Characterization of potential S-nitrosylation sites in the myocardium - Wikidata - awgldk - TriplyDB

Characterization of potential S-nitrosylation sites in the myocardium

Characterization of potential S-nitrosylation sites in the myocardium

http://www.wikidata.org/entity/Q28304250

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The Dual Function of Reactive Oxygen/Nitrogen Species in Bioenergetics and Cell Death: The Role of ATP Synthase Differential alkylation-based redox proteomics--Lessons learnt Nitric oxide-sphingolipid interplays in plant signalling: a new enigma from the Sphinx?The mitochondrial permeability transition pore: molecular nature and role as a target in cardioprotection An Interplay of S-Nitrosylation and Metal Ion Binding for Astrocytic S100B Protein Mitochondrial adenine nucleotide transport and cardioprotection Proteomic approaches to quantify cysteine reversible modifications in aging and neurodegenerative diseases.Methodologies for the characterization, identification and quantification of S-nitrosylated proteins.Pivotal role of mTORC2 and involvement of ribosomal protein S6 in cardioprotective signaling Adenosine A1 receptor activation increases myocardial protein S-nitrosothiols and elicits protection from ischemia-reperfusion injury in male and female hearts High Sensitivity of SIRT3 Deficient Hearts to Ischemia-Reperfusion Is Associated with Mitochondrial Abnormalities.Cardiac mitochondria and reactive oxygen species generation Global analysis of S-nitrosylation sites in the wild type (APP) transgenic mouse brain-clues for synaptic pathology.Glyceraldehyde-3-phosphate dehydrogenase acts as a mitochondrial trans-S-nitrosylase in the heart Cysteine 203 of cyclophilin D is critical for cyclophilin D activation of the mitochondrial permeability transition pore Structural mechanisms of cyclophilin D-dependent control of the mitochondrial permeability transition pore.S-nitrosylation: a radical way to protect the heart Identification and quantification of S-nitrosylation by cysteine reactive tandem mass tag switch assay Overexpression of Catalase Diminishes Oxidative Cysteine Modifications of Cardiac Proteins.S-Nitrosylation of Calcium-Handling Proteins in Cardiac Adrenergic Signaling and Hypertrophy The Mitochondrial Permeability Transition Pore: Channel Formation by F-ATP Synthase, Integration in Signal Transduction, and Role in Pathophysiology.S-Nitrosylation of Sarcomeric Proteins Depresses Myofilament Ca2+)Sensitivity in Intact Cardiomyocytes.Measurement of S-nitrosylation occupancy in the myocardium with cysteine-reactive tandem mass tags: short communication.Redox regulation of mitochondrial ATP synthase: implications for cardiac resynchronization therapy.Modulation of myocardial contraction by peroxynitrite S-nitrosylation: integrator of cardiovascular performance and oxygen delivery.Solid-phase capture for the detection and relative quantification of S-nitrosoproteins by mass spectrometry.Characterization of the sex-dependent myocardial S-nitrosothiol proteome.Mitochondrial permeability transition and cell death: the role of cyclophilin d Reduction of cardiomyocyte S-nitrosylation by S-nitrosoglutathione reductase protects against sepsis-induced myocardial depression.S-nitrosylation of TRIM72 mends the broken heart: a molecular modifier-mediated cardioprotection.High-throughput endogenous measurement of S-nitrosylation in Alzheimer's disease using oxidized cysteine-selective cPILOT.Dual Labeling Biotin Switch Assay to Reduce Bias Derived From Different Cysteine Subpopulations: A Method to Maximize S-Nitrosylation Detection.Quantitative site-specific reactivity profiling of S-nitrosylation in mouse skeletal muscle using cysteinyl peptide enrichment coupled with mass spectrometry.S-nitrosylation: specificity, occupancy, and interaction with other post-translational modifications.Postconditioning leads to an increase in protein S-nitrosylation.S-nitrosylation of TRIM72 at cysteine 144 is critical for protection against oxidation-induced protein degradation and cell death.Recent insights in the paracrine modulation of cardiomyocyte contractility by cardiac endothelial cells.Does the voltage dependent anion channel modulate cardiac ischemia-reperfusion injury?Development and application of site-specific proteomic approach for study protein S-nitrosylation.

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Characterization of potential S-nitrosylation sites in the myocardium

http://www.wikidata.org/entity/Q28304250

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2011 nî lūn-bûn

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2011 թուականի Ապրիլին հրատարակուած գիտական յօդուած

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2011 թվականի ապրիլին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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name

Characterization of potential S-nitrosylation sites in the myocardium

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Characterization of potential S-nitrosylation sites in the myocardium

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Characterization of potential S-nitrosylation sites in the myocardium

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type

label

Characterization of potential S-nitrosylation sites in the myocardium

@ast

Characterization of potential S-nitrosylation sites in the myocardium

@en

Characterization of potential S-nitrosylation sites in the myocardium

@nl

prefLabel

Characterization of potential S-nitrosylation sites in the myocardium

@ast

Characterization of potential S-nitrosylation sites in the myocardium

@en

Characterization of potential S-nitrosylation sites in the myocardium

@nl

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AJPHEART.00997.2010

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American Journal of Physiology - Heart and Circulatory Physiology

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Characterization of potential S-nitrosylation sites in the myocardium

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Angel M Aponte

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Charles Steenbergen

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Elizabeth Murphy

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Guanghui Wang

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Junhui Sun

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Marjan Gucek

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Mark J Kohr

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P2860

Endogenous S-nitrosothiols protect against myocardial injury

Probability-based protein identification by searching sequence databases using mass spectrometry data

Identification of S-nitrosated mitochondrial proteins by S-nitrosothiol difference in gel electrophoresis (SNO-DIGE): implications for the regulation of mitochondrial function by reversible S-nitrosation

Protein S-nitrosylation: purview and parameters

An iterative statistical approach to the identification of protein phosphorylation motifs from large-scale data sets.

An assessment of software solutions for the analysis of mass spectrometry based quantitative proteomics data.

Proteomic analysis of S-nitrosylation and denitrosylation by resin-assisted capture

Cysteine-3635 is responsible for skeletal muscle ryanodine receptor modulation by NO

SNOSID, a proteomic method for identification of cysteine S-nitrosylation sites in complex protein mixtures.

Nitric oxide synthase generates nitric oxide locally to regulate compartmentalized protein S-nitrosylation and protein trafficking.

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10.1152/AJPHEART.00997.2010

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