institutes | Cancer | Fanconi's anemia | Proteins | Medical research | Molecular genetics | Medicine, Experimental | Index Medicus
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6. Full Text Bach1 differentially regulates distinct Nrf2-dependent genes in human venous and coronary artery endothelial cells adapted to physiological oxygen levels
by Chapple, Sarah J and Keeley, Thomas P and Mastronicola, Daniela and Arno, Matthew and Vizcay-Barrena, Gema and Fleck, Roland and Siow, Richard C.M and Mann, Giovanni E
Free radical biology & medicine, ISSN 0891-5849, 03/2016, Volume 92, pp. 152 - 162
NQO1 | Bach1 | Solute Carrier Family 7-anionic amino acid transporter light chain xCT | Coronary artery | HO-1 | Redox signaling | Endothelial cells | Normoxia | GCL | Physiological oxygen tension | Mitochondria | Nuclear Factor-E2-Related Factor 2, Nrf2 | Glutathione reductase GR | Thioredoxin reductase-1 | Sequestosome-1 | Glutathione | Physiologicaloxygentension | NuclearFactor-E2-RelatedFactor2,Nrf2 | Redoxsignaling | transporterlightchainxCT | Solute CarrierFamily7-anionicaminoacid | Thioredoxinreductase-1 | Biochemistry & Molecular Biology | Endocrinology & Metabolism | Life Sciences & Biomedicine | Science & Technology | Heme Oxygenase-1 - metabolism | Basic-Leucine Zipper Transcription Factors - metabolism | Reactive Oxygen Species - metabolism | Glutathione - metabolism | Antioxidants - metabolism | Humans | NAD(P)H Dehydrogenase (Quinone) - genetics | Oxygen - metabolism | Coronary Vessels - metabolism | DNA-Binding Proteins - metabolism | Kelch-Like ECH-Associated Protein 1 - genetics | Heme Oxygenase-1 - genetics | Fanconi Anemia Complementation Group Proteins - metabolism | Amino Acid Transport System y+ - metabolism | Hypoxia-Inducible Factor 1, alpha Subunit - metabolism | NF-E2-Related Factor 2 - genetics | Glutamate-Cysteine Ligase - metabolism | Endothelial Cells - metabolism | Hypoxia-Inducible Factor 1, alpha Subunit - genetics | Fanconi Anemia Complementation Group Proteins - genetics | Kelch-Like ECH-Associated Protein 1 - metabolism | Basic-Leucine Zipper Transcription Factors - genetics | DNA-Binding Proteins - genetics | Veins - metabolism | NF-E2-Related Factor 2 - metabolism | NAD(P)H Dehydrogenase (Quinone) - metabolism | Genetic research | Physiological aspects | Genes | Endothelium | Surface active agents | RNA | Amino acids | DNA binding proteins | Index Medicus
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7. Full Text Identification of erythroferrone as an erythroid regulator of iron metabolism
by Kautz, Léon and Jung, Grace and Valore, Erika V and Rivella, Stefano and Nemeth, Elizabeta and Ganz, Tomas
Nature genetics, ISSN 1061-4036, 2014, Volume 46, Issue 7, pp. 678 - 684
Life Sciences & Biomedicine | Genetics & Heredity | Science & Technology | Hepcidins - metabolism | beta-Thalassemia - pathology | Liver - pathology | Iron Overload - drug therapy | Molecular Sequence Data | Erythropoiesis - drug effects | Male | Gene Expression Profiling | Iron Overload - pathology | Iron Overload - metabolism | Epoetin Alfa | Erythropoietin - metabolism | Real-Time Polymerase Chain Reaction | Anemia - etiology | Disease Models, Animal | Recombinant Proteins - metabolism | Hormones - pharmacology | Enzyme-Linked Immunosorbent Assay | Liver - metabolism | Mice, Inbred C57BL | RNA, Messenger - genetics | Hemorrhage - complications | Hemoglobins - metabolism | Hemorrhage - metabolism | Reverse Transcriptase Polymerase Chain Reaction | Iron - metabolism | Blotting, Western | Erythropoiesis - physiology | Mice, Knockout | Anemia - metabolism | Animals | Mice | beta-Thalassemia - metabolism | Physiological aspects | Genetic research | Genetic aspects | Iron in the body | Hormones | Research | Genetic regulation | Identification and classification | Flow cytometry | Plasma | Phosphorylation | Bone marrow | Homeostasis | Iron | Grants | Metabolism | Gene expression | Experiments | Hemorrhage | Index Medicus
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8. Full Text Leukaemogenesis induced by an activating β-catenin mutation in osteoblasts
by Kode, Aruna and Manavalan, John and Mosialou, Ioanna and Bhagat, Govind and Rathinam, Chozha and Luo, Nan and Khiabanian, Hossein and Lee, Albert and Murty, Vundavalli and Friedman, Richard and Brum-Oome, Anea and Park, David and Galili, Naomi and mukherjee, Siddhartha and Teruya-Feldstein, Julie and Raza, Azra and Rabadan, Raul and Berman, Ellin and Kousteni, Stavroula
Nature (London), ISSN 0028-0836, 01/2014, Volume 506, Issue 7487, pp. 240 - 244
Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | Osteoblasts - secretion | Receptors, Notch - metabolism | Humans | Leukemia, Myeloid, Acute - metabolism | Hematopoietic Stem Cells - pathology | Anemia - pathology | Male | Cell Differentiation - genetics | Intercellular Signaling Peptides and Proteins - metabolism | Membrane Proteins - deficiency | Anemia - genetics | Cell Nucleus - metabolism | Tumor Microenvironment - genetics | Cell Transformation, Neoplastic - genetics | Serrate-Jagged Proteins | Base Sequence | Female | Membrane Proteins - metabolism | Intercellular Signaling Peptides and Proteins - deficiency | Jagged-1 Protein | Calcium-Binding Proteins - metabolism | Myelodysplastic Syndromes - metabolism | Signal Transduction | Leukemia, Myeloid, Acute - pathology | Membrane Proteins - genetics | Intercellular Signaling Peptides and Proteins - genetics | Calcium-Binding Proteins - deficiency | Hematopoietic Stem Cells - metabolism | Mutation - genetics | beta Catenin - metabolism | beta Catenin - genetics | Anemia - metabolism | Cell Lineage | Osteoblasts - pathology | Animals | Chromosome Aberrations | Myeloid Cells - metabolism | Ligands | Mice | Myelodysplastic Syndromes - genetics | Myeloid Cells - pathology | Cell Transformation, Neoplastic - pathology | Myelodysplastic Syndromes - pathology | Osteoblasts - metabolism | Calcium-Binding Proteins - genetics | Leukemia, Myeloid, Acute - genetics | Index Medicus
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