ArticleFrontiers in immunology2011
The human c1q globular domain: structure and recognition of non-immune self ligands.
Article in Frontiers in immunology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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Who cites it
51 citing papers in PubMed, 87 citations in OpenAlex.
- Phosphatidylserine exposure by developing astrocytes initiates microglia-mediated developmental cell death.bioRxiv : the preprint server for biology · 2026Article
- C1q limits cystoid edema by maintaining basal β-catenin-dependent signaling and blood-retina barrier function.JCI insight · 2025Article
- C1q Is Recognized as a Soluble Autoantigen by Anti-C1q Antibodies of Patients with Systemic Lupus Erythematosus.Antibodies (Basel, Switzerland) · 2025Article
- The complement system in autoimmune diseases: pathogenesis, diagnostic markers, and therapeutic strategies.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2025Review
- Article
- Dysregulated complement activation during acute myocardial infarction leads to endothelial glycocalyx degradation and endothelial dysfunction via the C5a:C5a-Receptor1 axis.Frontiers in immunology · 2024Article
- Causal relationship between complementFrontiers in genetics · 2024Article
- Complement in Human Brain Health: Potential of Dietary Food in Relation to Neurodegenerative Diseases.Foods (Basel, Switzerland) · 2023Review
- Clinical Outcome of Kidney Transplant Recipients with C1q-Binding De Novo Donor Specific Antibodies: A Single-Center Experience.Journal of clinical medicine · 2023Article
- Hollow Octadecameric Self-Assembly of Collagen-like Peptides.Journal of the American Chemical Society · 2023Article
- C1q and central nervous system disorders.Frontiers in immunology · 2023Review
- Regulation of Conformational Changes in C-reactive Protein Alters its Bioactivity.Cell biochemistry and biophysics · 2022Review
- Nanometer- and angstrom-scale characteristics that modulate complement responses to nanoparticles.Journal of controlled release : official journal of the Controlled Release Society · 2022Article
- The yin and the yang of early classical pathway complement disorders.Clinical and experimental immunology · 2022Review
- Single-cell analyses highlight the proinflammatory contribution of C1q-high monocytes to Behçet's disease.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Complement System and Alarmin HMGB1 Crosstalk: For Better or Worse.Frontiers in immunology · 2022Review
- Biochemically prepared C-reactive protein conformational states differentially affect C1q binding.BBA advances · 2022Article
- Membrane attack complexes, endothelial cell activation, and direct allorecognition.Frontiers in immunology · 2022Review
- Balancing the View of C1q in Transplantation: Consideration of the Beneficial and Detrimental Aspects.Frontiers in immunology · 2022Article
- C1q as a potential tolerogenic therapeutic in transplantation.American journal of transplantation : official journal of the American Society of Transplantation and the American Society of Transplant Surgeons · 2021Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
C1q, the ligand-binding unit of the C1 complex of complement, is a pattern recognition molecule with the unique ability to sense an amazing variety of targets, including a number of altered structures from self, such as apoptotic cells. The three-dimensional structure of its C-terminal globular domain, responsible for its recognition function, has been solved by X-ray crystallography, revealing a tightly packed heterotrimeric assembly with marked differences in the surface patterns of the subunits, and yielding insights into its versatile binding properties. In conjunction with other approaches, this same technique has been used recently to decipher the mechanisms that allow this domain to interact with various non-immune self ligands, including molecules known to provide eat-me signals on apoptotic cells, such as phosphatidylserine and DNA. These investigations provide evidence for a common binding area for these ligands located in subunit C of the C1q globular domain, and suggest that ligand recognition through this area down-regulates C1 activation, hence contributing to the control of the inflammatory reaction. The purpose of this article is to give an overview of these advances which represent a first step toward understanding the recognition mechanisms of C1q and their biological implications.
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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.