Pinpointing oxidative modifications in proteins—recent advances in analytical methods

Törnvall, Ulrika

doi:10.1039/c0ay00375a

Cited by 29 publications

(24 citation statements)

References 168 publications

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“…It is well established that oxidation of redox-sensitive residues such as methionine, cysteine, and tyrosine can promote protein misfolding and aggregation (27). Here, we show that NOR3-induced GAPDH aggregation is a useful example of how oxidation of a surface-exposed "linchpin" residue can drive protein misfolding and aggregation.…”

Section: Discussionmentioning

confidence: 82%

“…Peptide and protein lists were generated following Peptide Prophet and Protein Prophet analysis using a peptide false discovery rate of Ͻ1%. These modifications were selected based on a database search using Peaks Studio (version 6, Bioinformatics Solutions Inc.) against the same protein sequence database that included unbiased post-translational modification analysis using the PeaksPTM module (26) (data not shown) and the recommendations of Tornvall (27). All pep.xml files generated by the X!…”

Section: Site-directed Mutagenesis Of Gapdh-n-terminally Hismentioning

confidence: 99%

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Oxidation of an Exposed Methionine Instigates the Aggregation of Glyceraldehyde-3-phosphate Dehydrogenase

Samson

Knaupp

Kass

et al. 2014

Journal of Biological Chemistry

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Background: GAPDH is a glycolytic enzyme that aggregates during disease. Cysteine oxidation is the putative cause of aggregation. Whether GAPDH aggregation influences disease is unknown. Results: Mutating Met-46 renders GAPDH resistant to free radical-induced aggregation. Conclusion: Methionine oxidation, rather than cysteine oxidation, is a primary event that instigates GAPDH aggregation. Significance: Mutating Met-46 in vivo should elucidate whether GAPDH aggregation causally contributes to disease.

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Section: Discussionmentioning

confidence: 82%

Section: Site-directed Mutagenesis Of Gapdh-n-terminally Hismentioning

confidence: 99%

Oxidation of an Exposed Methionine Instigates the Aggregation of Glyceraldehyde-3-phosphate Dehydrogenase

Samson

Knaupp

Kass

et al. 2014

Journal of Biological Chemistry

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“…Most of these AA modifications can be used as useful markers for total protein oxidation. The most common methods to identify oxidized proteins rely on analytical chemistry instruments {e.g., GC or HPLC coupled with MS) [136,137]. More recently, fluorescence-based…”

Section: Detection Of Oxidative Damage To Proteinsmentioning

confidence: 99%

“…4A). Many AA residues can be oxidized by ROS [136], including Met, Cys, Trp, Tyr, His, Pro, Arg, and Lys by the hydroxylation of aromatic groups and aliphatic AA side chains, or the conversion of some AA residues to carbonyl derivatives. Most of these AA modifications can be used as useful markers for total protein oxidation.…”

Section: Detection Of Oxidative Damage To Proteinsmentioning

confidence: 99%

Electrocatalytic oxidation of tyrosines shows signal enhancement in label-free protein biosensors

Wei

Famouri

Guo

2012

TrAC Trends in Analytical Chemistry

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Label-free electrochemical (EC) protein biosensors that derive electrical signal from redox-active amino acid (AA) residues can avoid disruption of delicate protein structures, and thus provide a great opportunity to reveal valid information about protein functions. However, the challenge is that such a signal is usually very limited due to the sluggish EC reaction of free AAs on most common electrodes and slow electron-transfer rates from the deeply-buried AA residues in a protein to the electrode. Signal enhancement therefore becomes crucial. We first survey recent progress in this area.We present a signal-enhancing system that relies on the electrocatalytic oxidation of tyrosine mediated by osmium bipyridine or phenoxazine complexes. We describe several applications of label-free protein EC biosensors based on this detection principle for the analysis of protein functions, including the monitoring of protein-conformation change, study of ligand/protein binding, and detection of protein oxidative damage and protein phosphorylation.We describe related works on protein-function analysis using other signal-enhancing methods. The results suggest that labelfree EC protein biosensors are suitable for the rapid survey of protein functions due to their fast response, ease of integration, cost effectiveness and convenience. Proof-of-concept work on the application of our system is paving the way for bio-analytical detections and protein-function analysis in future work. ª

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“…Considering that the protein structure is associated to its biological function, several biological pathways may be affected by protein oxidation, damaging the organism. Hence, the study of the protein oxidation processes is of importance to develop techniques that allow identifying such modifications 161 and to use antioxidants to prevent these processes.…”

Section: Sensory Descriptive Analysis and Acceptancementioning

confidence: 99%

Improving meat quality through cattle feed enriched with mate extract: an integrated approach of the metabolic profile and redox chemistry of meat

Zawadzki¹

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Pinpointing oxidative modifications in proteins—recent advances in analytical methods

Cited by 29 publications

References 168 publications

Oxidation of an Exposed Methionine Instigates the Aggregation of Glyceraldehyde-3-phosphate Dehydrogenase

Oxidation of an Exposed Methionine Instigates the Aggregation of Glyceraldehyde-3-phosphate Dehydrogenase

Electrocatalytic oxidation of tyrosines shows signal enhancement in label-free protein biosensors

Improving meat quality through cattle feed enriched with mate extract: an integrated approach of the metabolic profile and redox chemistry of meat

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