ArticleNature communications2020
Structural insights into tetraspanin CD9 function.
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 122 papers.
What it found
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Who cites it
122 citing papers in PubMed, 206 citations in OpenAlex.
- A Novel Reporter Mouse for Astrocyte-Derived Extracellular Vesicles Reveals Enrichment of Cargo at Neuronal Mitochondria.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026Article
- Molecular interplay between sperm and oocyte: a narrative review.Human reproduction update · 2026Review
- A potential mechanism for tetraspanin CD82-mediated regulation of EGFR.Life science alliance · 2026Article
- The Mechanistic Review of the Molecular Interface of RNA-Loaded Extracellular Vesicles: Redefining Targeted Therapy for Autoimmune Disorders.International journal of molecular sciences · 2026Review
- Membrane-Based Assembly and Interactions in Immune Receptors.Chemical reviews · 2026Review
- Surface CD81 supports leukemia stem cell function and reveals a therapeutic vulnerability in acute myeloid leukemia.Signal transduction and targeted therapy · 2026Article
- Enzymatically controlled release of proteins and peptides: A promising, alternative secretion approach.iScience · 2026Article
- Dynamics of the CD9 interactome during bacterial infection of epithelial cells by proximity labelling proteomics.The FEBS journal · 2026Article
- Article
- Conserved use of tetraspanin CD9 as an entry receptor by rhabdoviruses spanning multiple genera.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Gangliosides in molecular interactions and cell regulation.The Journal of biological chemistry · 2026Review
- Efficient Sampling of Short Protein Trajectories with Conditional Diffusion Models.Journal of chemical theory and computation · 2026Article
- Cholesterol Deficiency Directs Autophagy-Dependent Secretion of Extracellular Vesicles.Journal of extracellular vesicles · 2026Article
- Membrane Fusions During Mammalian Fertilization.Advances in experimental medicine and biology · 2026Review
- Review
- Mapping the placental galectin-3 interactome identifies CD9 and ITGB1 as functional glycoprotein counterreceptors during syncytialization.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Structural basis for regulation of Frizzled-4 signaling by the co-receptor Tetraspanin-12.bioRxiv : the preprint server for biology · 2025Article
- Extracellular vesicles: biogenesis mechanism and impacts on tumor immune microenvironment.Journal of biomedical science · 2025Review
- In-depth amino acid mutational analysis of the key interspecific incompatibility factor Stigmatic Privacy 1.Plant & cell physiology · 2025Article
- Architecture mechanics mediated osteogenic progression in bone regeneration of artificial scaffolds.Science advances · 2025Article
62 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
13 authors at 7 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tetraspanins play critical roles in various physiological processes, ranging from cell adhesion to virus infection. The members of the tetraspanin family have four membrane-spanning domains and short and large extracellular loops, and associate with a broad range of other functional proteins to exert cellular functions. Here we report the crystal structure of CD9 and the cryo-electron microscopic structure of CD9 in complex with its single membrane-spanning partner protein, EWI-2. The reversed cone-like molecular shape of CD9 generates membrane curvature in the crystalline lipid layers, which explains the CD9 localization in regions with high membrane curvature and its implications in membrane remodeling. The molecular interaction between CD9 and EWI-2 is mainly mediated through the small residues in the transmembrane region and protein/lipid interactions, whereas the fertilization assay revealed the critical involvement of the LEL region in the sperm-egg fusion, indicating the different dependency of each binding domain for other partner proteins.
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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.