ArticleAnalytical chemistry2006
Detailed map of oxidative post-translational modifications of human p21ras using Fourier transform mass spectrometry.
Article in Analytical chemistry, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
18 citing papers in PubMed, 34 citations in OpenAlex.
- Nitration in cancer signaling.Redox biology · 2026Review
- Oncogenic mutant KRAS inhibition through oxidation at cysteine 118.Molecular oncology · 2025Article
- Effects of acidic peptide size and sequence on trivalent praseodymium adduction and electron transfer dissociation mass spectrometry.Journal of mass spectrometry : JMS · 2017Article
- The Effects of Trivalent Lanthanide Cationization on the Electron Transfer Dissociation of Acidic Fibrinopeptide B and its Analogs.Journal of the American Society for Mass Spectrometry · 2016Article
- Endothelial Cell Redox Regulation of Ischemic Angiogenesis.Journal of cardiovascular pharmacology · 2016Review
- The Competitive influence of Li+, Na+, K+, Ag+, and H+ on the fragmentation of a PEGylated polymeric excipient.Journal of the American Society for Mass Spectrometry · 2015Article
- Multiple proteases to localize oxidation sites.PloS one · 2015Article
- Protein glutathionylation in cardiovascular diseases.International journal of molecular sciences · 2013Review
- Structural characterization of chlorophyll-a by high resolution tandem mass spectrometry.Journal of the American Society for Mass Spectrometry · 2013Article
- Autocatalytic nitration of prostaglandin endoperoxide synthase-2 by nitrite inhibits prostanoid formation in rat alveolar macrophages.Antioxidants & redox signaling · 2012Article
- The emerging paradigm of network medicine in the study of human disease.Circulation research · 2012Review
- Regulation of cell physiology and pathology by protein S-glutathionylation: lessons learned from the cardiovascular system.Antioxidants & redox signaling · 2012Review
- Short peptide induces an "uncultivable" microorganism to grow in vitro.Applied and environmental microbiology · 2008Article
- Probing the gas-phase folding kinetics of peptide ions by IR activated DR-ECD.Journal of the American Society for Mass Spectrometry · 2008Article
- Collisionally activated dissociation and electron capture dissociation provide complementary structural information for branched permethylated oligosaccharides.Journal of the American Society for Mass Spectrometry · 2008Article
- Thiol oxidation in signaling and response to stress: detection and quantification of physiological and pathophysiological thiol modifications.Free radical biology & medicine · 2007Review
- Quantification of oxidative posttranslational modifications of cysteine thiols of p21ras associated with redox modulation of activity using isotope-coded affinity tags and mass spectrometry.Free radical biology & medicine · 2007Article
- Use of a double resonance electron capture dissociation experiment to probe fragment intermediate lifetimes.Journal of the American Society for Mass Spectrometry · 2006Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
P21ras, the translation product of the most commonly mutated oncogene, is a small guanine nucleotide exchange protein. Oxidant-induced post-translational modifications of p21ras including S-nitrosation and S-glutathiolation have been demonstrated to modulate its activity. Structural characterization of this protein is critical to further understanding of the biological functions of p21ras. In this study, high-resolution and high mass accuracy Fourier transform mass spectrometry was utilized to map, in detail, the post-translational modifications of p21ras (H-ras) exposed to oxidants by combining bottom-up and top-down techniques. For peroxynitrite-treated p21ras, five oxidized methionines, five nitrated tyrosines, and at least two oxidized cysteines (including C118) were identified by "bottom-up" analysis, and the major oxidative modification of C118, Cys118-SO3H, was confirmed by several tandem mass spectrometry experiments. Additionally, "top-down" analysis was conducted on p21ras S-glutathiolated by oxidized glutathione and identified C118 as the major site of glutathiolation among the four surface cysteines. The present study provides a paradigm for an effective and efficient method not only for mapping post-translational modifications of proteins but also for predicting the relative selectivity and specificity of oxidative post-translational modifications, especially using top-down analysis.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.