Histone deacetylase (HDAC) inhibition as a novel treatment for diabetes mellitus. - Wikidata - awgldk - TriplyDB

Histone deacetylase (HDAC) inhibition as a novel treatment for diabetes mellitus.

Histone deacetylase (HDAC) inhibition as a novel treatment for diabetes mellitus.

http://www.wikidata.org/entity/Q37832964

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Histone deacetylase inhibitor (HDACi) suberoylanilide hydroxamic acid (SAHA)-mediated correction of α1-antitrypsin deficiency New insights into insulin: The anti-inflammatory effect and its clinical relevance Growing the growth cone: remodeling the cytoskeleton to promote axon regeneration Targeting inflammation in diabetes: Newer therapeutic options Metabolic reprogramming by class I and II histone deacetylases Islet inflammation: a unifying target for diabetes treatment?Metabolism, longevity and epigenetics Histone deacetylases as targets for treatment of multiple diseases Transcriptional regulation of chemokine genes: a link to pancreatic islet inflammation?Translational implications of the β-cell epigenome in diabetes mellitus Dosage-dependent tumor suppression by histone deacetylases 1 and 2 through regulation of c-Myc collaborating genes and p53 function Enhancement of glucose uptake in mouse skeletal muscle cells and adipocytes by P2Y6 receptor agonists Histone deacetylases 1 and 3 but not 2 mediate cytokine-induced beta cell apoptosis in INS-1 cells and dispersed primary islets from rats and are differentially regulated in the islets of type 1 diabetic children Virtual screening and experimental validation of novel histone deacetylase inhibitors Lysine deacetylase inhibition prevents diabetes by chromatin-independent immunoregulation and β-cell protection β-cell failure in type 2 diabetes: postulated mechanisms and prospects for prevention and treatment.Evidence for the gut microbiota short-chain fatty acids as key pathophysiological molecules improving diabetes.Histone deacetylase 1 reduces NO production in endothelial cells via lysine deacetylation of NO synthase 3.Genome-wide associations between genetic and epigenetic variation influence mRNA expression and insulin secretion in human pancreatic islets.Gadd45α: a novel diabetes-associated gene potentially linking diabetic cardiomyopathy and baroreflex dysfunction.The class I histone deacetylase inhibitor MS-275 prevents pancreatic beta cell death induced by palmitate.Histone deacetylase inhibitor suppresses virus-induced proinflammatory responses and type 1 diabetes.Histone deacetylase inhibitors for treating a spectrum of diseases not related to cancer Recent Progress in the Use of Glucagon and Glucagon Receptor Antago-nists in the Treatment of Diabetes Mellitus Lessons Learnt from Post-Infectious IBS.Helsinki alert of biodiversity and health.Sodium butyrate epigenetically modulates high-fat diet-induced skeletal muscle mitochondrial adaptation, obesity and insulin resistance through nucleosome positioning Targeting Histone Deacetylases in Diseases: Where Are We?DNA methylation profiling identifies epigenetic dysregulation in pancreatic islets from type 2 diabetic patients.Histone deacetylase (HDAC) inhibition improves myocardial function and prevents cardiac remodeling in diabetic mice.In Vivo Screening Using Transgenic Zebrafish Embryos Reveals New Effects of HDAC Inhibitors Trichostatin A and Valproic Acid on Organogenesis.Mitochondria and Oxidative Stress in the Cardiorenal Metabolic Syndrome.Molecular targets related to inflammation and insulin resistance and potential interventions HDAC expression and activity is upregulated in diseased lupus-prone mice.Metabolic Diseases Downregulate the Majority of Histone Modification Enzymes, Making a Few Upregulated Enzymes Novel Therapeutic Targets--"Sand Out and Gold Stays".Epigenetic Mechanisms of the Aging Human Retina.Butyrate alleviates metabolic impairments and protects pancreatic β cell function in pregnant mice with obesity.HDAC Inhibition Modulates Cardiac PPARs and Fatty Acid Metabolism in Diabetic Cardiomyopathy.Histone deacetylase inhibition regulates miR-449a levels in skeletal muscle cells.Trichostatin A affects the secretion pathways of beta and intestinal endocrine cells.

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Histone deacetylase (HDAC) inhibition as a novel treatment for diabetes mellitus.

http://www.wikidata.org/entity/Q37832964

description

article científic

@ca

article scientifique

@fr

articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on 25 January 2011

@en

vedecký článok

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vetenskaplig artikel

@sv

videnskabelig artikel

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vědecký článek

@cs

name

Histone deacetylase (HDAC) inhibition as a novel treatment for diabetes mellitus.

@en

type

label

Histone deacetylase (HDAC) inhibition as a novel treatment for diabetes mellitus.

@en

prefLabel

Histone deacetylase (HDAC) inhibition as a novel treatment for diabetes mellitus.

@en

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MOLMED.2011.00021

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Molecular Medicine

P1476

Histone deacetylase (HDAC) inhibition as a novel treatment for diabetes mellitus.

@en

P2093

Dan P Christensen

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

Lars G Grunnet

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

Mattias Dahllöf

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

Mette D Nielsen

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P2860

Activation of the myocyte enhancer factor-2 transcription factor by calcium/calmodulin-dependent protein kinase-stimulated binding of 14-3-3 to histone deacetylase 5

Critical and functional regulation of CHOP (C/EBP homologous protein) through the N-terminal portion

AMP-activated protein kinase regulates GLUT4 transcription by phosphorylating histone deacetylase 5

Insulin gene transcription is mediated by interactions between the p300 coactivator and PDX-1, BETA2, and E47.

The p65 (RelA) subunit of NF-kappaB interacts with the histone deacetylase (HDAC) corepressors HDAC1 and HDAC2 to negatively regulate gene expression

The role of epigenetics in the pathology of diabetic complications

Genome-wide association study and meta-analysis find that over 40 loci affect risk of type 1 diabetes

neurogenin3 is required for the development of the four endocrine cell lineages of the pancreas

Acetylation of insulin receptor substrate-1 is permissive for tyrosine phosphorylation

Lysine acetylation targets protein complexes and co-regulates major cellular functions

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molmed.2011.00021

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378-390

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scholarly article

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10.2119/MOLMED.2011.00021

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5-6

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P478

17

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Daniel Noesgaard

Nils Billestrup

Thomas Mandrup-Poulsen

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2011-01-25T00:00:00Z

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49792154

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1032078607

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21274504

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3105132

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