ArticleBlood2016
Structural basis for collagen recognition by the immune receptor OSCAR.
Article in Blood, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
30 citing papers in PubMed, 52 citations in OpenAlex.
- Differential Effects of Collagen Hydrolysate Digesta on Osteoclast and Osteoblast Responses In Vitro.Nutrients · 2026Article
- Immune-activating PTL/nanowire composite coating on Ti surface enables macrophage-driven bacterial clearance and osseointegration.Bioactive materials · 2026Article
- The extracellular matrix in inflammation and cancer.Molecular biomedicine · 2026Review
- Understanding the matrix: collagen modifications in tumors and their implications for immunotherapy.Journal of translational medicine · 2024Review
- 5-aminosalicylic acid suppresses osteoarthritis through the OSCAR-PPARγ axis.Nature communications · 2024Article
- Collagen-like Osteoclast-Associated Receptor (OSCAR)-Binding Motifs Show a Co-Stimulatory Effect on Osteoclastogenesis in a Peptide Hydrogel System.International journal of molecular sciences · 2023Article
- Proteomics and Precise Exercise Phenotypes in Heart Failure With Preserved Ejection Fraction: A Pilot Study.Journal of the American Heart Association · 2023Article
- Development of Anti-OSCAR Antibodies for the Treatment of Osteoarthritis.Biomedicines · 2023Article
- Gelatin Matrix as Functional Biomaterial for Immobilization of Nanoparticles of Metal-Containing Compounds.Journal of functional biomaterials · 2023Review
- Material matters: exploring the interplay between natural biomaterials and host immune system.Frontiers in immunology · 2023Review
- Collagen fibril formationMaterials today. Bio · 2022Review
- Review
- Prokaryotic Collagen-Like Proteins as Novel Biomaterials.Frontiers in bioengineering and biotechnology · 2022Review
- Sequence features, structure, ligand interaction, and diseases in small leucine rich repeat proteoglycans.Journal of cell communication and signaling · 2021Review
- Optimization of Novel Human Acellular Dermal Dressing Sterilization for Routine Use in Clinical Practice.International journal of molecular sciences · 2021Article
- Collagen Mimetic Peptides.Bioengineering (Basel, Switzerland) · 2021Review
- TARM1 contributes to development of arthritis by activating dendritic cells through recognition of collagens.Nature communications · 2021Article
- Role of OSCAR Signaling in Osteoclastogenesis and Bone Disease.Frontiers in cell and developmental biology · 2021Review
- Osteoclast-associated receptor blockade prevents articular cartilage destruction via chondrocyte apoptosis regulation.Nature communications · 2020Article
- Cellular uptake of collagens and implications for immune cell regulation in disease.Cellular and molecular life sciences : CMLS · 2020Review
Corrections and comments
- Commented on by
Authors and funding
10 authors at 3 institutions in 2 countries.
Funding
Abstract
The osteoclast-associated receptor (OSCAR) is a collagen-binding immune receptor with important roles in dendritic cell maturation and activation of inflammatory monocytes as well as in osteoclastogenesis. The crystal structure of the OSCAR ectodomain is presented, both free and in complex with a consensus triple-helical peptide (THP). The structures revealed a collagen-binding site in each immunoglobulin-like domain (D1 and D2). The THP binds near a predicted collagen-binding groove in D1, but a more extensive interaction with D2 is facilitated by the unusually wide D1-D2 interdomain angle in OSCAR. Direct binding assays, combined with site-directed mutagenesis, confirm that the primary collagen-binding site in OSCAR resides in D2, in marked contrast to the related collagen receptors, glycoprotein VI (GPVI) and leukocyte-associated immunoglobulin-like receptor-1 (LAIR-1). Monomeric OSCAR D1D2 binds to the consensus THP with a KD of 28 µM measured in solution, but shows a higher affinity (KD 1.5 μM) when binding to a solid-phase THP, most likely due to an avidity effect. These data suggest a 2-stage model for the interaction of OSCAR with a collagen fibril, with transient, low-affinity interactions initiated by the membrane-distal D1, followed by firm adhesion to the primary binding site in D2.
Indexed as
Identifiers
What OpenQuestion holds
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.