Targeted quantitation of site-specific cysteine oxidation in endogenous proteins using a differential alkylation and multiple reaction monitoring mass spectrometry approach
about
The Measurement of Reversible Redox Dependent Post-translational Modifications and Their Regulation of Mitochondrial and Skeletal Muscle FunctionDifferential alkylation-based redox proteomics--Lessons learntApplications of targeted proteomics in systems biology and translational medicineMass spectrometry in studies of protein thiol chemistry and signaling: opportunities and caveatsMass spectrometry-based methods for identifying oxidized proteins in disease: advances and challengesPurification of reversibly oxidized proteins (PROP) reveals a redox switch controlling p38 MAP kinase activity.Proteomic profile of reversible protein oxidation using PROP, purification of reversibly oxidized proteins.Mitochondrial ROS regulate thermogenic energy expenditure and sulfenylation of UCP1NOX2, p22phox and p47phox are targeted to the nuclear pore complex in ischemic cardiomyocytes colocalizing with local reactive oxygen speciesProteome-wide covalent ligand discovery in native biological systemsMeasurement of Reactive Oxygen Species, Reactive Nitrogen Species, and Redox-Dependent Signaling in the Cardiovascular System: A Scientific Statement From the American Heart Association.Determination of oxidative protein modifications using mass spectrometry.Quantifying reversible oxidation of protein thiols in photosynthetic organisms.Proteomic approaches to quantify cysteine reversible modifications in aging and neurodegenerative diseases.Click-PEGylation - A mobility shift approach to assess the redox state of cysteines in candidate proteinsCardioprotection by S-nitrosation of a cysteine switch on mitochondrial complex I.Quantification of beta-catenin signaling components in colon cancer cell lines, tissue sections, and microdissected tumor cells using reaction monitoring mass spectrometry.Distinction of thioredoxin transnitrosylation and denitrosylation target proteins by the ICAT quantitative approach.Effect of single amino acid substitution on oxidative modifications of the Parkinson's disease-related protein, DJ-1Functional proteomics approaches for the identification of transnitrosylase and denitrosylase targets.Quantitative mapping of reversible mitochondrial Complex I cysteine oxidation in a Parkinson disease mouse model.Proteome-wide light/dark modulation of thiol oxidation in cyanobacteria revealed by quantitative site-specific redox proteomics.Cysteine-based redox switches in enzymesExoplasmic cysteine Cys384 of the HDL receptor SR-BI is critical for its sensitivity to a small-molecule inhibitor and normal lipid transport activityGlobal analysis of myocardial peptides containing cysteines with irreversible sulfinic and sulfonic acid post-translational modifications.Recent advances in proteomics: towards the human proteome.Thioredoxin 1-mediated post-translational modifications: reduction, transnitrosylation, denitrosylation, and related proteomics methodologies.ROS-induced ROS release in vascular biology: redox-redox signaling.Identification of reduction-susceptible disulfide bonds in transferrin by differential alkylation using O(16)/O(18) labeled iodoacetic acid.Mass-spectrometry-based characterization of oxidations in proteins.Regulatory control or oxidative damage? Proteomic approaches to interrogate the role of cysteine oxidation status in biological processes.Advancing the sensitivity of selected reaction monitoring-based targeted quantitative proteomics.Methods to monitor classical protein-tyrosine phosphatase oxidation.Antibody-free, targeted mass-spectrometric approach for quantification of proteins at low picogram per milliliter levels in human plasma/serum.Oxidant sensing by reversible disulfide bond formationProteome-wide detection and quantitative analysis of irreversible cysteine oxidation using long column UPLC-pSRM.Long-gradient separations coupled with selected reaction monitoring for highly sensitive, large scale targeted protein quantification in a single analysis.Regulation of protein tyrosine phosphatases by reversible oxidation.Non-enzymatic glycation and glycoxidation protein products in foods and diseases: an interconnected, complex scenario fully open to innovative proteomic studies.Targeted proteomics of myofilament phosphorylation and other protein posttranslational modifications.
P2860
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P2860
Targeted quantitation of site-specific cysteine oxidation in endogenous proteins using a differential alkylation and multiple reaction monitoring mass spectrometry approach
description
2010 nî lūn-bûn
@nan
2010 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի մարտին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Targeted quantitation of site- ...... ing mass spectrometry approach
@ast
Targeted quantitation of site- ...... ing mass spectrometry approach
@en
Targeted quantitation of site- ...... ing mass spectrometry approach
@nl
type
label
Targeted quantitation of site- ...... ing mass spectrometry approach
@ast
Targeted quantitation of site- ...... ing mass spectrometry approach
@en
Targeted quantitation of site- ...... ing mass spectrometry approach
@nl
prefLabel
Targeted quantitation of site- ...... ing mass spectrometry approach
@ast
Targeted quantitation of site- ...... ing mass spectrometry approach
@en
Targeted quantitation of site- ...... ing mass spectrometry approach
@nl
P2093
P2860
P1476
Targeted quantitation of site- ...... ing mass spectrometry approach
@en
P2093
Birgit Schilling
Bradford W Gibson
Christian Atsriku
Christopher C Benz
David J Britton
Jessica B Behring
Judith Campisi
Rachel L Puckett
Steven R Danielson
P2860
P304
P356
10.1074/MCP.M900643-MCP200
P577
2010-03-16T00:00:00Z