ArticleFEBS open bio2020
Structural and biophysical characterization of the type VII collagen vWFA2 subdomain leads to identification of two binding sites.
Article in FEBS open bio, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 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.
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Who cites it
3 citing papers in PubMed, 6 citations in OpenAlex.
- Molecular basis of collagen triple helix recognition by VWF A-like domain two of collagen VII: Implications for interlaced anchoring fibril formation.The Journal of biological chemistry · 2026Article
- Electrochemical Profiling of vWFA2 for Systemic Inflammatory State Detection.ACS measurement science au · 2024Article
- Missense Variant c.3301C>T (p.R1101W) in von Willebrand Factor A Sequence in a Patient with Recessive Dystrophic Epidermolysis Bullosa Pruriginosa with Compound HeterozygousAnnals of dermatology · 2023Article
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
Type VII collagen is an extracellular matrix protein, which is important for skin stability; however, detailed information at the molecular level is scarce. The second vWFA (von Willebrand factor type A) domain of type VII collagen mediates important interactions, and immunization of mice induces skin blistering in certain strains. To understand vWFA2 function and the pathophysiological mechanisms leading to skin blistering, we structurally characterized this domain by X-ray crystallography and NMR spectroscopy. Cell adhesion assays identified two new interactions: one with β1 integrin via its RGD motif and one with laminin-332. The latter interaction was confirmed by surface plasmon resonance with a K
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