ArticleRedox biology2019
Identification and quantification of sites of nitration and oxidation in the key matrix protein laminin and the structural consequences of these modifications.
Article in Redox biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed, 21 citations in OpenAlex.
- Modification of extracellular matrix proteins by oxidants and electrophiles.Biochemical Society transactions · 2024Review
- Identification and quantification of protein nitration sites in human coronary artery smooth muscle cells in the absence and presence of peroxynitrous acid/peroxynitrite.Redox biology · 2023Article
- Designing Cardiovascular Implants Taking in View the Endothelial Basement Membrane.International journal of molecular sciences · 2021Review
- Secondary Formation of Aromatic Nitroderivatives of Environmental Concern: Photonitration Processes Triggered by the Photolysis of Nitrate and Nitrite Ions in Aqueous Solution.Molecules (Basel, Switzerland) · 2021Review
- Modifying the Tumour Microenvironment: Challenges and Future Perspectives for Anticancer Plasma Treatments.Cancers · 2019Review
- Uncommon posttranslational modifications in proteomics: ADP-ribosylation, tyrosine nitration, and tyrosine sulfation.Mass spectrometry reviewsReview
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Laminin is a major protein of the basement membrane (BM), a specialized extracellular matrix (ECM) of the artery wall. The potent oxidizing and nitrating agent peroxynitrous acid (ONOOH) is formed at sites of inflammation, and data implicate ONOOH in ECM damage and cardiovascular disease. Co-localization of 3-nitrotyrosine, a product of ONOOH-mediated tyrosine (Tyr) modification, and laminin has been reported in human atherosclerotic lesions. The sites and consequences of 3-nitrotyrosine (and related nitrated tryptophan) formation on laminin, it's self-assembly and cell interactions are poorly understood. In this study murine laminin-111 was exposed to ONOOH (1-500-fold molar excess). Nitration sites were mapped and quantified using LC-MS/MS. Mono-nitration was detected at 148 sites (126 Tyr, 22 Trp), and di-nitration at 14 sites. Label-free quantification showed enhanced nitration with increasing oxidant doses. Tyr nitration was ∼10-fold greater than at Trp. CO
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Registered trials
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