ArticleInternational journal of molecular sciences2022
Protein Dimerization via Tyr Residues: Highlight of a Slow Process with Co-Existence of Numerous Intermediates and Final Products.
Article in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Myosin Post-Translational Modifications Associated With Critical Illness Myopathy.Acta physiologica (Oxford, England) · 2026Article
- Insights into heme degradation and hydrogen peroxide-induced dimerization of human neuroglobin.Bioscience reports · 2025Article
- From data extraction to analysis: a comparative study of ELISE capabilities in scientific literature.Frontiers in artificial intelligence · 2025Article
- Light from Afield: Fast, High-Resolution, and Layer-Free Deep Vat 3D Printing.Chemical reviews · 2024Review
- Photoradical-Mediated Catalyst-Independent Protein Cross-Link with Unusual Fluorescence Properties.Chembiochem : a European journal of chemical biology · 2023Article
- Spontaneous and Ionizing Radiation-Induced Aggregation of Human Serum Albumin: Dityrosine as a Fluorescent Probe.International journal of molecular sciences · 2022Article
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Authors and funding
5 authors.
Funding
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Abstract
Protein dimerization via tyrosine residues is a crucial process in response to an oxidative attack, which has been identified in many ageing-related pathologies. Recently, it has been found that for isolated tyrosine amino acid, dimerization occurs through three types of tyrosine-tyrosine crosslinks and leads to at least four final products. Herein, considering two protected tyrosine residues, tyrosine-containing peptides and finally proteins, we investigate the dimerization behavior of tyrosine when embedded in a peptidic sequence. After azide radical oxidation and by combining UPLC-MS and H/D exchange analyzes, we were able to evidence: (i) the slow kinetics of Michael Addition Dimers (MAD) formation, i.e., more than 48 h; (ii) the co-existence of intermediates and final cyclized dimer products; and (iii) the probable involvement of amide functions to achieve Michael additions even in proteins. This raises the question of the possible in vivo existence of both intermediates and final entities as well as their toxicity and the potential consequences on protein structure and/or function.
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