Loss of Bmal1 leads to uncoupling and impaired glucose-stimulated insulin secretion in β-cells. - Wikidata - awgldk - TriplyDB

Loss of Bmal1 leads to uncoupling and impaired glucose-stimulated insulin secretion in β-cells.

Loss of Bmal1 leads to uncoupling and impaired glucose-stimulated insulin secretion in β-cells.

http://www.wikidata.org/entity/Q35897323

about

Evidences of Polymorphism Associated with Circadian System and Risk of Pathologies: A Review of the Literature Clock genes in hypertension: novel insights from rodent models Does disruption of circadian rhythms contribute to beta-cell failure in type 2 diabetes?Circadian dysfunction may be a key component of the non-motor symptoms of Parkinson's disease: insights from a transgenic mouse model Circadian regulation of metabolism Circadian System and Glucose Metabolism: Implications for Physiology and Disease Clock genes, pancreatic function, and diabetes Carbohydrate response element-binding protein (ChREBP) plays a pivotal role in beta cell glucotoxicity Mechanism of the circadian clock in physiology.Uncoupling protein 2 regulates daily rhythms of insulin secretion capacity in MIN6 cells and isolated islets from male mice Advances in understanding the peripheral circadian clocks.Small molecule modifiers of circadian clocks.Global loss of bmal1 expression alters adipose tissue hormones, gene expression and glucose metabolism PD-L1-driven tolerance protects neurogenin3-induced islet neogenesis to reverse established type 1 diabetes in NOD mice.Trastuzumab alters the expression of genes essential for cardiac function and induces ultrastructural changes of cardiomyocytes in mice.The Fragile X proteins Fmrp and Fxr2p cooperate to regulate glucose metabolism in mice.Transcriptional control of circadian metabolic rhythms in the liver.Reprogramming of the circadian clock by nutritional challenge.CLOCK gene variation is associated with incidence of type-2 diabetes and cardiovascular diseases in type-2 diabetic subjects: dietary modulation in the PREDIMED randomized trial.Circadian control of β-cell function and stress responses.Bmal1 and β-cell clock are required for adaptation to circadian disruption, and their loss of function leads to oxidative stress-induced β-cell failure in mice Molecular clock integration of brown adipose tissue formation and function.Consequences of exposure to light at night on the pancreatic islet circadian clock and function in rats.Synchronized human skeletal myotubes of lean, obese and type 2 diabetic patients maintain circadian oscillation of clock genes.Decompensation of β-cells in diabetes: when pancreatic β-cells are on ICE(R).Clocks and cardiovascular function.Experimental and clinical aspects of melatonin and clock genes in diabetes.MicroRNAs modulate core-clock gene expression in pancreatic islets during early postnatal life in rats.Pancreatic α- and β-cellular clocks have distinct molecular properties and impact on islet hormone secretion and gene expression.Unique Aspects of Cryptochrome in Chronobiology and Metabolism, Pancreatic β-Cell Dysfunction, and Regeneration: Research into Cysteine414-Alanine Mutant CRY1.Circadian factors BMAL1 and RORα control HIF-1α transcriptional activity in nucleus pulposus cells: implications in maintenance of intervertebral disc health A functional circadian clock is required for proper insulin secretion by human pancreatic islet cells.Suppression of circadian secretion of glucagon-like peptide-1 by the saturated fatty acid, palmitate.Circadian rhythms in mitochondrial respiration.Decreased insulin secretion in pregnant rats fed a low protein diet.A role for circadian clock in metabolic disease.Untimely Oxidative Stress in β-cells Leads to Diabetes - Role of Circadian Clock in β-cell Function.Circadian Rhythms in Diet-Induced Obesity.

P2860

Q26745529-F80A7CED-B2FA-463B-99AA-5CB50C9002EA Q26782018-7BF8461A-7D21-4F90-BD92-2FAAFA455058 Q27026480-C5A2B5D1-58B3-4382-A54F-CA90ED064DB2 Q28384426-3583F7B2-53D5-40F3-83E3-ABEA40AD9212 Q28390852-D7C26207-95FE-4A27-926C-8289247CE261 Q28392828-5BA5EB38-16C1-4E38-A9C4-AB67B49FAB56 Q28393998-BB521E02-6BA5-45C6-A30E-E7024D9DA423 Q33566931-6426DF44-28C5-4E0C-AB5D-5CE15B9EE0C1 Q33816493-BB83436E-30F9-4AEE-8A3B-FEE8A89836D2 Q33836038-D2AD44E8-2EAB-4B44-9CD1-7B5B344AD5E3 Q34278723-8977E30A-9C71-45A0-A045-B23B26B86502 Q34480532-EAB2CB83-6C51-40B8-9888-B8439344CD14 Q34764246-5FAEFBAE-BDC4-4BF4-AF31-FEE6499D6E7E Q35004384-1C6C0484-6D90-47BC-BF42-39D501B1A2BF Q35047415-C7C500D0-65F2-4CDA-AB1C-134197F9DE24 Q35234080-603792D1-0B1C-41EE-8393-B48B24F91816 Q36034647-447477B7-D474-4477-9C13-A82F9F50EDCA Q36069161-1CFFF5D8-EEA4-4C61-915D-B60C44E48771 Q36439651-D1A35617-6CBF-4C0B-B5BC-E9E39AEF9CA4 Q36604026-893D27A2-466F-4CAB-A6ED-7DF85DCEFB62 Q36827096-43A5FD75-E1DF-42BA-B9DA-E8E20CBF4B22 Q37028370-2D9C382F-5C29-4881-A04A-AF7F7027092C Q37193371-11AB6F4B-57A8-45F7-8821-F9DA6E98BAC6 Q37348759-D1C4506B-FB68-4666-B5E4-3FA5B21E04CC Q37615190-34FC5A56-E618-4821-81F3-756347FA3F25 Q38364377-ABBDF3A8-FAAC-4296-A819-E9E28894EE8E Q38436840-C76853EC-917E-47D9-A8A7-B64431579B4E Q38695011-D00A1FD4-1673-4333-889A-FA4579EB9F39 Q38919759-678E1538-AD32-4F83-A1B3-89B8505C09C6 Q39096012-7D704960-7867-4546-B404-61E3AC24E259 Q41133336-6251AC50-6214-493F-BA68-8EB3F1E257CD Q42486168-9E58E156-9A15-460B-9403-FA8562BCE076 Q47343038-CD90E9A5-4F40-493C-A032-8E9B868F4EEB Q47552237-350EAA9F-1DC2-43F6-81B6-F6B56126D7B8 Q47661190-5975DE29-C1C9-486B-AA4A-41177B8A5FE4 Q47886728-5B1FFD83-E628-42DE-992A-FFABB095AE1D Q49846774-04381C8C-3102-49B5-9AA4-151C013E7457 Q50599434-A67CF7BB-7C40-4B75-94CA-430EF52398C7

P2860

Loss of Bmal1 leads to uncoupling and impaired glucose-stimulated insulin secretion in β-cells.

http://www.wikidata.org/entity/Q35897323

description

2011 nî lūn-bûn

@nan

2011年の論文

@ja

2011年論文

@yue

2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

@wuu

2011年论文

@zh

2011年论文

@zh-cn

name

Loss of Bmal1 leads to uncoupl ...... insulin secretion in β-cells.

@ast

Loss of Bmal1 leads to uncoupl ...... insulin secretion in β-cells.

@en

type

label

Loss of Bmal1 leads to uncoupl ...... insulin secretion in β-cells.

@ast

Loss of Bmal1 leads to uncoupl ...... insulin secretion in β-cells.

@en

prefLabel

Loss of Bmal1 leads to uncoupl ...... insulin secretion in β-cells.

@ast

Loss of Bmal1 leads to uncoupl ...... insulin secretion in β-cells.

@en

P1433

Q35897323-44BB9F91-3DA5-4A05-839C-84E306737678

P1476

Q35897323-EC86FD08-4E01-497C-BECC-6CEDCB09E209

P2093

Q35897323-32ADA19D-6E7E-41A4-8196-1F68FCF8045B

Q35897323-35BCAF6D-A2D6-450E-AAD0-187B6C28E476

Q35897323-6C79E535-1BEB-4A70-85B6-62A0C5E3A650

Q35897323-73B32188-2C0A-4FCC-911C-F701EEF22511

Q35897323-7F6F3C01-5399-48AA-9396-3ED1FA7997FA

Q35897323-7F871975-4150-4483-A0FA-19887449C02A

Q35897323-B83877F1-889A-4DB4-87BA-5F4A5A216409

Q35897323-C8793465-9886-49CE-9C1C-5913A304406B

P2860

Q35897323-097CFFE5-B535-41CF-A891-121F02868B11

Q35897323-1446451F-63E5-4AC4-87DD-A265C79540F6

Q35897323-1532AD68-3C0B-45D7-BF42-5C35F50F4B4A

Q35897323-153EF1EC-4993-4AEC-B692-15E60B3DB3AF

Q35897323-16A62F7B-A0C3-44B9-892C-CD2700F2A637

Q35897323-1CF3C945-F77F-46C2-AF32-94CE15E4D057

Q35897323-22D9EAC6-8148-4776-8244-76345FF29899

Q35897323-244EBA46-5F1D-49BA-A9FB-E5AFAF1FA2FC

Q35897323-2DEE933D-CA1C-46D6-B258-66E80D18E2A1

Q35897323-326BBE1E-8957-48BA-B7FF-2C8A5D85E5B0

P304

Q35897323-7F8AEF13-0AFD-4FA7-B1AB-2373DA646780

P31

Q35897323-C09DC497-8DD4-41F2-ABA7-C9216E8884CE

P356

Q35897323-57581C8C-6A35-407B-BD9A-A7C3747B87FE

P433

Q35897323-FE89567A-2AB0-4705-8641-BBA88A53694B

P478

Q35897323-54A7E883-7333-49DF-A585-1373ADEC57B2

P577

Q35897323-74086982-1867-4A90-92E2-E22D42A6578E

P5875

Q35897323-32E6EC3F-D4B8-4E5E-8F55-76072E4E2D62

P698

Q35897323-F5D63D71-37E4-4A35-8F28-A18C535E5C71

P932

Q35897323-8DEB3A95-FF08-49B8-A486-68C923306D20

P356

P1433

P1476

Loss of Bmal1 leads to uncoupl ...... insulin secretion in β-cells.

@en

P2093

David D Moore

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

Jeongkyung Lee

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

Ke Ma

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

Loning Fu

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

Mi-Sun Kim

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

Rongying Li

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

Victoria Y Liu

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

Vijay K Yechoor

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

P2860

REV-ERBalpha participates in circadian SREBP signaling and bile acid homeostasis

BMAL1 and CLOCK, two essential components of the circadian clock, are involved in glucose homeostasis

Rev-erbalpha, a heme sensor that coordinates metabolic and circadian pathways

SIRT1 regulates circadian clock gene expression through PER2 deacetylation

Accurate normalization of real-time quantitative RT-PCR data by geometric averaging of multiple internal control genes

The NAD+-dependent deacetylase SIRT1 modulates CLOCK-mediated chromatin remodeling and circadian control

Disruption of the clock components CLOCK and BMAL1 leads to hypoinsulinaemia and diabetes

Circadian clock feedback cycle through NAMPT-mediated NAD+ biosynthesis

Aryl hydrocarbon receptor nuclear translocator-like (BMAL1) is associated with susceptibility to hypertension and type 2 diabetes

Sirt1 regulates insulin secretion by repressing UCP2 in pancreatic beta cells

P304

381-388

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

P31

scholarly article

P356

10.4161/ISL.3.6.18157

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

P433

6

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

P478

3

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

P577

2011-11-01T00:00:00Z

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

P5875

51728942

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

P698

22045262

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

P932

3329519

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