Regulation of erythropoiesis by hypoxia-inducible factors - Wikidata - thesis-toulmin - TriplyDB

Regulation of erythropoiesis by hypoxia-inducible factors

Regulation of erythropoiesis by hypoxia-inducible factors

http://www.wikidata.org/entity/Q37063716

about

The Role of the Multiple Hormonal Dysregulation in the Onset of "Anemia of Aging": Focus on Testosterone, IGF-1, and Thyroid Hormones Erythropoietin: powerful protection of ischemic and post-ischemic brain The Role of the PERK/eIF2α/ATF4/CHOP Signaling Pathway in Tumor Progression During Endoplasmic Reticulum Stress β-thalassemias: paradigmatic diseases for scientific discoveries and development of innovative therapies miR-190 Enhances HIF-Dependent Responses to Hypoxia in Drosophila by Inhibiting the Prolyl-4-hydroxylase Fatiga Testosterone induces erythrocytosis via increased erythropoietin and suppressed hepcidin: evidence for a new erythropoietin/hemoglobin set point.The physiological functions of iron regulatory proteins in iron homeostasis - an update.Hypoxia, HIF, and Associated Signaling Networks in Chronic Kidney Disease.β-Thalassemia and Polycythemia vera: targeting chronic stress erythropoiesis.Real-World Impact of Cardiovascular Disease and Anemia on Quality of Life and Productivity in Patients with Non-Dialysis-Dependent Chronic Kidney Disease.Tumor suppressor SPOP ubiquitinates and degrades EglN2 to compromise growth of prostate cancer cells HIF-prolyl hydroxylases as therapeutic targets in erythropoiesis and iron metabolism Intestinal inflammation modulates expression of the iron-regulating hormone hepcidin depending on erythropoietic activity and the commensal microbiota.AltitudeOmics: rapid hemoglobin mass alterations with early acclimatization to and de-acclimatization from 5260 m in healthy humans.The optimum hematocrit.Oncostatin M maintains the hematopoietic microenvironment in the bone marrow by modulating adipogenesis and osteogenesis.Convergence of hypoxia and TGFβ pathways on cell cycle regulation in human hematopoietic stem/progenitor cells.Epoetin zeta in the management of anemia associated with chronic kidney disease, differential pharmacology and clinical utility.Iron-hepcidin dysmetabolism, anemia and renal hypoxia, inflammation and fibrosis in the remnant kidney rat model.Duodenal cytochrome b (DCYTB) in iron metabolism: an update on function and regulation.Emerging EPO and EPO receptor regulators and signal transducers.Pharmacological HIF2α inhibition improves VHL disease-associated phenotypes in zebrafish model.Anaemia in kidney disease: harnessing hypoxia responses for therapy Lack of the Transcription Factor Hypoxia-Inducible Factor 1α (HIF-1α) in Macrophages Accelerates the Necrosis of Mycobacterium avium-Induced Granulomas.AG490 suppresses EPO-mediated activation of JAK2-STAT but enhances blood flow recovery in rats with critical limb ischemia.Effects of intravenous iron on fibroblast growth factor 23 (FGF23) in haemodialysis patients: a randomized controlled trial.Anti-VEGF therapy in the management of retinopathy of prematurity: what we learn from representative animal models of oxygen-induced retinopathy Conditional Deletion of Prolyl Hydroxylase Domain-Containing Protein 2 (Phd2) Gene Reveals Its Essential Role in Chondrocyte Function and Endochondral Bone Formation.Four-Week Studies of Oral Hypoxia-Inducible Factor-Prolyl Hydroxylase Inhibitor GSK1278863 for Treatment of Anemia Haemoglobin mass alterations in healthy humans following four-day head-down tilt bed rest The Local HIF-2α/EPO Pathway in the Bone Marrow is Associated with Excessive Erythrocytosis and the Increase in Bone Marrow Microvessel Density in Chronic Mountain Sickness.Retinal nerve fiber layer thickness and retinal vessel calibers in children with thalassemia minor.Out of balance--systemic iron homeostasis in iron-related disorders A knock-in mouse model of human PHD2 gene-associated erythrocytosis establishes a haploinsufficiency mechanism.Senp1 drives hypoxia-induced polycythemia via GATA1 and Bcl-xL in subjects with Monge's disease.Microvascular pericytes in healthy and diseased kidneys.Human Umbilical Cord Blood CD34-Positive Cells as Predictors of the Incidence and Short-Term Outcome of Neonatal Hypoxic-Ischemic Encephalopathy: A Pilot Study Emerging evidence of the physiological role of hypoxia in mammary development and lactation.Hypoxia-inducible factors link iron homeostasis and erythropoiesis.The Promotion of Erythropoiesis via the Regulation of Reactive Oxygen Species by Lactic Acid.

P2860

Q26771431-29A498C0-0633-4A10-ADED-D6FA41ED10F7 Q26999392-E1DCF41D-FA6E-4838-A913-1AC2F62AC977 Q28068986-DD4EBD8E-6FCC-44D1-98F9-D9E8FD586FD6 Q28086960-F3FF9331-4B61-4629-843A-E89655F4F1A4 Q28395196-A76066D5-9D1E-4C12-AD47-F96D65724C94 Q33615967-C2A79C8C-5966-47C6-960B-C7BE13C7BF46 Q33752116-86F546BB-0994-4725-A438-02D8D748CA9C Q33754900-56A0B21C-9084-4690-B73D-178F8AD8103B Q33853100-D6DBF799-2CDC-4292-96E7-3070F6606D6C Q33890794-B481F75F-58CA-4065-864F-457EADCABEA9 Q33906824-C57C53D5-C2AC-4FFA-8261-80BB0A8D8180 Q33926530-08BBE0AA-B4DC-46AD-A28A-E87C9CBB19FA Q33940769-D84A87A0-11C1-4C5E-9576-44446AFA92D9 Q34278320-90C4C783-E1D0-489A-862B-D0A54DF4AD73 Q34679370-B4659764-E50C-4C4B-BB93-D55DA663000D Q34796811-265E364A-B4D4-46C7-9DEA-2A1CEFB5EF09 Q35136050-C583BF7B-E0CE-4143-AFDD-B05CDE030114 Q35162053-3C041F76-CFDF-47B4-A8BE-E11D07B9A64C Q35388676-0F9082CC-A0C2-4D48-B16E-14F1EFF26038 Q35585864-68B63755-B925-43DC-ADA2-1D7A82C9AF44 Q35692391-3407B791-19AE-41E3-89FE-B008CB1FF1A4 Q35719850-35F7477E-26DC-4632-AE94-CE7214A668B6 Q35836904-6309801C-11FB-43D6-BBC1-FD3CE3C6CC9F Q35947464-24F1E2AC-23C4-4C60-945C-49D233F136BE Q36044491-C64D8BBB-8EFA-4C2B-8711-E4159B8511DC Q36194460-2B84D931-4A61-403B-A267-C05E9365EE6F Q36379513-29E318A8-DE93-4A9E-92AC-D4CCE95F5D35 Q36431785-3A041A87-2EEC-4A58-A66D-2A077CF9BD09 Q36746039-06D22D27-2BC6-409A-96BC-D160ED579375 Q36853220-37005FA5-B78F-4A79-844D-D69DBAAEDB65 Q36866696-85521B15-56F5-4BC6-89FF-55C5E8924E85 Q37151789-74DB0BC9-CCF1-4AE9-9645-6EB002A28909 Q37177398-C58CB4B7-9345-451B-A927-F5772B57B801 Q37333699-CA6C16C3-9BA2-4633-9836-3230CBA6A008 Q37415199-26263843-1E83-4892-8700-83F1A2E8A877 Q37509308-C99A2347-F406-4B8A-A53B-368289DB3B4F Q37591787-AF1A3E0A-3006-4EA5-9B93-7454C5248964 Q37593365-726798D1-58F0-47A8-AD2D-82B078152045 Q37620078-FB11449D-50B0-4195-820C-EB62192AAD43 Q37625714-C789BB72-061B-482C-A7F3-BA67F3DAE561

P2860

Regulation of erythropoiesis by hypoxia-inducible factors

http://www.wikidata.org/entity/Q37063716

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on 03 January 2013

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Regulation of erythropoiesis by hypoxia-inducible factors

@en

Regulation of erythropoiesis by hypoxia-inducible factors.

@nl

type

label

Regulation of erythropoiesis by hypoxia-inducible factors

@en

Regulation of erythropoiesis by hypoxia-inducible factors.

@nl

prefLabel

Regulation of erythropoiesis by hypoxia-inducible factors

@en

Regulation of erythropoiesis by hypoxia-inducible factors.

@nl

P1433

Q37063716-8290DF0F-BFA1-4550-BC34-6D9FDE00AAA1

P1476

Q37063716-CDE769EF-6725-478F-AE17-111B2095FB89

P2093

Q37063716-10EFD519-89D6-44F5-851E-0CCB5C4D8320

P2860

Q37063716-0078F280-F6A6-42AF-8BFB-145520475002

Q37063716-01FB5BA9-8115-4DF3-AA91-5AA62E9E64D5

Q37063716-028F0075-A03A-465F-83EF-3A20B68DF948

Q37063716-03BBACFE-E383-4666-9D45-6279BE0660F3

Q37063716-03DF47D4-6721-4FBF-A2C5-EF5FB1D1220D

Q37063716-03F5B6E3-B67E-4ECD-9D33-50C04F37CD0E

Q37063716-04351507-9BB2-4424-B994-AA03E7029980

Q37063716-062387E3-65E0-4011-9075-96E431A8C1CC

Q37063716-06F0CB58-D4D4-4A19-9347-2E26F77E26B0

Q37063716-09A00FF3-206E-4782-AAF3-C124F0B58734

P304

Q37063716-28032433-A5EB-484E-97F3-627496010E62

P31

Q37063716-8FFFB31A-827E-42F8-AA6E-93DCB0C4EC40

P356

Q37063716-51901ED3-AEEB-4C1E-839C-74A3AF9AA500

P433

Q37063716-EBB058ED-4E82-496A-96B2-A7B86C8136D9

P478

Q37063716-4F474485-ACB3-4DB0-A704-F9611705E289

P577

Q37063716-2735972B-27CD-447E-B21F-1A8F16BC7C5D

P5875

Q37063716-0706D318-0E9C-4B63-A41C-E1A58CCBF0C0

P698

Q37063716-1008D2D3-787D-4A8B-94DE-56215322EE76

P921

Q37063716-89F6D87A-0546-4375-9553-67A90518602A

P932

Q37063716-BEB9430E-C6BF-4B56-8F92-CF04BE393889

P356

J.BLRE.2012.12.003

P1433

P1476

Regulation of erythropoiesis by hypoxia-inducible factors

@en

P2093

Volker H Haase

http://www.w3.org/2001/XMLSchema#string

P2860

Identifying signatures of natural selection in Tibetan and Andean populations using dense genome scan data

Structure of the VHL-ElonginC-ElonginB complex: implications for VHL tumor suppressor function

The tumour suppressor protein VHL targets hypoxia-inducible factors for oxygen-dependent proteolysis

Role of hypoxia-inducible factor-1 in transcriptional activation of ceruloplasmin by iron deficiency

HIFalpha targeted for VHL-mediated destruction by proline hydroxylation: implications for O2 sensing

C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation

A conserved family of prolyl-4-hydroxylases that modify HIF

A nuclear factor induced by hypoxia via de novo protein synthesis binds to the human erythropoietin gene enhancer at a site required for transcriptional activation

Calorie restriction promotes mammalian cell survival by inducing the SIRT1 deacetylase

Furin-mediated release of soluble hemojuvelin: a new link between hypoxia and iron homeostasis

P304

41-53

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1016/J.BLRE.2012.12.003

http://www.w3.org/2001/XMLSchema#string

P433

1

http://www.w3.org/2001/XMLSchema#string

P478

27

http://www.w3.org/2001/XMLSchema#string

P577

2013-01-03T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

234067202

http://www.w3.org/2001/XMLSchema#string

P698

23291219

http://www.w3.org/2001/XMLSchema#string

P921

P932

3731139

http://www.w3.org/2001/XMLSchema#string