ArticleJournal of proteome research2016
Comprehensive Characterization of Glycosylation and Hydroxylation of Basement Membrane Collagen IV by High-Resolution Mass Spectrometry.
Article in Journal of proteome research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers, 1 of them a synthesis that pooled it.
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Who cites it
50 citing papers in PubMed, 1 synthesis or guideline pooled it, 85 citations in OpenAlex.
- Type VIII collagen: advances in matrix biology and translational promise.Frontiers in bioengineering and biotechnology · 2025Pooled it
- Proteomics of highly post-translationally modified proteins in kidney tubulointerstitium.bioRxiv : the preprint server for biology · 2026Article
- Article
- Identification of Potential Proteins Interacting with α-Galactosidase A to Analyze the Pathogenesis of Fabry Disease.International journal of molecular sciences · 2026Article
- Prolyl-3-hydroxylase 1 is a central regulator of collagen post-translational modifications and the collagen biosynthetic network.The Journal of biological chemistry · 2026Article
- Revealing sex-specific changes across protein structure in the aging bone extracellular matrix.Matrix biology plus · 2026Article
- Prolyl 3-Hydroxylase 2 Supports a Pro-Angiogenic Milieu Promoting Colorectal Cancer Progression and Metastasis.International journal of molecular sciences · 2026Article
- A transcriptomic and proteomic map of primary human cell types.Nucleic acids research · 2026Article
- Comparative Study of the Positions of Glycosylated Residues in the Chains of Fibril-Forming Collagens and the Role that These Residues Play in Axial and Lateral Assembly.Sub-cellular biochemistry · 2026Review
- Collagen IV biosynthesis: Intracellular choreography of post-translational modifications.Matrix biology : journal of the International Society for Matrix Biology · 2025Review
- Enzymatic craftsmanship in collagen glycosylation.Nature communications · 2025Article
- The life cycle of type IV collagen.Matrix biology : journal of the International Society for Matrix Biology · 2025Review
- Post-translational modifications of collagen and its related diseases in metabolic pathways.Acta pharmaceutica Sinica. B · 2025Review
- Lysyl hydroxylase 2 glucosylates collagen VI to drive lung cancer progression.The Journal of clinical investigation · 2025Article
- The structural basis for the human procollagen lysine hydroxylation and dual-glycosylation.Nature communications · 2025Article
- Proteomic insights into the extracellular matrix: a focus on proteoforms and their implications in health and disease.Expert review of proteomics · 2024Review
- ColPTMScape: An open access knowledge base for tissue-specific collagen PTM maps.Matrix biology plus · 2024Article
- Lectin binding to pectoral fin of neonate little skates reared under ambient and projected-end-of-century temperature regimes.Journal of morphology · 2024Article
- Extracellular Matrix Proteomics: TheBiomolecules · 2023Review
- Impact of Bioinformatics Search Parameters for Peptides' Identification and Their Post-Translational Modifications: A Case Study of Proteolysed Gelatines from Beef, Pork, and Fish.Foods (Basel, Switzerland) · 2023Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Collagen IV is the main structural protein that provides a scaffold for assembly of basement membrane proteins. Posttranslational modifications such as hydroxylation of proline and lysine and glycosylation of lysine are essential for the functioning of collagen IV triple-helical molecules. These modifications are highly abundant posing a difficult challenge for in-depth characterization of collagen IV using conventional proteomics approaches. Herein, we implemented an integrated pipeline combining high-resolution mass spectrometry with different fragmentation techniques and an optimized bioinformatics workflow to study posttranslational modifications in mouse collagen IV. We achieved 82% sequence coverage for the α1 chain, mapping 39 glycosylated hydroxylysine, 148 4-hydroxyproline, and seven 3-hydroxyproline residues. Further, we employed our pipeline to map the modifications on human collagen IV and achieved 85% sequence coverage for the α1 chain, mapping 35 glycosylated hydroxylysine, 163 4-hydroxyproline, and 14 3-hydroxyproline residues. Although lysine glycosylation heterogeneity was observed in both mouse and human, 21 conserved sites were identified. Likewise, five 3-hydroxyproline residues were conserved between mouse and human, suggesting that these modification sites are important for collagen IV function. Collectively, these are the first comprehensive maps of hydroxylation and glycosylation sites in collagen IV, which lay the foundation for dissecting the key role of these modifications in health and disease.
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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.