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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

https://doi.org/10.1042/bj20100633
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Outgoing claims: the papers this work cites, builds on, or argues with.

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Probability-based protein identification by searching sequence databases using mass spectrometry data
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Sample pooling in 2‐D gel electrophoresis: A new approach to reduce nonspecific expression background
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Inactivation of oxidized and S -nitrosylated mitochondrial proteins in alcoholic fatty liver of rats
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Evaluation of saturation labelling two‐dimensional difference gel electrophoresis fluorescent dyes
inferredcites →https://doi.org/10.1002/pmic.200300681openalex-snapshot
Determining a significant change in protein expression with DeCyder™ during a pair‐wise comparison using two‐dimensional difference gel electrophoresis
inferredcites →https://doi.org/10.1002/pmic.200500083openalex-snapshot
Maximising sensitivity for detecting changes in protein expression: Experimental design using minimal CyDyes
inferredcites →https://doi.org/10.1002/pmic.200800485openalex-snapshot
Investigating sample pooling strategies for DIGE experiments to address biological variability
inferredcites →https://doi.org/10.1006/niox.2000.0272openalex-snapshot
Kinetics and Mechanism of the Decomposition of S-Nitrosoglutathione by l-Ascorbic Acid and Copper Ions in Aqueous Solution to Produce Nitric Oxide
inferredcites →https://doi.org/10.1007/s00216-005-3126-3openalex-snapshot
The development of the DIGE system: 2D fluorescence difference gel analysis technology
inferredcites →https://doi.org/10.1016/0003-9861(85)90603-4openalex-snapshot
Aldehyde dehydrogenase activity as the rate-limiting factor for acetaldehyde metabolism in rat liver
inferredcites →https://doi.org/10.1016/0014-5793(96)00560-1openalex-snapshot
Role of ascorbic acid in the metabolism of S‐nitroso‐glutathione
inferredcites →https://doi.org/10.1016/b978-0-408-70360-4.50009-2openalex-snapshot
PREPARATION OF MITOCHONDRIA FROM ANIMAL TISSUES AND YEASTS
inferredcites →https://doi.org/10.1016/j.bbrc.2005.12.013openalex-snapshot
Ascorbic acid reduction of microtubule protein disulfides and its relevance to protein S-nitrosylation assays
inferredcites →https://doi.org/10.1016/j.febslet.2005.09.082openalex-snapshot
Inhibition of mitochondrial aldehyde dehydrogenase by nitric oxide‐mediated S‐nitrosylation
inferredcites →https://doi.org/10.1016/j.freeradbiomed.2006.03.006openalex-snapshot
An ascorbate-dependent artifact that interferes with the interpretation of the biotin switch assay
inferredcites →https://doi.org/10.1016/j.freeradbiomed.2007.01.007openalex-snapshot
Mitochondrial aconitase reaction with nitric oxide, S-nitrosoglutathione, and peroxynitrite: Mechanisms and relative contributions to aconitase inactivation
inferredcites →https://doi.org/10.1016/j.freeradbiomed.2007.12.032openalex-snapshot
Copper dependence of the biotin switch assay: Modified assay for measuring cellular and blood nitrosated proteins
inferredcites →https://doi.org/10.1016/j.niox.2008.07.007openalex-snapshot
Selective fluorescent labeling of S-nitrosothiols (S-FLOS): A novel method for studying S-nitrosation
inferredcites →https://doi.org/10.1016/j.yjmcc.2007.01.010openalex-snapshot
Cardioprotection and mitochondrial S-nitrosation: Effects of S-nitroso-2-mercaptopropionyl glycine (SNO-MPG) in cardiac ischemia–reperfusion injury
inferredcites →https://doi.org/10.1016/j.yjmcc.2009.01.012openalex-snapshot
In vivo cardioprotection by S-nitroso-2-mercaptopropionyl glycine
inferredcites →https://doi.org/10.1016/s0008-6363(02)00675-2openalex-snapshot
The cardioprotective and mitochondrial depolarising properties of exogenous nitric oxide in mouse heart
inferredcites →https://doi.org/10.1016/s0021-9258(18)57021-6openalex-snapshot
DETERMINATION OF SERUM PROTEINS BY MEANS OF THE BIURET REACTION
inferredcites →https://doi.org/10.1016/s0076-6879(02)49317-2openalex-snapshot
Aconitase: Sensitive target and measure of superoxide
inferredcites →https://doi.org/10.1016/s0076-6879(08)04419-4openalex-snapshot
Chapter 19 Measuring Redox Changes to Mitochondrial Protein Thiols With Redox Difference Gel Electrophoresis (Redox‐Dige)
inferredcites →https://doi.org/10.1021/pr800233ropenalex-snapshot
Quantitative Analysis of Redox-Sensitive Proteome with DIGE and ICAT
inferredcites →https://doi.org/10.1038/379466a0openalex-snapshot
Femtomole sequencing of proteins from polyacrylamide gels by nano-electrospray mass spectrometry
inferredcites →https://doi.org/10.1038/nrm762openalex-snapshot
Does nitric oxide modulate mitochondrial energy generation and apoptosis?
inferredcites →https://doi.org/10.1038/nsb0498-267openalex-snapshot
Enzyme inactivation through sulfhydryl oxidation by physiologic NO-carriers
inferredcites →https://doi.org/10.1042/bj20031758openalex-snapshot
Mechanisms of the interaction of nitroxyl with mitochondria
inferredcites →https://doi.org/10.1042/bj20051916openalex-snapshot
Localization of GRP78 to mitochondria under the unfolded protein response
inferredcites →https://doi.org/10.1042/bj20081386openalex-snapshot
How mitochondria produce reactive oxygen species
inferredcites →https://doi.org/10.1042/bj2410883openalex-snapshot
Reactions of electron-transfer flavoprotein and electron-transfer flavoprotein: ubiquinone oxidoreductase
inferredcites →https://doi.org/10.1046/j.1432-1033.2003.03947.xopenalex-snapshot
Mitochondrial β‐oxidation
inferredcites →https://doi.org/10.1073/pnas.0903250106openalex-snapshot
A mitochondria-targeted S -nitrosothiol modulates respiration, nitrosates thiols, and protects against ischemia-reperfusion injury
inferredcites →https://doi.org/10.1074/jbc.273.46.30255openalex-snapshot
Formation of S-Nitrosothiols via Direct Nucleophilic Nitrosation of Thiols by Peroxynitrite with Elimination of Hydrogen Peroxide
inferredcites →https://doi.org/10.1074/jbc.m109.025882openalex-snapshot
Mitochondrial Localization of PARP-1 Requires Interaction with Mitofilin and Is Involved in the Maintenance of Mitochondrial DNA Integrity
inferredcites →https://doi.org/10.1074/jbc.m109.054346openalex-snapshot
Lack of Oxygen Deactivates Mitochondrial Complex I
inferredcites →https://doi.org/10.1074/jbc.m308504200openalex-snapshot
Docking of Endothelial Nitric Oxide Synthase (eNOS) to the Mitochondrial Outer Membrane
inferredcites →https://doi.org/10.1074/jbc.m512203200openalex-snapshot
Persistent S-Nitrosation of Complex I and Other Mitochondrial Membrane Proteins by S-Nitrosothiols but Not Nitric Oxide or Peroxynitrite
inferredcites →https://doi.org/10.1074/jbc.m702294200openalex-snapshot
Mitochondrial Complex II in the Post-ischemic Heart
inferredcites →https://doi.org/10.1074/jbc.m703591200openalex-snapshot
Detection of Reactive Oxygen Species-sensitive Thiol Proteins by Redox Difference Gel Electrophoresis
inferredcites →https://doi.org/10.1091/mbc.e04-08-0697openalex-snapshot
The Mitochondrial Inner Membrane Protein Mitofilin Controls Cristae Morphology
inferredcites →https://doi.org/10.1093/bioinformatics/bth193openalex-snapshot
DNA microarray normalization methods can remove bias from differential protein expression analysis of 2D difference gel electrophoresis results
inferredcites →https://doi.org/10.1093/emboj/20.14.3676openalex-snapshot
Myosin VI isoform localized to clathrin‐coated vesicles with a role in clathrin‐mediated endocytosis
inferredcites →https://doi.org/10.1093/jxb/erj141openalex-snapshot
Methods of quantitative proteomics and their application to plant organelle characterization
inferredcites →https://doi.org/10.1111/j.1471-4159.1986.tb00768.xopenalex-snapshot
Brain α‐Ketoglutarate Dehydrogenase Complex: Kinetic Properties, Regional Distribution, and Effects of Inhibitors
inferredcites →https://doi.org/10.1111/j.1742-4658.2010.07576.xopenalex-snapshot
Cysteine residues exposed on protein surfaces are the dominant intramitochondrial thiol and may protect against oxidative damage
inferredcites →https://doi.org/10.1146/annurev.pharmtox.42.092501.104328openalex-snapshot
The Biochemistry and Physiology of S-Nitrosothiols
inferredcites →https://doi.org/10.1161/circresaha.107.155879openalex-snapshot
Preconditioning Results in S -Nitrosylation of Proteins Involved in Regulation of Mitochondrial Energetics and Calcium Transport

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

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Mitochondrial Thiols in Antioxidant Protection and Redox Signaling: Distinct Roles for Glutathionylation and Other Thiol Modifications
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Selective Vulnerability of Synaptic Signaling and Metabolism to Nitrosative Stress
inferred← citeshttps://doi.org/10.1089/ars.2012.4706openalex-snapshot
Cardiovascular Redox and Ox Stress Proteomics
inferred← citeshttps://doi.org/10.1089/ars.2012.4788openalex-snapshot
Sensing Hypoxia by Mitochondria: A Unifying Hypothesis Involving S-Nitrosation
inferred← citeshttps://doi.org/10.1089/ars.2012.5056openalex-snapshot
S -Nitrosylation: Specificity, Occupancy, and Interaction with Other Post-Translational Modifications
inferred← citeshttps://doi.org/10.1089/ars.2017.7123openalex-snapshot
The Incomplete Glutathione Puzzle: Just Guessing at Numbers and Figures?
inferred← citeshttps://doi.org/10.1089/ars.2019.7916openalex-snapshot
Nitric Oxide-Dependent Protein Post-Translational Modifications Impair Mitochondrial Function and Metabolism to Contribute to Neurodegenerative Diseases
inferred← citeshttps://doi.org/10.1089/ars.2019.7921openalex-snapshot
Anaerobic Transcription by OxyR: A Novel Paradigm for Nitrosative Stress
inferred← citeshttps://doi.org/10.1093/cvr/cvq277openalex-snapshot
What can we learn about cardioprotection from the cardiac mitochondrial proteome?
inferred← citeshttps://doi.org/10.1111/bph.12405openalex-snapshot
Mitochondrially targeted nitro‐linoleate: a new tool for the study of cardioprotection
inferred← citeshttps://doi.org/10.1111/bph.12975openalex-snapshot
Redox signalling and cardioprotection: translatability and mechanism
inferred← citeshttps://doi.org/10.1111/jpi.12099openalex-snapshot
The beneficial effects of melatonin against heart mitochondrial impairment during sepsis: inhibition of i NOS and preservation of n NOS
inferred← citeshttps://doi.org/10.1152/ajpendo.00510.2010openalex-snapshot
Nitrosative modifications of protein and lipid signaling molecules by reactive nitrogen species
inferred← citeshttps://doi.org/10.1152/ajpheart.00997.2010openalex-snapshot
Characterization of potentialS-nitrosylation sites in the myocardium
inferred← citeshttps://doi.org/10.1155/2018/1435934openalex-snapshot
Mitoproteomics: Tackling Mitochondrial Dysfunction in Human Disease
inferred← citeshttps://doi.org/10.1161/circresaha.110.232173openalex-snapshot
Simultaneous Measurement of Protein Oxidation and S -Nitrosylation During Preconditioning and Ischemia/Reperfusion Injury With Resin-Assisted Capture
inferred← citeshttps://doi.org/10.1177/0271678x18770331openalex-snapshot
Deactivation of mitochondrial complex I after hypoxia–ischemia in the immature brain
inferred← citeshttps://doi.org/10.1177/1535370214522935openalex-snapshot
Protein S-nitrosylation in preconditioning and postconditioning
inferred← citeshttps://doi.org/10.1186/1471-2229-13-61openalex-snapshot
Vinyl sulfone silica: application of an open preactivated support to the study of transnitrosylation of plant proteins by S-nitrosoglutathione
inferred← citeshttps://doi.org/10.1186/s40478-021-01224-4openalex-snapshot
Reappraisal of metabolic dysfunction in neurodegeneration: Focus on mitochondrial function and calcium signaling
inferred← citeshttps://doi.org/10.1201/b12308-24openalex-snapshot
_-Ketoglutarate Dehydrogenase Complex in Neurodegeneration
inferred← citeshttps://doi.org/10.1210/en.2013-2174openalex-snapshot
Endogenous NO Upon Estradiol-17β Stimulation and NO Donor Differentially Regulate Mitochondrial S-Nitrosylation in Endothelial Cells
inferred← citeshttps://doi.org/10.1210/me.2014-1297openalex-snapshot
S-Nitrosylation of Cofilin-1 Mediates Estradiol-17β-Stimulated Endothelial Cytoskeleton Remodeling
inferred← citeshttps://doi.org/10.1242/jcs.098475openalex-snapshot
Mitochondrial redox signalling at a glance
inferred← citeshttps://doi.org/10.1371/journal.pone.0177315openalex-snapshot
Adenosine A1 receptor activation increases myocardial protein S-nitrosothiols and elicits protection from ischemia-reperfusion injury in male and female hearts
inferred← citeshttps://doi.org/10.14336/ad.2024.0099openalex-snapshot
The Role of Protein S-Nitrosylation in Mitochondrial Quality Control in Central Nervous System Diseases
inferred← citeshttps://doi.org/10.1515/hsz-2020-0321openalex-snapshot
Prediction and analysis of redox-sensitive cysteines using machine learning and statistical methods
inferred← citeshttps://doi.org/10.1515/irm-2013-0004openalex-snapshot
The complex mechanistic aspects of redox-active compounds, commonly regarded as SOD mimics
inferred← citeshttps://doi.org/10.1586/epr.11.74openalex-snapshot
Proteomics insights into deregulated proteinS-nitrosylation and disease
inferred← citeshttps://doi.org/10.3109/10715762.2012.684244openalex-snapshot
SNO spectral counting (SNOSC), a label-free proteomic method for quantification of changes in levels of protein S-nitrosation
inferred← citeshttps://doi.org/10.3109/10715762.2015.1110241openalex-snapshot
Measurement and meaning of cellular thiol:disufhide redox status
inferred← citeshttps://doi.org/10.3390/antiox8090404openalex-snapshot
S-Nitrosylation: An Emerging Paradigm of Redox Signaling
inferred← citeshttps://doi.org/10.3390/cells14090653openalex-snapshot
Targeted Redox Regulation α-Ketoglutarate Dehydrogenase Complex for the Treatment of Human Diseases
inferred← citeshttps://doi.org/10.3390/ijms22052563openalex-snapshot
A Commonly Used Biocide 2-N-octyl-4-isothiazolin-3-oneInduces Blood–Brain Barrier Dysfunction via Cellular Thiol Modification and Mitochondrial Damage
inferred← citeshttps://doi.org/10.3390/pharmaceutics12111122openalex-snapshot
Mitochondria-Targeted Drug Delivery in Cardiovascular Disease: A Long Road to Nano-Cardio Medicine
inferred← citeshttps://doi.org/10.3390/pharmaceutics14122760openalex-snapshot
The Therapeutic Strategies Targeting Mitochondrial Metabolism in Cardiovascular Disease
inferred← citeshttps://doi.org/10.4103/2319-4170.155591openalex-snapshot
The emerging theme of redox bioenergetics in health and disease
inferred← citeshttps://doi.org/10.5772/46075openalex-snapshot
Trends in the Evaluation of Lipid Peroxidation Processes
inferred← citeshttps://doi.org/10.5812/jjm.22935openalex-snapshot
Distributions and Types of Multidrug-Resistant Acinetobacter baumannii in Different Departments of a General Hospital
inferred← citeshttps://doi.org/10.70675/9f9dbd9bzf0dez4f8fz89a2zb149f08eccc9openalex-snapshot
Analyse de la S-nitrosylation des protéines chez Arabidopsis thaliana en situations de stress
inferred← citeshttps://doi.org/10.7554/elife.58573openalex-snapshot
ALKBH7 mediates necrosis via rewiring of glyoxal metabolism
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