ArticleStructure (London, England : 1993)2015
Structural basis for VEGF-C binding to neuropilin-2 and sequestration by a soluble splice form.
Article in Structure (London, England : 1993), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 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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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
37 citing papers in PubMed, 66 citations in OpenAlex.
- Structural Basis of Lymphangiogenic Receptor VEGFR-3 Activation Mediated by Distinctive Clustering of the Ligand-Receptor Complex.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Discovery and Cryo-EM-Guided Development of a Neuropilin-2-Binding Aptamer for Receptor Antagonism.Journal of the American Chemical Society · 2026Article
- Decreased potential for lymphatic vessel generation is a hallmark of early diagnosed arterial hypertension and can be reversed by treatment with angiotensin converting enzyme inhibitors.Scientific reports · 2026Article
- Differential expression of viral entry protein neuropilin 1 (NRP1) and neuropilin 2 (NRP2) in fatal COVID-19.Journal of virology · 2025Article
- Neuropilin-2 functions as a coinhibitory receptor to regulate antigen-induced inflammation and allograft rejection.The Journal of clinical investigation · 2025Article
- Vascular endothelial growth factor signaling in health and disease: from molecular mechanisms to therapeutic perspectives.Signal transduction and targeted therapy · 2025Review
- Regulation of VEGFR3 signaling in lymphatic endothelial cells.Frontiers in cell and developmental biology · 2025Review
- Vascular Endothelial Growth Factor (VEGF) Family and the Immune System: Activators or Inhibitors?Biomedicines · 2024Review
- Orchestrating Resilience: How Neuropilin-2 and Macrophages Contribute to Cardiothoracic Disease.Journal of clinical medicine · 2024Review
- Tissue-resident macrophages specifically express Lactotransferrin and Vegfc during ear pinna regeneration in spiny mice.Developmental cell · 2024Article
- Review
- Inhibition of VEGF binding to neuropilin-2 enhances chemosensitivity and inhibits metastasis in triple-negative breast cancer.Science translational medicine · 2023Article
- Neuropilin 2 in osteoblasts regulates trabecular bone mass in male mice.Frontiers in endocrinology · 2023Article
- Role of Neuropilin-2-mediated signaling axis in cancer progression and therapy resistance.Cancer metastasis reviews · 2022Review
- Neuropilin-2 regulates androgen-receptor transcriptional activity in advanced prostate cancer.Oncogene · 2022Article
- Structural basis for HCMV Pentamer recognition by neuropilin 2 and neutralizing antibodies.Science advances · 2022Article
- VEGFA, B, C: Implications of the C-Terminal Sequence Variations for the Interaction with Neuropilins.Biomolecules · 2022Article
- TGF-β superfamily co-receptors in cancer.Developmental dynamics : an official publication of the American Association of Anatomists · 2022Review
- A Structural Overview of Vascular Endothelial Growth Factors Pharmacological Ligands: From Macromolecules to Designed Peptidomimetics.Molecules (Basel, Switzerland) · 2021Review
- Review
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Vascular endothelial growth factor C (VEGF-C) is a potent lymphangiogenic cytokine that signals via the coordinated action of two cell surface receptors, Neuropilin-2 (Nrp2) and VEGFR-3. Diseases associated with both loss and gain of VEGF-C function, lymphedema and cancer, respectively, motivate studies of VEGF-C/Nrp2 binding and inhibition. Here, we demonstrate that VEGF-C binding to Nrp2 is regulated by C-terminal proteolytic maturation. The structure of the VEGF-C C terminus in complex with the ligand binding domains of Nrp2 demonstrates that a cryptic Nrp2 binding motif is released upon proteolysis, allowing specific engagement with the b1 domain of Nrp2. Based on the identified structural requirements for Nrp2 binding to VEGF-C, we hypothesized that the endogenous secreted splice form of Nrp2, s9Nrp2, may function as a selective inhibitor of VEGF-C. We find that s9Nrp2 forms a stable dimer that potently inhibits VEGF-C/Nrp2 binding and cellular signaling. These data provide critical insight into VEGF-C/Nrp2 binding and inhibition.
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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.