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• W2063710860 abstract "Models for exploring tyrosine nitration in proteins have been created based on 3D structural features of 20 proteins for which high-resolution X-ray crystallographic or NMR data are available and for which nitration of 35 total tyrosines has been experimentally proven under oxidative stress. Factors suggested in previous work to enhance nitration were examined with quantitative structural descriptors. The role of neighboring acidic and basic residues is complex: for the majority of tyrosines that are nitrated the distance to the heteroatom of the closest charged side chain corresponds to the distance needed for suspected nitrating species to form hydrogen bond bridges between the tyrosine and that charged amino acid. This suggests that such bridges play a very important role in tyrosine nitration. Nitration is generally hindered for tyrosines that are buried and for those tyrosines for which there is insufficient space for the nitro group. For in vitro nitration, closed environments with nearby heteroatoms or unsaturated centers that can stabilize radicals are somewhat favored. Four quantitative structure-based models, depending on the conditions of nitration, have been developed for predicting site-specific tyrosine nitration. The best model, relevant for both in vitro and in vivo cases, predicts 30 of 35 tyrosine nitrations (positive predictive value) and has a sensitivity of 60/71 (11 false positives)." @default.
• W2063710860 created "2016-06-24" @default.
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• W2063710860 date "2011-03-01" @default.
• W2063710860 modified "2023-10-16" @default.
• W2063710860 title "Factors influencing protein tyrosine nitration—structure-based predictive models" @default.
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• W2063710860 doi "https://doi.org/10.1016/j.freeradbiomed.2010.12.016" @default.
• W2063710860 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3039091" @default.
• W2063710860 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/21172423" @default.
• W2063710860 hasPublicationYear "2011" @default.
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