ArticleThe Journal of biological chemistry2019
Neutrophil myeloperoxidase harbors distinct site-specific peculiarities in its glycosylation.
Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers, 1 of them a synthesis that pooled it.
What it found
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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
28 citing papers in PubMed, 1 synthesis or guideline pooled it, 44 citations in OpenAlex.
- Recent Advances in Software Tools for More Generic and Precise Intact Glycopeptide Analysis.Molecular & cellular proteomics : MCP · 2021Pooled it
- Mapping ST3GAL transferase specificities in the glycosylation landscape of N/TERT-1 keratinocytes using Glycogenomics and mass spectrometry.Glycobiology · 2026Article
- Myeloperoxidase as a therapeutic target for oxidative damage in Alzheimer's disease.Journal of enzyme inhibition and medicinal chemistry · 2025Review
- Glycoproteomics analysis of colorectal cancer reveals differential alterations of glycoproteins and glycans.Analytical and bioanalytical chemistry · 2025Article
- Glycosylation in kidney diseases.Precision clinical medicine · 2025Review
- Anti-myeloperoxidase IgM B cells in anti-neutrophil cytoplasmic antibody-associated vasculitis.Nature communications · 2025Article
- The ferroform and glycoform landscape of human milk lactoferrin dissected through hybrid mass spectrometric approaches.Frontiers in nutrition · 2025Article
- Functional role of IL-19 in a mouse model of L-arginine-induced pancreatitis and related lung injury.Experimental animals · 2024Article
- Protein N-glycosylation in the bronchoalveolar space differs between never-smokers and long-term smokers with and without COPD.Glycobiology · 2023Article
- Ceruloplasmin Reduces the Lactoferrin/Oleic Acid Antitumor Complex-Mediated Release of Heme-Containing Proteins from Blood Cells.International journal of molecular sciences · 2023Article
- Glycoproteome remodeling and organelle-specificProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Coating and Corruption of Human Neutrophils by Bacterial Outer Membrane Vesicles.Microbiology spectrum · 2022Article
- Native glycosylation and binding of the antidepressant paroxetine in a low-resolution crystal structure of human myeloperoxidase.Acta crystallographica. Section D, Structural biology · 2022Article
- Article
- N-acetyl-β-D-hexosaminidases mediate the generation of paucimannosidic proteins via a putative noncanonical truncation pathway in human neutrophils.Glycobiology · 2022Article
- Finding the sweet spot: glycosylation mediated regulation of intestinal inflammation.Mucosal immunology · 2022Review
- Mass spectrometry-based N-glycosylation analysis in kidney disease.Frontiers in molecular biosciences · 2022Review
- New prognostic factors and scoring system for patients with acute myeloid leukemia.Oncology letters · 2021Article
- The many roles of myeloperoxidase: From inflammation and immunity to biomarkers, drug metabolism and drug discovery.Redox biology · 2021Review
- Neutrophil azurophilic granule glycoproteins are distinctively decorated by atypical pauci- and phosphomannose glycans.Communications biology · 2021Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Anti-neutrophil cytoplasmic autoantibodies (ANCAs) are directed against lysosomal components of neutrophils. ANCAs directed to proteinase 3 and myeloperoxidase (MPO) in particular are associated with distinct forms of small vessel vasculitides. MPO is an abundant neutrophil-derived heme protein that is part of the antimicrobial defense system. The protein is typically present in the azurophilic granules of neutrophils, but a large portion may also enter the extracellular space. It remains unclear why MPO is frequently the target of antibody-mediated autoimmune responses. MPO is a homodimeric glycoprotein, posttranslationally modified with complex sugars at specific sites. Glycosylation can strongly influence protein function, affecting its folding, receptor interaction, and backbone accessibility. MPO potentially can be heavily modified as it harbors 5 putative
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Registered trials
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.