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Published in 2017 at "Basic Research in Cardiology"
DOI: 10.1007/s00395-017-0644-z
Abstract: Asymmetric dimethylarginine (ADMA) is an endogenous inhibitor of nitric oxide synthases that limits nitric oxide bioavailability. Dimethylarginine dimethylaminohydrolase-1 (DDAH1) exerts a critical role for ADMA degradation and plays an important role in NO signaling. In…
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Keywords:
plays important;
dimethylarginine;
ddah1;
important role ... See more keywords
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Published in 2017 at "Amino Acids"
DOI: 10.1007/s00726-017-2483-5
Abstract: The relationship of both asymmetric (ADMA) and symmetric (SDMA) dimethylarginine with carotid wall thickness is inconclusive especially among black populations. We aimed to compare carotid intima media thickness (cIMT) and dimethylarginine levels in 75 black…
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Keywords:
percentage change;
dimethylarginine;
black men;
adma ... See more keywords
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Published in 2018 at "Amino Acids"
DOI: 10.1007/s00726-018-2684-6
Abstract: Asymmetric dimethylarginine (ADMA) and symmetric dimethylarginine (SDMA) are endogenous inhibitors of nitric oxide (NO) synthase. SDMA is excreted in the urine without major metabolization. About 10% of daily produced ADMA are excreted unchanged in the…
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Keywords:
dimethylarginine;
dimethyl;
ddah activity;
citrulline ... See more keywords
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Published in 2018 at "Inhalation Toxicology"
DOI: 10.1080/08958378.2018.1474976
Abstract: Abstract Objective: Workers exposed to dusts from concentrated animal feeding operations have a high prevalence of pulmonary diseases. These exposures lead to chronic inflammation and aberrant airway remodeling. Previous work shows that activating cAMP-dependent protein…
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Keywords:
epithelial cells;
dimethylarginine;
wound repair;
airway epithelial ... See more keywords
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Published in 2018 at "Thorax"
DOI: 10.1136/thorax-2018-212555.147
Abstract: Background Increased nitric oxide (NO) and its generating enzyme, inducible nitric oxide synthase (iNOS), are observed in experimental models of idiopathic pulmonary fibrosis (IPF). Asymmetric dimethylarginine (ADMA) competitively inhibits iNOS and is hydrolysed by dimethylarginine…
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Keywords:
dimethylarginine;
fibrosis;
ddah1;
decline ... See more keywords
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Published in 2023 at "Physiology"
DOI: 10.1152/physiol.2023.38.s1.5734348
Abstract: Cardiovascular disease is a leading cause of death in chronic kidney disease (CKD), yet the mechanisms remain unclear. Asymmetric dimethylarginine (ADMA) and symmetric dimethylarginine (SDMA) are endogenous nitric oxide synthase inhibitors shown to be independent…
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Keywords:
function;
dimethylarginine;
ckd;
patients stage ... See more keywords
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Published in 2017 at "Medycyna Weterynaryjna"
DOI: 10.21521/mw.5741
Abstract: Diabetes is one of the systemic chronic metabolic diseases accompanied by hyperglycemia, dyslipidemia, glycosuria and much clinical and biochemical evidence (18). In diabetes, both acute and chronic complications can be seen in all organs. This…
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Keywords:
free radicals;
dimethylarginine;
dimethylarginine nitric;
measurement asymmetric ... See more keywords
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Published in 2022 at "AntiCancer Research"
DOI: 10.21873/anticanres.16138
Abstract: Background/Aim: Asymmetric dimethylarginine (ADMA) is an endogenous inhibitor of nitric oxide (NO) production and a newly discovered risk factor involved in endothelial dysfunction and adverse cardiovascular events. Recently, both NO and ADMA have also emerged…
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Keywords:
dimethylarginine;
asymmetric dimethylarginine;
dimethylarginine nmu;
sdma arginine ... See more keywords
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Published in 2019 at "Biomolecules"
DOI: 10.3390/biom9070277
Abstract: Despite genetic heterogeneity, early manifestation of diastolic dysfunction (DD) is common in hypertrophic cardiomyopathy (HCM). Nitric oxide (NO) may contribute to myocardial relaxation. NO synthases (NOS) use l-arginine (Arg) as a substrate, as asymmetric dimethylarginine…
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Keywords:
dimethylarginine;
hypertrophic cardiomyopathy;
association;
diastolic dysfunction ... See more keywords
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Published in 2022 at "Molecules"
DOI: 10.3390/molecules27030983
Abstract: Epigenetic readout of the combinatorial posttranslational modification comprised of trimethyllysine and asymmetric dimethylarginine (H3K4me3R8me2a) takes place via biomolecular recognition of tandem Tudor-domain-containing protein Spindlin1. Through comparative thermodynamic data and molecular dynamics simulations, we sought to…
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Keywords:
recognition;
protein spindlin1;
dimethylarginine;
tandem tudor ... See more keywords