Global Analysis of Protein Damage by the Lipid Electrophile 4-Hydroxy-2-nonenal
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Summary
Protein interaction network analysis indicated several subsystems impacted by endogenous electrophiles in oxidative stress, including the 26 S proteasomal and chaperonin containing TCP-1 systems involved in protein-folding and degradation, as well as the COP9 signalosome, translation initiation complex, and a large network of ribonucleoproteins.
- Type
- article
- Published
- 2009-04-01
- Cited by
- 142
- References
- 66
- Access
- Open access
- OpenAlex
- https://openalex.org/W2044357091
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:1502682
Keywords
Chemistry, Biochemistry, Biotinylation, Chaperonin, Lipid peroxidation
References
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- Endogenous DNA damage and mutation.
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- Cell surface engineering by a modified Staudinger reaction.
- Protein targets of reactive electrophiles in human liver microsomes.
- Long-lived 4-oxo-2-enal-derived apparent lysine michael adducts are actually the isomeric 4-ketoamides.
- DNA damage from micronutrient deficiencies is likely to be a major cause of cancer.
- 4-Oxo-2-nonenal is both more neurotoxic and more protein reactive than 4-hydroxy-2-nonenal.
- Protein interaction networks beyond artifacts
- Proteomic parsimony through bipartite graph analysis improves accuracy and transparency.
- Is oxidative damage the fundamental pathogenic mechanism of Alzheimer's and other neurodegenerative diseases?
- A model for random sampling and estimation of relative protein abundance in shotgun proteomics.
- Protein Adducts Generated from Products of Lipid Oxidation: Focus on HNE and ONE
- Induction of redox instability of bovine myoglobin by adduction with 4-hydroxy-2-nonenal.
- Free radicals, antioxidants, and human disease: curiosity, cause, or consequence?
- Immunohistochemical detection of 4-hydroxynonenal protein adducts in Parkinson disease.
- Covalent adduction of human serum albumin by 4-hydroxy-2-nonenal: kinetic analysis of competing alkylation reactions.
- Mass spectroscopic characterization of protein modification by 4-hydroxy-2-(E)-nonenal and 4-oxo-2-(E)-nonenal.
Cited by
- Biotinylated Probes for Analysis of Protein Modification by Electrophiles
- An Azido-Biotin Reagent for Use in the Isolation of Protein Adducts of Lipid-derived Electrophiles by Streptavidin Catch and Photorelease*
- Cardiovascular Redox and Ox Stress Proteomics
- Chemoproteomic profiling of targets of lipid-derived electrophiles by bioorthogonal aminooxy probe
- Characterization of the product specificity and kinetic mechanism of protein arginine methyltransferase 1
- Mass spectrometry approaches for the redox characterization of protein cysteine residues the case of the transcription factor Pax-8.
- Targeted Protein Capture for Analysis of Electrophile-Protein Adducts
- Affinity enrichment and mass spectrometric quantitation of protein carbonyls
- Integrated Haematological Profiles of Redox Status, Lipid, and Inflammatory Protein Biomarkers in Benign Obesity and Unhealthy Obesity with Metabolic Syndrome
- Measuring Electrophile Stress
- Protein carbonylation as a major hallmark of oxidative damage: update of analytical strategies.
- Global, in situ, site-specific analysis of protein S-sulphenylation
- Endogenous Generation and Signaling Actions of Omega-3 Fatty Acid Electrophilic Derivatives
- 4-Hydroxy-nonenal—A Bioactive Lipid Peroxidation Product
- Increased hepatocellular protein carbonylation in human end-stage alcoholic cirrhosis
- Impact of 4‐hydroxynonenal on matrix metalloproteinase‐9 regulation in lipopolysaccharide‐stimulated RAW 264.7 cells
- Chemical approaches to detect and analyze protein sulfenic acids
- Modulation of Protein Quality Control Systems as Novel Mechanisms Underlying Functionality of Food Phytochemicals
- Probing lipid-protein adduction with alkynyl surrogates: application to Smith-Lemli-Opitz syndrome[S]
- The Electrophile Responsive Proteome: Integrating Proteomics and Lipidomics with Cellular Function
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