3-Hydroxy-3-methylglutaric and 3-methylglutaric acids impair redox status and energy production and transfer in rat heart: relevance for the pathophysiology of cardiac dysfunction in 3-hydroxy-3-methylglutaryl-coenzyme A lyase deficiency. (Q39588663)

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scientific article published on 18 July 2016

Language	Label	Description	Also known as
English	3-Hydroxy-3-methylglutaric and 3-methylglutaric acids impair redox status and energy production and transfer in rat heart: relevance for the pathophysiology of cardiac dysfunction in 3-hydroxy-3-methylglutaryl-coenzyme A lyase deficiency.	scientific article published on 18 July 2016

Statements

scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

13 September 2017

3-Hydroxy-3-methylglutaric and 3-methylglutaric acids impair redox status and energy production and transfer in rat heart: relevance for the pathophysiology of cardiac dysfunction in 3-hydroxy-3-methylglutaryl-coenzyme A lyase deficiency. (English)

1 reference

Europe PubMed Central

PubMed publication ID

13 September 2017

pathophysiology

0 references

Belisa Parmeggiani

object named as

Belisa Parmeggiani

4

0 references

César Augusto João Ribeiro

object named as

César Augusto João Ribeiro

3

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author name string

Mateus Struecker da Rosa

1

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Europe PubMed Central

PubMed publication ID

13 September 2017

Bianca Seminotti

2

1 reference

Europe PubMed Central

PubMed publication ID

13 September 2017

Mateus Grings

5

1 reference

Europe PubMed Central

PubMed publication ID

13 September 2017

Moacir Wajner

6

1 reference

Europe PubMed Central

PubMed publication ID

13 September 2017

Guilhian Leipnitz

7

1 reference

Europe PubMed Central

PubMed publication ID

13 September 2017

publication date

18 July 2016

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Europe PubMed Central

PubMed publication ID

13 September 2017

Free Radical Research

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Europe PubMed Central

PubMed publication ID

13 September 2017

50

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Europe PubMed Central

PubMed publication ID

13 September 2017

9

1 reference

Europe PubMed Central

PubMed publication ID

13 September 2017

997-1010

1 reference

Europe PubMed Central

PubMed publication ID

13 September 2017

Differential HMG-CoA lyase expression in human tissues provides clues about 3-hydroxy-3-methylglutaric aciduria

1 reference

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Evidence that 3-hydroxy-3-methylglutaric acid promotes lipid and protein oxidative damage and reduces the nonenzymatic antioxidant defenses in rat cerebral cortex.

1 reference

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Induction of oxidative stress by the metabolites accumulating in 3-methylglutaconic aciduria in cerebral cortex of young rats.

1 reference

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In vivo experimental evidence that the major metabolites accumulating in 3-hydroxy-3-methylglutaryl-CoA lyase deficiency induce oxidative stress in striatum of developing rats: a potential pathophysiological mechanism of striatal damage in this diso

1 reference

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21 January 2018

Redox homeostasis is compromised in vivo by the metabolites accumulating in 3-hydroxy-3-methylglutaryl-CoA lyase deficiency in rat cerebral cortex and liver.

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Disturbance of brain energy and redox homeostasis provoked by sulfite and thiosulfate: potential pathomechanisms involved in the neuropathology of sulfite oxidase deficiency.

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α-Lipoic acid protected cardiomyoblasts from the injury induced by sodium nitroprusside through ROS-mediated Akt/Gsk-3β activation

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Inhibition of creatine kinase activity from rat cerebral cortex by D-2-hydroxyglutaric acid in vitro.

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Catalase in vitro

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3-Hydroxy-3-methylglutaric aciduria in an Italian patient is caused by a new nonsense mutation in the HMGCL gene.

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3-Hydroxy-3-methylglutaryl coenzyme a lyase deficiency with reversible white matter changes after treatment

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Differential effects of peroxynitrite on human mitochondrial creatine kinase isoenzymes. Inactivation, octamer destabilization, and identification of involved residues

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Mitochondrial dysfunction in heart failure

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Creatine kinase and ATP synthase reaction rates in human frontal lobe measured by ³¹P magnetization transfer spectroscopy at 4T.

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Hydrogen peroxide targets the cysteine at the active site and irreversibly inactivates creatine kinase

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An unusually low pK(a) for Cys282 in the active site of human muscle creatine kinase

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Rapid and irreversible inhibition of creatine kinase by peroxynitrite

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Oligomeric state and membrane binding behaviour of creatine kinase isoenzymes: implications for cellular function and mitochondrial structure.

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Protein carbonyl groups as biomarkers of oxidative stress.

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H2O2 and tumor necrosis factor-alpha induce differential binding of the redox-responsive transcription factors AP-1 and NF-kappaB to the interleukin-8 promoter in endothelial and epithelial cells

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Oxidative stress and neurodegeneration: where are we now?

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Inactivation of human Cu,Zn superoxide dismutase by peroxynitrite and formation of histidinyl radical.

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Vitamin D treatment protects against and reverses oxidative stress induced muscle proteolysis

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Intracerebral accumulation of glutaric and 3-hydroxyglutaric acids secondary to limited flux across the blood-brain barrier constitute a biochemical risk factor for neurodegeneration in glutaryl-CoA dehydrogenase deficiency

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Identifiers

10.1080/10715762.2016.1214952

1 reference

Europe PubMed Central

PubMed publication ID

13 September 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

13 September 2017

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