Immuno-Affinity Study of Oxidative Tyrosine Containing Peptides

Darie-Ion, Laura; Neamţu, Andrei; Iliescu, Radu; Petre, Brînduşa Alina

doi:10.1007/s10989-021-10329-2

Cited by 1 publication

(3 citation statements)

References 45 publications

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“…In an earlier study, an anti-3-nTyr antibody exhibited a higher affinity toward synthetic nitropeptides containing basic residues N-terminal to nTyr (Drǎguşanu et al, 2011). Additionally, anti-3-nTyr antibodies demonstrate high-affinity binding to both nitro and hydroxy-Tyr containing synthetic peptides lowering the specificity towards nTyr (Darie- Ion et al, 2022). These studies exhibit the need for a high affinity pan-specific anti-3-nTyr antibody regardless of the peptide sequence to permit unbiased profiling of nitroproteome (Drǎguşanu et al, 2011;Zhao et al, 2017).…”

Section: Tyrosine Nitration: Enrichment Strategiesmentioning

confidence: 99%

“…Zhang et al, 2007). There is no consensus motif for Tyr nitration, but several studies have shown that nTyrs are present in flexible loops and turns and in more solvent-accessible regions (Bartesaghi et al, 2007;Darie-Ion et al, 2022;Ion et al, 2020;Sacksteder et al, 2006). The presence of a nearby charged residue also favors Tyr nitration as it enables the formation of hydrogen bonds and salt bridges (Batthyány et al, 2017).…”

Section: Tyrosine Nitrationmentioning

confidence: 99%

“…This leads to structural changes, disrupts hydrogen bonding interactions, alters protein–protein interactions, inactivates enzymes and receptors, and impedes the phosphorylation of Tyr residues (Bandookwala & Sengupta, 2020; Zhan et al, 2015; Q. Zhang et al, 2007). There is no consensus motif for Tyr nitration, but several studies have shown that nTyrs are present in flexible loops and turns and in more solvent‐accessible regions (Bartesaghi et al, 2007; Darie‐Ion et al, 2022; Ion et al, 2020; Sacksteder et al, 2006). The presence of a nearby charged residue also favors Tyr nitration as it enables the formation of hydrogen bonds and salt bridges (Batthyány et al, 2017).…”

Section: Posttranslational Modifications Of Tyrosinementioning

confidence: 99%

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Uncommon posttranslational modifications in proteomics: ADP‐ribosylation, tyrosine nitration, and tyrosine sulfation

Bashyal

Brodbelt

2022

Mass Spectrometry Reviews

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Posttranslational modifications (PTMs) are covalent modifications of proteins that modulate the structure and functions of proteins and regulate biological processes. The development of various mass spectrometry‐based proteomics workflows has facilitated the identification of hundreds of PTMs and aided the understanding of biological significance in a high throughput manner. Improvements in sample preparation and PTM enrichment techniques, instrumentation for liquid chromatography‐tandem mass spectrometry (LC‐MS/MS), and advanced data analysis tools enhance the specificity and sensitivity of PTM identification. Highly prevalent PTMs like phosphorylation, glycosylation, acetylation, ubiquitinylation, and methylation are extensively studied. However, the functions and impact of less abundant PTMs are not as well understood and underscore the need for analytical methods that aim to characterize these PTMs. This review focuses on the advancement and analytical challenges associated with the characterization of three less common but biologically relevant PTMs, specifically, adenosine diphosphate‐ribosylation, tyrosine sulfation, and tyrosine nitration. The advantages and disadvantages of various enrichment, separation, and MS/MS techniques utilized to identify and localize these PTMs are described.

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