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Mass spectrometry analysis of nitrotyrosine‐containing proteins
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Outgoing claims: the papers this work cites, builds on, or argues with.
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Enrichment and Detection of Tyrosine‐Nitrated Proteins
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Mass Spectrometry Approaches for the Molecular Characterization of Oxidatively/Nitrosatively Modified Proteins
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Protein nitration during defense response in Arabidopsis thaliana
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A simple and robust LC‐MS/MS method for quantification of free 3‐nitrotyrosine in human plasma from patients receiving on‐pump CABG surgery
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Investigation of tyrosine nitration in proteins by mass spectrometry
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Proteomic identification of nitrated brain proteins in traumatic brain‐injured rats treated postinjury with gamma‐glutamylcysteine ethyl ester: Insights into the role of elevation of glutathione as a potential therapeutic strategy for traumatic brain injury
inferredcites →https://doi.org/10.1002/mas.20006openalex-snapshot
Proteins as biomarkers of oxidative/nitrosative stress in diseases: The contribution of redox proteomics
inferredcites →https://doi.org/10.1002/mas.21404openalex-snapshot
Redox proteomics: from protein modifications to cellular dysfunction and disease
inferredcites →https://doi.org/10.1002/pmic.200800493openalex-snapshot
Quantitative identification of protein nitration sites
inferredcites →https://doi.org/10.1002/pmic.201000526openalex-snapshot
A stringent approach to improve the quality of nitrotyrosine peptide identifications
inferredcites →https://doi.org/10.1002/pro.311openalex-snapshot
Mechanism of glyceraldehyde‐3‐phosphate dehydrogenase inactivation by tyrosine nitration
inferredcites →https://doi.org/10.1002/psc.1298openalex-snapshot
Epitope motif of an anti‐nitrotyrosine antibody specific for tyrosine‐nitrated peptides revealed by a combination of affinity approaches and mass spectrometry
inferredcites →https://doi.org/10.1002/rcm.2676openalex-snapshot
Improved tandem mass spectrometric characterization of 3‐nitrotyrosine sites in peptides
inferredcites →https://doi.org/10.1002/rcm.3145openalex-snapshot
Investigation of tyrosine nitration and nitrosylation of angiotensin II and bovine serum albumin with electrospray ionization mass spectrometry
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Detection of 4-Hydroxy-2-Nonenal- and 3-Nitrotyrosine-Modified Proteins Using a Proteomics Approach
inferredcites →https://doi.org/10.1007/978-1-59745-562-6_10openalex-snapshot
Mass Spectrometric Identification of In Vivo Nitrotyrosine Sites in the Human Pituitary Tumor Proteome
inferredcites →https://doi.org/10.1007/978-1-60327-517-0_2openalex-snapshot
A Rapid and Selective Mass Spectrometric Method for the Identification of Nitrated Proteins
inferredcites →https://doi.org/10.1007/s00216-005-3145-0openalex-snapshot
The detection of nitrated tyrosine in neuropeptides: a MALDI matrix-dependent response
inferredcites →https://doi.org/10.1007/s00216-010-4280-9openalex-snapshot
Analysis of nitrated proteins and tryptic peptides by HPLC-chip-MS/MS: site-specific quantification, nitration degree, and reactivity of tyrosine residues
inferredcites →https://doi.org/10.1007/s00726-010-0585-4openalex-snapshot
Protein oxidation: role in signalling and detection by mass spectrometry
inferredcites →https://doi.org/10.1007/s00726-010-0604-5openalex-snapshot
Analytical methods for 3-nitrotyrosine quantification in biological samples: the unique role of tandem mass spectrometry
inferredcites →https://doi.org/10.1007/s00726-010-0693-1openalex-snapshot
Plasma nitroproteome of kidney disease patients
inferredcites →https://doi.org/10.1007/s13167-010-0028-zopenalex-snapshot
The use of variations in proteomes to predict, prevent, and personalize treatment for clinically nonfunctional pituitary adenomas
inferredcites →https://doi.org/10.1007/s13361-010-0041-4openalex-snapshot
Characterization of Tyrosine Nitration and Cysteine Nitrosylation Modifications by Metastable Atom-Activation Dissociation Mass Spectrometry
inferredcites →https://doi.org/10.1007/s13361-011-0095-yopenalex-snapshot
Identification of Nitrotyrosine Containing Peptides using Combined Fractional Diagonal Chromatography (COFRADIC) and Off-Line Nano-LC-MALDI
inferredcites →https://doi.org/10.1007/s13361-012-0461-4openalex-snapshot
When is Mass Spectrometry Combined with Affinity Approaches Essential? A Case Study of Tyrosine Nitration in Proteins
inferredcites →https://doi.org/10.1016/j.ab.2006.05.024openalex-snapshot
Nitroproteins from a human pituitary adenoma tissue discovered with a nitrotyrosine affinity column and tandem mass spectrometry
inferredcites →https://doi.org/10.1016/j.ab.2011.07.024openalex-snapshot
A methodology for simultaneous fluorogenic derivatization and boronate affinity enrichment of 3-nitrotyrosine-containing peptides
inferredcites →https://doi.org/10.1016/j.abb.2008.07.026openalex-snapshot
LDL protein nitration: Implication for LDL protein unfolding
inferredcites →https://doi.org/10.1016/j.abb.2008.12.012openalex-snapshot
Inactivation of rabbit muscle glycogen phosphorylase b by peroxynitrite revisited: Does the nitration of Tyr613 in the allosteric inhibition site control enzymatic function?
inferredcites →https://doi.org/10.1016/j.bbapap.2008.12.008openalex-snapshot
Proteomic analysis of protein tyrosine nitration after ischemia reperfusion injury: Mitochondria as the major target
inferredcites →https://doi.org/10.1016/j.bbapap.2009.10.010openalex-snapshot
Post-translational modifications of superoxide dismutase
inferredcites →https://doi.org/10.1016/j.bbrc.2004.10.169openalex-snapshot
The human pituitary nitroproteome: detection of nitrotyrosyl-proteins with two-dimensional Western blotting, and amino acid sequence determination with mass spectrometry
inferredcites →https://doi.org/10.1016/j.bbrc.2012.10.142openalex-snapshot
Differential hepatic protein tyrosine nitration of mouse due to aging – Effect on mitochondrial energy metabolism, quality control machinery of the endoplasmic reticulum and metabolism of drugs
inferredcites →https://doi.org/10.1016/j.exer.2010.01.014openalex-snapshot
Age-related accumulation of 3-nitrotyrosine and nitro-A2E in human Bruch's membrane
inferredcites →https://doi.org/10.1016/j.exger.2006.02.012openalex-snapshot
Age-associated tyrosine nitration of rat skeletal muscle glycogen phosphorylase b: characterization by HPLC–nanoelectrospray–Tandem mass spectrometry
inferredcites →https://doi.org/10.1016/j.freeradbiomed.2008.05.018openalex-snapshot
Role of copper,zinc-superoxide dismutase in catalyzing nitrotyrosine formation in murine liver
inferredcites →https://doi.org/10.1016/j.freeradbiomed.2009.08.020openalex-snapshot
Lipoprotein lipase is nitrated in vivo after lipopolysaccharide challenge
inferredcites →https://doi.org/10.1016/j.freeradbiomed.2010.01.010openalex-snapshot
Oxidative and nitrative modifications of α-enolase in cardiac proteins from diabetic rats
inferredcites →https://doi.org/10.1016/j.ijms.2006.06.009openalex-snapshot
Linear ion-trap mass spectrometric characterization of human pituitary nitrotyrosine-containing proteins
inferredcites →https://doi.org/10.1016/j.ijms.2008.08.020openalex-snapshot
MALDI-induced fragmentation of leucine enkephalin, nitro-Tyr-leucine enkaphalin, and d5-Phe-nitro-Tyr-leucine enkephalin
inferredcites →https://doi.org/10.1016/j.jasms.2009.10.011openalex-snapshot
Electron capture dissociation mass spectrometry of tyrosine nitrated peptides
inferredcites →https://doi.org/10.1016/j.jprot.2011.04.007openalex-snapshot
Confident identification of 3-nitrotyrosine modifications in mass spectral data across multiple mass spectrometry platforms
inferredcites →https://doi.org/10.1016/j.jprot.2011.11.025openalex-snapshot
Investigation of local primary structure effects on peroxynitrite-mediated tyrosine nitration using targeted mass spectrometry
inferredcites →https://doi.org/10.1016/j.neulet.2005.10.011openalex-snapshot
Tubulin nitration in human gliomas
inferredcites →https://doi.org/10.1016/j.taap.2008.12.010openalex-snapshot
Impaired mitochondrial respiration and protein nitration in the rat hippocampus after acute inhalation of combustion smoke
inferredcites →https://doi.org/10.1016/j.talanta.2009.02.002openalex-snapshot
Chemical labeling and enrichment of nitrotyrosine-containing peptides
inferredcites →https://doi.org/10.1016/s0006-291x(67)80033-0openalex-snapshot
Conversion of 3-nitrotyrosine to 3-aminotyrosine in peptides and proteins
inferredcites →https://doi.org/10.1016/s0076-6879(05)96015-1openalex-snapshot
Dynamic Assessment of Nitration Reactions In Vivo
inferredcites →https://doi.org/10.1016/s0076-6879(05)96016-3openalex-snapshot
Protein Nitration in Biological Aging: Proteomic and Tandem Mass Spectrometric Characterization of Nitrated Sites
inferredcites →https://doi.org/10.1016/s0076-6879(05)96023-0openalex-snapshot
Mapping Sites of Tyrosine Nitration by Matrix‐Assisted Laser Desorption/Ionization Mass Spectrometry
inferredcites →https://doi.org/10.1016/s0076-6879(07)00802-6openalex-snapshot
Detecting Nitrated Proteins by Proteomic Technologies
inferredcites →https://doi.org/10.1016/s0076-6879(07)00811-7openalex-snapshot
Quantitative Proteome Mapping of Nitrotyrosines
inferredcites →https://doi.org/10.1016/s1044-0305(01)00213-6openalex-snapshot
Analysis of peptides and proteins containing nitrotyrosine by matrix-assisted laser desorption/ionization mass spectrometry
inferredcites →https://doi.org/10.1021/ac0620361openalex-snapshot
Bidimensional Tandem Mass Spectrometry for Selective Identification of Nitration Sites in Proteins
inferredcites →https://doi.org/10.1021/ac102080dopenalex-snapshot
Selective Enrichment and Mass Spectrometric Identification of Nitrated Peptides Using Fluorinated Carbon Tags
inferredcites →https://doi.org/10.1021/ac202000vopenalex-snapshot
Enhanced Sample Multiplexing for Nitrotyrosine-Modified Proteins Using Combined Precursor Isotopic Labeling and Isobaric Tagging
inferredcites →https://doi.org/10.1021/ac301597ropenalex-snapshot
Reactive Nitrogen Oxide Species-Induced Post-Translational Modifications in Human Hemoglobin and the Association with Cigarette Smoking
inferredcites →https://doi.org/10.1021/ac9005099openalex-snapshot
Chemical Approach for Specific Enrichment and Mass Analysis of Nitrated Peptides
inferredcites →https://doi.org/10.1021/ac901176topenalex-snapshot
Preferentially Increased Nitration of α-Synuclein at Tyrosine-39 in a Cellular Oxidative Model of Parkinson’s Disease
inferredcites →https://doi.org/10.1021/bi00875a029openalex-snapshot
Tetranitromethane. A Reagent for the Nitration of Tyrosyl Residues in Proteins*
inferredcites →https://doi.org/10.1021/bi0352365openalex-snapshot
Generation of the R2 Subunit of Ribonucleotide Reductase by Intein Chemistry: Insertion of 3-Nitrotyrosine at Residue 356 as a Probe of the Radical Initiation Process
inferredcites →https://doi.org/10.1021/bi060474wopenalex-snapshot
Endogenously Nitrated Proteins in Mouse Brain: Links to Neurodegenerative Disease
inferredcites →https://doi.org/10.1021/bi7009713openalex-snapshot
Identification of a Denitrase Activity against Calmodulin in Activated Macrophages Using High-Field Liquid Chromatography−FTICR Mass Spectrometry
inferredcites →https://doi.org/10.1021/pr0606934openalex-snapshot
A Method for Selective Enrichment and Analysis of Nitrotyrosine-Containing Peptides in Complex Proteome Samples
inferredcites →https://doi.org/10.1021/pr900039copenalex-snapshot
Protein Tyrosine Nitration: Selectivity, Physicochemical and Biological Consequences, Denitration, and Proteomics Methods for the Identification of Tyrosine-Nitrated Proteins
inferredcites →https://doi.org/10.1021/tx3002753openalex-snapshot
Reaction of Human Cytochrome P450 3A4 with Peroxynitrite: Nitrotyrosine Formation on the Proximal Side Impairs Its Interaction with NADPH-Cytochrome P450 Reductase
inferredcites →https://doi.org/10.1021/tx700220eopenalex-snapshot
Peroxynitrite Inactivation of Human Cytochrome P450s 2B6 and 2E1: Heme Modification and Site-Specific Nitrotyrosine Formation
inferredcites →https://doi.org/10.1039/c0cp00623hopenalex-snapshot
Probing the mechanisms of electron capture dissociation mass spectrometry with nitrated peptides
inferredcites →https://doi.org/10.1042/bj20020339openalex-snapshot
Inducible nitric oxide synthase (NOS2) expressed in septic patients is nitrated on selected tyrosine residues: implications for enzymic activity
inferredcites →https://doi.org/10.1073/pnas.221269198openalex-snapshot
Proteomic method identifies proteins nitrated in vivo during inflammatory challenge
inferredcites →https://doi.org/10.1073/pnas.94.7.3211openalex-snapshot
Inflammation and NO x -induced nitration: Assay for 3-nitrotyrosine by HPLC with electrochemical detection
inferredcites →https://doi.org/10.1074/jbc.m109.099788openalex-snapshot
Endotoxin Conditioning Induces VCP/p97-mediated and Inducible Nitric-oxide Synthase-dependent Tyr284 Nitration in Protein Phosphatase 2A
inferredcites →https://doi.org/10.1074/jbc.m208916200openalex-snapshot
Nitric Oxide-dependent Generation of Reactive Species in Sickle Cell Disease
inferredcites →https://doi.org/10.1074/jbc.m413111200openalex-snapshot
Protein Nitration in a Mouse Model of Familial Amyotrophic Lateral Sclerosis
inferredcites →https://doi.org/10.1074/jbc.m501773200openalex-snapshot
Proteomic Analysis of Protein Nitration in Aging Skeletal Muscle and Identification of Nitrotyrosine-containing Sequences in Vivo by Nanoelectrospray Ionization Tandem Mass Spectrometry
inferredcites →https://doi.org/10.1074/jbc.m801196200openalex-snapshot
Post-translational Tyrosine Nitration of Eosinophil Granule Toxins Mediated by Eosinophil Peroxidase
inferredcites →https://doi.org/10.1074/jbc.m802691200openalex-snapshot
Protein Tyrosine Nitration of the Flavin Subunit Is Associated with Oxidative Modification of Mitochondrial Complex II in the Post-ischemic Myocardium
inferredcites →https://doi.org/10.1074/mcp.m100034-mcp200openalex-snapshot
Evidence That Light Modulates Protein Nitration in Rat Retina
inferredcites →https://doi.org/10.1074/mcp.m110.002923openalex-snapshot
Selective Chemoprecipitation and Subsequent Release of Tagged Species for the Analysis of Nitropeptides by Liquid Chromatography–Tandem Mass Spectrometry
inferredcites →https://doi.org/10.1074/mcp.m900259-mcp200openalex-snapshot
In Vitro and in Vivo Protein-bound Tyrosine Nitration Characterized by Diagonal Chromatography
inferredcites →https://doi.org/10.1074/mcp.m900321-mcp200openalex-snapshot
Endogenous 3,4-Dihydroxyphenylalanine and Dopaquinone Modifications on Protein Tyrosine
inferredcites →https://doi.org/10.1089/ars.2012.5058openalex-snapshot
Proteomic Approaches to Analyze Protein Tyrosine Nitration
inferredcites →https://doi.org/10.1093/cvr/cvq028openalex-snapshot
Cyclosporine A-induced nitration of tyrosine 34 MnSOD in endothelial cells: role of mitochondrial superoxide
inferredcites →https://doi.org/10.1093/jxb/erp263openalex-snapshot
Protein targets of tyrosine nitration in sunflower (Helianthus annuus L.) hypocotyls
inferredcites →https://doi.org/10.1093/molehr/gal071openalex-snapshot
Nitration of p38 MAPK in the placenta: association of nitration with reduced catalytic activity of p38 MAPK in pre-eclampsia
inferredcites →https://doi.org/10.1111/j.1365-2184.2010.00708.xopenalex-snapshot
Identification of tyrosine‐nitrated proteins in HT22 hippocampal cells during glutamate‐induced oxidative stress
inferredcites →https://doi.org/10.1111/jpi.12009openalex-snapshot
Ischemic injury promotes Keap1 nitration and disturbance of antioxidative responses in endothelial cells: a potential vasoprotective effect of melatonin
inferredcites →https://doi.org/10.1152/ajpcell.00518.2007openalex-snapshot
Shear stress influences spatial variations in vascular Mn-SOD expression: implication for LDL nitration
inferredcites →https://doi.org/10.1152/ajpheart.01030.2003openalex-snapshot
Proteomic identification of 3-nitrotyrosine-containing rat cardiac proteins: effects of biological aging
inferredcites →https://doi.org/10.1155/2013/580710openalex-snapshot
Pituitary Adenoma Nitroproteomics: Current Status and Perspectives
inferredcites →https://doi.org/10.1167/iovs.07-0432openalex-snapshot
SOD2 Knockdown Mouse Model of Early AMD
inferredcites →https://doi.org/10.1172/jci117607openalex-snapshot
Quantitation of nitrotyrosine levels in lung sections of patients and animals with acute lung injury.
inferredcites →https://doi.org/10.1186/1755-8794-3-13openalex-snapshot
Signaling pathway networks mined from human pituitary adenoma proteomics data
inferredcites →https://doi.org/10.1248/bpb.30.15openalex-snapshot
Nitration of Specific Tyrosine Residues of Cytochrome c Is Associated with Caspase-Cascade Inactivation
inferredcites →https://doi.org/10.1248/cpb.58.488openalex-snapshot
Efficient Identification and Quantification of Peptides Containing Nitrotyrosine by Matrix-Assisted Laser Desorption/Ionization Time-of-Flight Mass Spectrometry after Derivatization
inferredcites →https://doi.org/10.1255/ejms.777openalex-snapshot
Structural Characterisation of Tyrosine-Nitrated Peptides by Ultraviolet and Infrared Matrix-Assisted Laser Desorption/Ionisation Fourier Transform Ion Cyclotron Resonance Mass Spectrometry
inferredcites →https://doi.org/10.1515/cclm.2009.095openalex-snapshot
Determination of nitrotyrosine concentrations in plasma samples of diabetes mellitus patients by four different immunoassays leads to contradictive results and disqualifies the majority of the tests
inferredcites →https://doi.org/10.2353/ajpath.2008.080047openalex-snapshot
Enhanced Nitrosative Stress during Trypanosoma cruzi Infection Causes Nitrotyrosine Modification of Host Proteins
inferredcites →https://doi.org/10.3164/jcbn.08-185openalex-snapshot
Quantification of Modified Tyrosines in Healthy and Diabetic Human Urine using Liquid Chromatography/Tandem Mass Spectrometry
inferredcites →https://doi.org/10.4049/jimmunol.0900593openalex-snapshot
Site-Specific Carboxypeptidase B1 Tyrosine Nitration and Pathophysiological Implications following Its Physical Association with Nitric Oxide Synthase-3 in Experimental Sepsis
inferredcites →https://doi.org/10.4049/jimmunol.0902720openalex-snapshot
Protein Tyrosine Nitration of Aldolase in Mast Cells: A Plausible Pathway in Nitric Oxide-Mediated Regulation of Mast Cell Function
inferredcites →https://doi.org/10.4049/jimmunol.176.1.372openalex-snapshot
Nitration and Inactivation of IDO by Peroxynitrite
inferredcites →https://doi.org/10.4049/jimmunol.176.9.5587openalex-snapshot
Nitrotyrosine Proteome Survey in Asthma Identifies Oxidative Mechanism of Catalase Inactivation
inferredcites →https://doi.org/10.5483/bmbrep.2008.41.3.194openalex-snapshot
Nitrosative protein tyrosine modifications: biochemistry and functional significance
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Incoming claims: where this work appears in other papers’ reference lists and arguments.
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Proteomic Analysis of Human Esophageal Cancer Using Tandem Mass Tag Quantifications
inferred← citeshttps://doi.org/10.1186/s12920-014-0069-6openalex-snapshot
Heterogeneity analysis of the proteomes in clinically nonfunctional pituitary adenomas
inferred← citeshttps://doi.org/10.14800/ics.841openalex-snapshot
Hormone-related proteomic and functional variations in human nonfunctional pituitary adenomas
inferred← citeshttps://doi.org/10.1586/14789450.2015.1050384openalex-snapshot
Quantification of biopharmaceuticals and biomarkers in complex biological matrices: a comparison of liquid chromatography coupled to tandem mass spectrometry and ligand binding assays
inferred← citeshttps://doi.org/10.20900/mo.20170027openalex-snapshot
The Untapped Potential of Nitroproteomics for Medicine
inferred← citeshttps://doi.org/10.3109/10715762.2015.1007968openalex-snapshot
Exploring oxidative modifications of tyrosine: An update on mechanisms of formation, advances in analysis and biological consequences
inferred← citeshttps://doi.org/10.33612/diss.206613225openalex-snapshot
Pharmacokinetics and biotransformation of biopharmaceuticals
inferred← citeshttps://doi.org/10.3389/fendo.2016.00054openalex-snapshot
Human Pituitary Adenoma Proteomics: New Progresses and Perspectives
inferred← citeshttps://doi.org/10.3389/fendo.2018.00468openalex-snapshot
Prolactin Variants in Human Pituitaries and Pituitary Adenomas Identified With Two-Dimensional Gel Electrophoresis and Mass Spectrometry
inferred← citeshttps://doi.org/10.3389/fendo.2020.00026openalex-snapshot
Editorial: Molecular Network Study of Pituitary Adenomas
inferred← citeshttps://doi.org/10.3390/molecules23071667openalex-snapshot
NTyroSite: Computational Identification of Protein Nitrotyrosine Sites Using Sequence Evolutionary Features
inferred← citeshttps://doi.org/10.3791/56739openalex-snapshot
Two-dimensional Gel Electrophoresis Coupled with Mass Spectrometry Methods for an Analysis of Human Pituitary Adenoma Tissue Proteome
inferred← citeshttps://doi.org/10.5107/sccj.58.139openalex-snapshot
Extracellular Matrix Nitration: Role in Elastic Fiber Accumulation and Skin Photoaging
inferred← citeshttps://doi.org/10.5772/intechopen.76889openalex-snapshot
The Use of Gel Electrophoresis and Mass Spectrometry to Identify Nitroproteins in Nervous System Tumors
inferred← citeshttps://doi.org/10.5772/intechopen.77443openalex-snapshot
Bioinformatics Tools for Detection and Clinical Interpretation of Genomic Variations
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Recognition of Multiomics-Based Molecule-Pattern Biomarker for Precise Prediction, Diagnosis, and Prognostic Assessment in Cancer
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