Inhibition of succinate dehydrogenase dysregulates histone modification in mammalian cells. - Wikidata - wikimedia - TriplyDB

Inhibition of succinate dehydrogenase dysregulates histone modification in mammalian cells.

Inhibition of succinate dehydrogenase dysregulates histone modification in mammalian cells.

http://www.wikidata.org/entity/Q39784567

about

SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways Succinate Dehydrogenase Loss in Familial Paraganglioma: Biochemistry, Genetics, and Epigenetics Regulation of SOD2 in cancer by histone modifications and CpG methylation: closing the loop between redox biology and epigenetics Genetically-defined metabolic reprogramming in cancer RhNRG-1β Protects the Myocardium against Irradiation-Induced Damage via the ErbB2-ERK-SIRT1 Signaling Pathway Defects in mitochondrial metabolism and cancer The mitochondrial side of epigenetics Current views on cell metabolism in SDHx-related pheochromocytoma and paraganglioma Molecular Subtypes of KIT/PDGFRA Wild-Type Gastrointestinal Stromal Tumors: A Report From the National Institutes of Health Gastrointestinal Stromal Tumor Clinic.Succinate dehydrogenase mutation underlies global epigenomic divergence in gastrointestinal stromal tumor 2-Oxoglutarate-dependent dioxygenases are sensors of energy metabolism, oxygen availability, and iron homeostasis: potential role in the regulation of aging process.The redox basis of epigenetic modifications: from mechanisms to functional consequences.A novel microscopy-based high-throughput screening method to identify proteins that regulate global histone modification levels.Succinate dehydrogenase inhibition leads to epithelial-mesenchymal transition and reprogrammed carbon metabolism.Hypoxia-inducible factor directs POMC gene to mediate hypothalamic glucose sensing and energy balance regulation Chronic alcoholism-mediated metabolic disorders in albino rat testes.Structural basis for malfunction in complex II.A metabolic signature for long life in the Caenorhabditis elegans Mit mutants.Acquired hypermethylation of the P16INK4A promoter in abdominal paraganglioma: relation to adverse tumor phenotype and predisposing mutation.Functional characterization of nonmetastatic paraganglioma and pheochromocytoma by (18) F-FDOPA PET: focus on missed lesions.Single-molecule analysis of combinatorial epigenomic states in normal and tumor cells.Succinate dehydrogenase (SDHx) mutations in pituitary tumors: could this be a new role for mitochondrial complex II and/or Krebs cycle defects?Autophagy: resetting glutamine-dependent metabolism and oxygen consumption.Influence of metabolism on epigenetics and disease.Role of hypoxia and HIF2α in development of the sympathoadrenal cell lineage and chromaffin cell tumors with distinct catecholamine phenotypic features.Metabolism and epigenetics.Mitochondrial control through nutritionally regulated global histone H3 lysine-4 demethylation.Alpha-Ketoglutarate as a Molecule with Pleiotropic Activity: Well-Known and Novel Possibilities of Therapeutic Use Inborn and acquired metabolic defects in cancer.Cancer and altered metabolism: potential importance of hypoxia-inducible factor and 2-oxoglutarate-dependent dioxygenases From transcriptional profiling to tumor biology in pheochromocytoma and paraganglioma.Paediatric and adult malignant glioma: close relatives or distant cousins?Sensing cellular states--signaling to chromatin pathways targeting Polycomb and Trithorax group function.Oncometabolites-driven tumorigenesis: From genetics to targeted therapy.Genetically modeled mice with mutations in mitochondrial metabolic enzymes for the study of cancer Metabolic regulation of histone post-translational modifications.Exploring the emerging complexity in transcriptional regulation of energy homeostasis.Inactivation of SDH and FH cause loss of 5hmC and increased H3K9me3 in paraganglioma/pheochromocytoma and smooth muscle tumors.Oncometabolic mutation IDH1 R132H confers a metformin-hypersensitive phenotype.Molecular Pathogenesis and Diagnostic, Prognostic and Predictive Molecular Markers in Sarcoma.

P2860

Q24296915-713D1E65-9E68-45FE-BE46-8FB9EEFDBF0D Q26796203-3CECBD74-7032-47C2-A823-E7E4634A2ACB Q27001050-78BEEAD1-98CB-4C3A-86E3-489A3D585E53 Q27004739-9ED4C7E5-3180-4621-A236-C8D4D37D9BBD Q27319491-658B3D7E-221D-453B-8C73-58BFEB2FC33B Q27694117-436F70ED-A567-49D3-A1BC-71D3D5FBF259 Q28081686-E80A82DB-D06C-4D31-B311-A8A28B2608B0 Q33590969-4898F5D7-1C60-4599-8241-283815F4491B Q33802730-28E5D549-7E91-4AED-A6C4-D05F295FA4FE Q34055567-91E28502-EE36-41BE-9486-353D55F55A38 Q34482634-33EBDACC-493B-4BDF-BE1F-21136488EE6B Q35055739-2D054D1B-9F10-4FD4-9BA3-C5ED54052E1D Q35066149-38FB851E-A693-49D8-89E7-669ACBB19DB4 Q35067274-48668400-6239-4B92-AD6F-1A3CF6DC6287 Q35129455-9C64E264-816A-477B-8C85-3497655F3E14 Q35614002-CFF8B6AB-E629-4AB6-9119-0D5591A7114A Q36318828-D5D8E906-D551-4297-BE47-CFAD5C604A2F Q36553737-B2E97831-8B0F-402B-8311-A07AB37A33BE Q36613916-7FFAC5CA-F579-487D-B8EF-BE6B89EB7B06 Q36724520-C66CCB93-80A5-4212-89A0-C4C0FE1AF1BA Q36835792-3C7C6DB4-CE79-4F5F-91D6-DE6DC2C3A91B Q36865610-7A5AF8FD-B3A6-4EFB-9C5E-D72E51AFBAF3 Q36920096-B65D0851-127F-441C-AE0F-3D4E82832E01 Q37177814-3BCE9E85-A517-49D0-A5F6-61787EA91EBC Q37202015-6C2496AF-9C3F-4D04-8953-076702101BBC Q37388258-8A30737B-168C-435A-A54C-C14FB3E1A26A Q37448916-167C7D0B-8B19-44A7-8304-42FBF2982103 Q37611238-7F679205-1770-4A72-9628-E1D7E1B7F112 Q37837594-1661BA6F-0D79-4417-B1A1-9EBCF06BE6B3 Q37957006-B1BFDECC-2B62-4EE7-A65A-92B8361873FD Q37983021-BDE4610B-1961-4C27-91DA-40909E0FBE60 Q38013990-F9D125F0-B837-423F-A729-48D250C9D14F Q38204298-3293004A-F45A-4F17-B607-E674F275D61D Q38240032-D3A68BDD-4466-4070-98B8-8F0B44BF04A8 Q38240153-007E92A9-8193-49EB-A5D9-88F38749B1ED Q38308759-0CC4F28C-36CD-4548-9AA4-3EEADFF561A6 Q38605684-4F1F0174-DFFD-4D91-A975-0711E09D64B5 Q38673602-8D905431-764F-413F-9302-C67BA4FD6375 Q38874166-F4EC767F-223E-4690-9DC6-ECFF05521D3C Q38927569-A93E093A-8736-4F23-AEF4-F3238625A5C2

P2860

Inhibition of succinate dehydrogenase dysregulates histone modification in mammalian cells.

http://www.wikidata.org/entity/Q39784567

description

2009 nî lūn-bûn

@nan

2009年の論文

@ja

2009年論文

@yue

2009年論文

@zh-hant

2009年論文

@zh-hk

2009年論文

@zh-mo

2009年論文

@zh-tw

2009年论文

@wuu

2009年论文

@zh

2009年论文

@zh-cn

name

Inhibition of succinate dehydr ...... dification in mammalian cells.

@en

Inhibition of succinate dehydr ...... dification in mammalian cells.

@nl

type

label

Inhibition of succinate dehydr ...... dification in mammalian cells.

@en

Inhibition of succinate dehydr ...... dification in mammalian cells.

@nl

prefLabel

Inhibition of succinate dehydr ...... dification in mammalian cells.

@en

Inhibition of succinate dehydr ...... dification in mammalian cells.

@nl

P1433

Q39784567-9E3E2AB0-8B5F-49BE-9FFC-ED9505F8292E

P1476

Q39784567-5274AB27-4092-4E70-9AE6-4B852359AB09

P2093

Q39784567-BB2C4DC9-71F5-43ED-AF73-AFD770F961C3

Q39784567-C8A6C66B-BDFF-4064-BD0A-E87814CEC399

Q39784567-E9252851-DCC2-4857-B9F1-22D0626D9191

Q39784567-FD9E4F1D-BC71-44D4-BBD1-6A4B44E8915B

P2860

Q39784567-10C201A9-1577-45E7-A4D6-98F56EA2F287

Q39784567-1CEE465F-DC2C-4B02-85CD-2A8680D7E51E

Q39784567-246A0C12-F87A-43AA-9A10-0221E6CB8BB5

Q39784567-3F05A930-C551-42AA-AC3F-C66D8F160B7F

Q39784567-3F0B2EBA-87F5-47D6-ADA8-7B7AFDD2E3E9

Q39784567-3F3850FD-4C9D-4302-90A6-9E694E3C6471

Q39784567-4BC0247D-BF91-4AEF-B8C1-2895027CBC43

Q39784567-53FD1BD3-5CBE-4881-AD97-854F32AE2EED

Q39784567-54EC2A50-C772-4CAD-BC20-3CE525C2B99B

Q39784567-56C23D3B-154C-499C-8A4E-2617CE5719CB

P2888

Q39784567-D2EE41D2-0CEA-4655-8C22-965A5501132C

P304

Q39784567-C87616FD-1699-4277-A4C7-626CED722C11

P31

Q39784567-2AD0E55F-5D86-42D0-AE43-80B5E96E7D1B

P356

Q39784567-CA1EE232-EFE1-4826-929D-1374D72F38C4

P478

Q39784567-6D087889-0536-44F4-AC5A-4E112CB1A10E

P577

Q39784567-6006C721-BF27-4388-9484-42242989F94E

P5875

Q39784567-83DE9289-AE9F-42C5-A213-B858228A12B6

P6179

Q39784567-E9ACC070-BA95-41F0-9DD5-ED6EF2939E48

P698

Q39784567-0701604F-2DDF-4110-97FB-1B282E83558E

P932

Q39784567-4871868A-76D2-4945-8F93-79D04ED94AB0

P356

P1433

Molecular Cancer

P1476

Inhibition of succinate dehydr ...... dification in mammalian cells.

@en

P2093

Ana M Cervera

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

Jean-Pierre Bayley

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

Kenneth J McCreath

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

Peter Devilee

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

P2860

A bivalent chromatin structure marks key developmental genes in embryonic stem cells

Histone demethylation by a family of JmjC domain-containing proteins.

The histone H3 lysine-27 demethylase Jmjd3 links inflammation to inhibition of polycomb-mediated gene silencing

Succinate links TCA cycle dysfunction to oncogenesis by inhibiting HIF-alpha prolyl hydroxylase

The R22X mutation of the SDHD gene in hereditary paraganglioma abolishes the enzymatic activity of complex II in the mitochondrial respiratory chain and activates the hypoxia pathway

Mutations in SDHD, a mitochondrial complex II gene, in hereditary paraganglioma

The impact of O2 availability on human cancer

Neurotransmission and neuromodulation in the chemosensory carotid body.

The emerging functions of histone demethylases.

Epigenetic biomarkers for human cancer: the time is now.

P2888

P304

89

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

P31

scholarly article

P356

10.1186/1476-4598-8-89

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

P478

8

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

P577

2009-10-22T00:00:00Z

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

P5875

38029421

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

P6179

1004274639

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

P698

19849834

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

P932

2770992

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