Quantitative mapping of reversible mitochondrial Complex I cysteine oxidation in a Parkinson disease mouse model.
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The Measurement of Reversible Redox Dependent Post-translational Modifications and Their Regulation of Mitochondrial and Skeletal Muscle FunctionImaging multiple sclerosis and other neurodegenerative diseasesRecent advances in quantitative neuroproteomicsProteomic approaches to quantify cysteine reversible modifications in aging and neurodegenerative diseases.Oxidative stress and mitochondrial dysfunction across broad-ranging pathologies: toward mitochondria-targeted clinical strategies.HIBCH mutations can cause Leigh-like disease with combined deficiency of multiple mitochondrial respiratory chain enzymes and pyruvate dehydrogenase.Regulatory control or oxidative damage? Proteomic approaches to interrogate the role of cysteine oxidation status in biological processes.Antioxidant treatment normalizes mitochondrial energetics and myocardial insulin sensitivity independently of changes in systemic metabolic homeostasis in a mouse model of the metabolic syndrome.Reactive oxygen species scavenger N-acetyl cysteine reduces methamphetamine-induced hyperthermia without affecting motor activity in mice.Glutathione and modulation of cell apoptosis.Thiol-redox signaling, dopaminergic cell death, and Parkinson's diseaseOXPHOS mutations and neurodegenerationEndogenous reactive oxygen species cause astrocyte defects and neuronal dysfunctions in the hippocampus: a new model for aging brain.Sex-specific differences in mitochondria biogenesis, morphology, respiratory function, and ROS homeostasis in young mouse heart and brain.Selective vulnerability of synaptic signaling and metabolism to nitrosative stressThe interplay between iron accumulation, mitochondrial dysfunction, and inflammation during the execution step of neurodegenerative disorders.Quantitative proteomic characterization of redox-dependent post-translational modifications on protein cysteines.Post-Translational Oxidative Modifications of Mitochondrial Complex I (NADH: Ubiquinone Oxidoreductase): Implications for Pathogenesis and Therapeutics in Human Diseases.A LON-ClpP Proteolytic Axis Degrades Complex I to Extinguish ROS Production in Depolarized Mitochondria.Zonisamide attenuates MPP+-induced oxidative toxicity through modulation of Ca2+ signaling and caspase-3 activity in neuronal PC12 cells.Fatiguing contractions increase protein S-glutathionylation occupancy in mouse skeletal muscle.
P2860
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P2860
Quantitative mapping of reversible mitochondrial Complex I cysteine oxidation in a Parkinson disease mouse model.
description
2011 nî lūn-bûn
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2011 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2011年の論文
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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
name
Quantitative mapping of revers ...... Parkinson disease mouse model.
@ast
Quantitative mapping of revers ...... Parkinson disease mouse model.
@en
Quantitative mapping of revers ...... Parkinson disease mouse model.
@nl
type
label
Quantitative mapping of revers ...... Parkinson disease mouse model.
@ast
Quantitative mapping of revers ...... Parkinson disease mouse model.
@en
Quantitative mapping of revers ...... Parkinson disease mouse model.
@nl
prefLabel
Quantitative mapping of revers ...... Parkinson disease mouse model.
@ast
Quantitative mapping of revers ...... Parkinson disease mouse model.
@en
Quantitative mapping of revers ...... Parkinson disease mouse model.
@nl
P2093
P2860
P356
P1476
Quantitative mapping of revers ...... Parkinson disease mouse model.
@en
P2093
Bradford W Gibson
Jason M Held
Julie K Andersen
Rebeccah Riley
Steven R Danielson
P2860
P304
P356
10.1074/JBC.M110.190108
P407
P577
2011-01-01T00:00:00Z