Regulation of the histone demethylase JMJD1A by hypoxia-inducible factor 1 alpha enhances hypoxic gene expression and tumor growth. - Wikidata - wikimedia - TriplyDB

Regulation of the histone demethylase JMJD1A by hypoxia-inducible factor 1 alpha enhances hypoxic gene expression and tumor growth.

Regulation of the histone demethylase JMJD1A by hypoxia-inducible factor 1 alpha enhances hypoxic gene expression and tumor growth.

http://www.wikidata.org/entity/Q33558169

about

Human AlkB homologue 5 is a nuclear 2-oxoglutarate dependent oxygenase and a direct target of hypoxia-inducible factor 1α (HIF-1α)Hypoxia upregulates PGI-synthase and increases PGI₂ release in human vascular cells exposed to inflammatory stimuli MiR-210--micromanager of the hypoxia pathway State of the science: an update on renal cell carcinoma Hypoxia-Inducible Histone Lysine Demethylases: Impact on the Aging Process and Age-Related Diseases Targeting Protein-Protein Interactions in the HIF System Hypoxia and Hypoxia-Inducible Factors in Leukemias The Role of Oxygen Sensors, Hydroxylases, and HIF in Cardiac Function and Disease Epigenetic Therapy for Solid Tumors: Highlighting the Impact of Tumor Hypoxia Epigenetic Regulation of Carotid Body Oxygen Sensing: Clinical Implications The control of histone methylation and gene expression by oxidative stress, hypoxia, and metals Epigenetic regulation by histone demethylases in hypoxia HIF1α and HIF2α: sibling rivalry in hypoxic tumour growth and progression Histone deacetylase inhibitors and epigenetic modifications as a novel strategy in renal cell carcinoma Structural and Evolutionary Basis for the Dual Substrate Selectivity of Human KDM4 Histone Demethylase Family Hypoxia-inducing factors as master regulators of stemness properties and altered metabolism of cancer- and metastasis-initiating cells Jumonji domain-containing protein 6 (Jmjd6) is required for angiogenic sprouting and regulates splicing of VEGF-receptor 1 HIF-KDM3A-MMP12 regulatory circuit ensures trophoblast plasticity and placental adaptations to hypoxia.KDM4B/JMJD2B is a p53 target gene that modulates the amplitude of p53 response after DNA damage.Buckley-James boosting for survival analysis with high-dimensional biomarker data.The histone demethylase KDM4B regulates peritoneal seeding of ovarian cancer.The histone demethylase JMJD1A induces cell migration and invasion by up-regulating the expression of the long noncoding RNA MALAT1 Adrenomedullin as a therapeutic target in angiogenesis.Epigenetics and the environment: in search of the "toleroasome" vital to execution of ischemic preconditioning.Hypoxia and regulation of cancer cell stemness.The histone demethylase KDM3A regulates the transcriptional program of the androgen receptor in prostate cancer cells.Time-series clustering of gene expression in irradiated and bystander fibroblasts: an application of FBPA clustering.Upregulation of MiR-155 in nasopharyngeal carcinoma is partly driven by LMP1 and LMP2A and downregulates a negative prognostic marker JMJD1A.Growth differentiation factor 15 in erythroid health and disease.Divergent molecular mechanisms underlying the pleiotropic functions of macrophage inhibitory cytokine-1 in cancer Chromatin and oxygen sensing in the context of JmjC histone demethylases Direct regulation of GAS6/AXL signaling by HIF promotes renal metastasis through SRC and MET.The hypoxia-inducible epigenetic regulators Jmjd1a and G9a provide a mechanistic link between angiogenesis and tumor growth.Expression and significance of histone H3K27 demethylases in renal cell carcinoma.DNA methylation, isocitrate dehydrogenase mutation, and survival in glioma VHL loss in renal cell carcinoma leads to up-regulation of CUB domain-containing protein 1 to stimulate PKC{delta}-driven migration Epigenetic programming of hypoxic-ischemic encephalopathy in response to fetal hypoxia.The histone demethylase enzyme KDM3A is a key estrogen receptor regulator in breast cancer.Acidic stress promotes a glioma stem cell phenotype.Growth differentiation factor 15: a prognostic marker for recurrence in colorectal cancer

P2860

Q24338321-5EC3B151-4E4E-4F17-ACCD-806BF7DBE618 Q24339277-D22B7F74-BD63-4579-BCC5-9DECA79E121E Q24628401-B6A370B6-C272-455C-AED6-99DA5E530E83 Q24630685-AF7C4034-A206-4FB2-B6F3-BB71211D60F6 Q26750099-73260622-7310-4FE7-8681-91653F1A58CC Q26753176-D64EFA3C-1A94-48F6-9D7B-BCD5297186B5 Q26767167-A1EBB1CB-1F2A-415C-A241-072C7240FACE Q26780548-1C9BB596-75A4-4079-8807-D71BB57850CC Q26783014-D6E23151-5EEA-4594-AAA0-74402DBDD2EB Q26798010-C99B4D08-7D92-4C77-AB7A-0AAFDCB9950B Q26824372-2E681DE0-B5F1-4AE2-9BD0-F9E8A7BC06FC Q26825704-0F0C0386-F758-48B8-8AC1-37083A36B3A0 Q27025886-1A300C48-DD3B-46CD-A03B-3D0495369F59 Q27025984-1B2A7488-4B67-42AC-9DAD-492E308926FE Q27673793-5EFBD174-B3C8-4FFA-9866-85A7307A1E7B Q28393898-18C285F3-07D5-446A-B987-5ED15E2B4E58 Q28507470-EC7A04D9-FAFA-4A37-B494-0E6801ACFDF0 Q31812581-2FB715A5-7A54-425B-ADAF-2E9B9EE7AC03 Q33580494-D36E0126-C32B-40FB-9822-C5322079E02C Q33624066-DBFF9462-5079-45B2-9D01-F74E7F86F06D Q33638726-B84B3491-76FD-4190-811F-71B67EA5049D Q33688385-09AAA521-7071-4789-94D4-73E0DB956597 Q33693793-D04792A3-D120-446D-9362-1C448B1CEB69 Q33693885-FDDD24FC-DB07-49DA-B695-A2C55F20A88E Q33705149-42B4CA04-3A80-423E-BEFE-F9A4D9690CE3 Q33728316-A0620301-F906-4828-B6C5-716F3293B80E Q33785409-5D7BD7E7-5EC0-4645-A50E-D7E8652D1402 Q33889404-76DFB403-CF6A-4DEA-9F10-B449D808073A Q33908936-44FB3B9D-E2F4-4E20-84C5-D5A550AC2C98 Q34099900-8C365932-EC53-45E3-A9A0-F578B7FC5E74 Q34103385-A175D38B-361D-41A2-AB98-13BA67D29B33 Q34217927-04CCDA1C-222F-4924-87BC-C1D0A6AEA6FC Q34298049-D85BDBB8-F2E0-40D2-AEE2-970890035963 Q34443684-45CDC615-9528-4F07-9AD0-A1DF25CF8F1D Q34498783-F4F77555-58A6-432C-A246-3F48CFCEE48E Q34549885-6D2D45E7-1479-43F0-9FF7-B418688D2549 Q34747263-7568F914-F34F-44AC-BAF3-8004139C54B7 Q34883436-B1B04B12-AF1B-40C0-AA8A-0402496F37B2 Q34985109-D75CDCFA-A378-42AE-980D-B73B2B8D7534 Q35006757-111C31E8-0CAE-4B1F-841C-4802ABEEC7FB

P2860

Regulation of the histone demethylase JMJD1A by hypoxia-inducible factor 1 alpha enhances hypoxic gene expression and tumor growth.

http://www.wikidata.org/entity/Q33558169

description

2010 nî lūn-bûn

@nan

2010 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի հունվարին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

name

Regulation of the histone deme ...... e expression and tumor growth.

@ast

Regulation of the histone deme ...... e expression and tumor growth.

@en

Regulation of the histone deme ...... e expression and tumor growth.

@nl

type

label

Regulation of the histone deme ...... e expression and tumor growth.

@ast

Regulation of the histone deme ...... e expression and tumor growth.

@en

Regulation of the histone deme ...... e expression and tumor growth.

@nl

prefLabel

Regulation of the histone deme ...... e expression and tumor growth.

@ast

Regulation of the histone deme ...... e expression and tumor growth.

@en

Regulation of the histone deme ...... e expression and tumor growth.

@nl

P1433

Q33558169-85BF8C49-213C-44FF-A1B5-0A967B922EB4

P1476

Q33558169-B60C2631-8BFA-400A-8BD6-CD7BB1B728B2

P2093

Q33558169-3AF26B39-8323-4C26-9712-91B276448730

Q33558169-759679FA-D24B-4F3B-B95B-207AFE0FA9A3

Q33558169-94BCE2E2-1F39-4565-BE7E-A05C26721186

Q33558169-9D75DCD4-888C-400D-9E4C-00C220F24177

P2860

Q33558169-0413E426-2E99-49E8-A659-7DF76EC627FF

Q33558169-048E99AF-3752-4502-8AB5-EB5BE29F135A

Q33558169-09D6650D-4CFE-4783-A56F-E40F177E8865

Q33558169-0C98DB9C-9436-4A48-99E2-C56E98548371

Q33558169-0E2BB29D-BD63-4191-BE20-B9C2C8B7658A

Q33558169-1B3755F3-2123-46BC-918D-B9868CE7E5A0

Q33558169-21009470-4D5B-464B-B2B9-9B719F6DBE96

Q33558169-246CFEF1-3BEE-49FB-AA88-0E760A7EBCD5

Q33558169-25B46EA1-5DAA-43BD-97AC-D7857A14E683

Q33558169-277EE5A2-A021-4D2C-A8F6-A91669E00A4D

P304

Q33558169-550C6541-CAF6-46BB-88FE-7D7C3876A64A

P31

Q33558169-390888A0-DA7E-4488-AAC5-1F4894030E05

P356

Q33558169-A888A9CA-03A6-41E2-967D-90E0CD4DF3F1

P407

Q33558169-852D486A-62B0-493C-8FB6-F68ACED426C5

P433

Q33558169-8CB7464C-74A2-472D-A841-E4541406B696

P478

Q33558169-368C4CE1-4B79-4193-AA4E-B4D87C159154

P50

Q33558169-5097A5C4-9A0F-4126-B9AD-BA8F95665774

Q33558169-F24100AF-FC2B-4E57-9A23-861F6CE66E87

P577

Q33558169-B4F2B3F3-5B83-48C0-BEC0-1BF460A92872

P5875

Q33558169-B7B9F5E6-B996-497E-A24A-039BF2DD804D

P698

Q33558169-E93E6DF2-90B9-4972-B3B2-D025D4474794

P921

Q33558169-3276D723-18A1-427A-8FFA-DCBE3DB6A3D1

P932

Q33558169-12356EF6-CB79-4FB5-A45B-1633A966381A

P356

P1433

Molecular and Cellular Biology

P1476

Regulation of the histone deme ...... e expression and tumor growth.

@en

P2093

Amato J Giaccia

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

Denise Chan

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

Olga Razorenova

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

Sully Fernandez

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

P2860

Transcription factors bind thousands of active and inactive regions in the Drosophila blastoderm

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

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

Hypoxia-inducible factor 1 is a basic-helix-loop-helix-PAS heterodimer regulated by cellular O2 tension

JHDM2A, a JmjC-containing H3K9 demethylase, facilitates transcription activation by androgen receptor

Reversal of histone lysine trimethylation by the JMJD2 family of histone demethylases

Activation of vascular endothelial growth factor gene transcription by hypoxia-inducible factor 1

Redox-regulated recruitment of the transcriptional coactivators CREB-binding protein and SRC-1 to hypoxia-inducible factor 1alpha

Significance analysis of microarrays applied to the ionizing radiation response

Targeting of HIF-alpha to the von Hippel-Lindau ubiquitylation complex by O2-regulated prolyl hydroxylation

P304

344-353

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

P31

scholarly article

P356

10.1128/MCB.00444-09

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

P407

P433

1

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

P478

30

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

P50

Erinn B. Rankin

P577

2010-01-01T00:00:00Z

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

P5875

38037617

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

P698

19858293

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

P921

P932

2798291

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