Mass spectrometry-based quantitative proteomics for dissecting multiplexed redox cysteine modifications in nitric oxide-protected cardiomyocyte under hypoxia.
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The Measurement of Reversible Redox Dependent Post-translational Modifications and Their Regulation of Mitochondrial and Skeletal Muscle FunctionDifferential alkylation-based redox proteomics--Lessons learntMass spectrometry-based methods for identifying oxidized proteins in disease: advances and challengesProteomic approaches to quantify cysteine reversible modifications in aging and neurodegenerative diseases.Quantitative proteomics in lung cancer.Proteomic quantification and site-mapping of S-nitrosylated proteins using isobaric iodoTMT reagentsDifferential cysteine labeling and global label-free proteomics reveals an altered metabolic state in skeletal muscle aging.Proteome-wide light/dark modulation of thiol oxidation in cyanobacteria revealed by quantitative site-specific redox proteomics.Isobaric labeling-based relative quantification in shotgun proteomics.The Expanding Landscape of the Thiol Redox Proteome.SNOs Differ: Methodological and Biological Implications.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.Assessing Cardiac Metabolism: A Scientific Statement From the American Heart Association.Analysis of protein carbonylation--pitfalls and promise in commonly used methods.Fishing the PTM proteome with chemical approaches using functional solid phases.Redox proteomics: Methods for the identification and enrichment of redox-modified proteins and their applications.Spatial perspectives in the redox code-Mass spectrometric proteomics studies of moonlighting proteins.Quantitative analysis of the cysteine redoxome by iodoacetyl tandem mass tags.Redox proteomics screening cellular factors associated with oxidative stress in hepatocarcinogenesis.Characteristic tandem mass spectral features under various collision chemistries for site-specific identification of protein S-glutathionylation.Quantitative proteomic characterization of redox-dependent post-translational modifications on protein cysteines.Comprehensive Redox Profiling of the Thiol Proteome of Clostridium difficile.A simple isotopic labeling method to study cysteine oxidation in Alzheimer's disease: oxidized cysteine-selective dimethylation (OxcysDML).SMYD2 glutathionylation contributes to degradation of sarcomeric proteins
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Mass spectrometry-based quantitative proteomics for dissecting multiplexed redox cysteine modifications in nitric oxide-protected cardiomyocyte under hypoxia.
description
article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on 23 October 2013
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Mass spectrometry-based quanti ...... d cardiomyocyte under hypoxia.
@en
Mass spectrometry-based quanti ...... d cardiomyocyte under hypoxia.
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type
label
Mass spectrometry-based quanti ...... d cardiomyocyte under hypoxia.
@en
Mass spectrometry-based quanti ...... d cardiomyocyte under hypoxia.
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prefLabel
Mass spectrometry-based quanti ...... d cardiomyocyte under hypoxia.
@en
Mass spectrometry-based quanti ...... d cardiomyocyte under hypoxia.
@nl
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P2860
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Mass spectrometry-based quanti ...... ed cardiomyocyte under hypoxia
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Chun-Yi Yang
John C Rogers
Kuan-Ting Pan
Ryan D Bomgarden
Tsung-Hsien Pu
Tzu-Ching Meng
Yi-Yun Chen
Yu-Shu Chao
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P304
P356
10.1089/ARS.2013.5326
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2013-10-23T00:00:00Z