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Protein oxidation: role in signalling and detection by mass spectrometry
Corinne M Spickett
,
Andrew R Pitt
Aston Pharmacy School
College of Health and Life Sciences
School of Biosciences
Aston University
Research output
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Article
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peer-review
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Keyphrases
Protein Oxidation
100%
Mass Spectrometry
100%
Oxidative Post-translational Modification
100%
Tyrosine
66%
Methionine
33%
Oxidized Proteins
33%
Cysteine
33%
Disulfide
33%
Protein Tyrosine Phosphatase 1B (PTP1B)
33%
Thiols
33%
Dissociation
33%
Molecular Mechanism
33%
Biological Role
33%
Nitration
33%
Signal Modulation
33%
Tandem Mass Spectrometry
33%
Peptide Sequencing
33%
Mass Spectrometry Methods
33%
Analogous Method
33%
Specific Oxidation
33%
Neutral Loss
33%
Apoptosis Signal-regulating Kinase 1 (ASK1)
33%
Sulfenic Acid
33%
Keap1-Nrf2
33%
Specific Enrichment
33%
Cysteine Oxidation
33%
Chlorination
33%
Analytical Technologies
33%
Scan Loss
33%
S-nitrosylation
33%
Enrichment Method
33%
Reversible Modification
33%
Partial Oxidation
33%
Specific Labeling
33%
Methods for Detection
33%
Proline Hydroxylation
33%
Disulfide Bond Formation
33%
Physiological Processes
33%
HIF Signaling
33%
Transcription Factor Complex
33%
Non-reversible
33%
Precursor Ion Scan
33%
Biochemistry, Genetics and Molecular Biology
Posttranslational Modification
100%
Mass Spectrometry
100%
Disulfide
66%
Cysteine
66%
Kinase
33%
Phosphotransferase
33%
Protein Sequencing
33%
Tyrosine
33%
Precursor
33%
Thiol
33%
Methionine
33%
Protein Tyrosine Phosphatase
33%
Transcription Factors
33%
Hydroxylation
33%
Proline
33%
Tandem Mass Spectrometry
33%
Sulfenic Acid
33%
Transcription Factor Nrf2
33%
Physiological Process
33%
ASK1
33%
S-Nitrosylation
33%
Neuroscience
Mass Spectrometry
100%
Posttranslational Modification
100%
Cysteine
66%
Oxidizing Agent
33%
Kinase
33%
Protein Sequencing
33%
Thiol
33%
Transcription Factors
33%
Methionine
33%
Nitrotyrosine
33%
Hydroxylation
33%
Proline
33%
Transcription Factor Nrf2
33%
ASK1
33%
Protein Tyrosine Phosphatase
33%