ArticleProceedings of the National Academy of Sciences of the United States of America2016
Structural basis of collagen recognition by human osteoclast-associated receptor and design of osteoclastogenesis inhibitors.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 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
17 citing papers in PubMed, 30 citations in OpenAlex.
- OSCAR functions as a collagen I receptor to suppress hippo signaling and reprogram lipid metabolism in clear-cell renal cell carcinoma.Cell death & disease · 2026Article
- Signaling Dynamics in Osteogenesis: Unraveling Therapeutic Targets for Bone Generation.Current drug targets · 2025Review
- 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
- Development of Anti-OSCAR Antibodies for the Treatment of Osteoarthritis.Biomedicines · 2023Article
- Material matters: exploring the interplay between natural biomaterials and host immune system.Frontiers in immunology · 2023Review
- Review
- The complex interactions between the cellular and non-cellular components of the brain tumor microenvironmental landscape and their therapeutic implications.Frontiers in oncology · 2022Review
- Immune Modulatory Properties of Collagen in Cancer.Frontiers in immunology · 2021Review
- Role of OSCAR Signaling in Osteoclastogenesis and Bone Disease.Frontiers in cell and developmental biology · 2021Review
- Collagen Structure-Function Mapping Informs Applications for Regenerative Medicine.Bioengineering (Basel, Switzerland) · 2020Review
- Three Decades of Research on Recombinant Collagens: Reinventing the Wheel or Developing New Biomedical Products?Bioengineering (Basel, Switzerland) · 2020Review
- Osteoclast-associated receptor blockade prevents articular cartilage destruction via chondrocyte apoptosis regulation.Nature communications · 2020Article
- Ultrastructural Location and Interactions of the Immunoglobulin Receptor Binding Sequence within Fibrillar Type I Collagen.International journal of molecular sciences · 2020Article
- The Natural Cytotoxicity Receptors in Health and Disease.Frontiers in immunology · 2019Review
- Adapting extracellular matrix proteomics for clinical studies on cardiac remodeling post-myocardial infarction.Clinical proteomics · 2016Review
- A Structural Bridge Between Kingdoms: How Collagen-Derived Peptides Influence Plant Stress and Growth Pathways.Physiologia plantarumArticle
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human osteoclast-associated receptor (OSCAR) is an immunoglobulin (Ig)-like collagen receptor that is up-regulated on osteoclasts during osteoclastogenesis and is expressed in a range of myeloid cells. As a member of the leukocyte receptor complex family of proteins, OSCAR shares a high degree of sequence and structural homology with other collagen receptors of this family, including glycoprotein VI, leukocyte-associated Ig-like receptor-1, and leukocyte Ig-like receptor B4, but recognizes a unique collagen sequence. Here, we present the crystal structures of OSCAR in its free form and in complex with a triple-helical collagen-like peptide (CLP). These structures reveal that the CLP peptide binds only one of the two Ig-like domains, the membrane-proximal domain (domain 2) of OSCAR, with the middle and trailing chain burying a total of 661 Å(2) of solvent-accessible collagen surface. This binding mode is facilitated by the unusual topography of the OSCAR protein, which displays an obtuse interdomain angle and a rotation of domain 2 relative to the membrane-distal domain 1. Moreover, the binding of the CLP to OSCAR appears to be mediated largely by tyrosine residues and conformational changes at a shallow Phe pocket. Furthermore, we investigated CLP peptides as inhibitors of osteoclastogenesis and found that a peptide length of 40 amino acids is required to ensure adequate inhibition of osteoclastogenesis in vitro. These findings provide valuable structural insights into the mode of collagen recognition by OSCAR and into the use of synthetic peptide matrikines for osteoclastogenesis inhibition.
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.