ReviewImmunology letters2004
Structural and functional anatomy of the globular domain of complement protein C1q.
Review in Immunology letters, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 75 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
75 citing papers in PubMed, 188 citations in OpenAlex.
- A Peptide-Centric DIA-NN Reanalysis Uncovers Structurally Coherent Salivary Signatures of Type 2 Diabetes.International journal of molecular sciences · 2026Article
- Complement C1q promotes primary haemostasis in a microfluidic bleeding model.Frontiers in immunology · 2026Article
- Battle of the Biomarkers of Systemic Inflammation.Biology · 2025Review
- Innate Immune Mechanisms in the Central Nervous System.Advances in experimental medicine and biology · 2025Review
- LYVE-1-expressing Macrophages Modulate the Hyaluronan-containing Extracellular Matrix in the Mammary Stroma and Contribute to Mammary Tumor Growth.Cancer research communications · 2024Article
- Epigenetic regulation of complement C1Q gene expression.Frontiers in immunology · 2024Article
- Complement-Coagulation Cross-talk: Factor H-mediated regulation of the Complement Classical Pathway activation by fibrin clots.Frontiers in immunology · 2024Article
- Causal relationship between complementFrontiers in genetics · 2024Article
- Next generation of multispecific antibody engineering.Antibody therapeutics · 2024Review
- Complement in Human Brain Health: Potential of Dietary Food in Relation to Neurodegenerative Diseases.Foods (Basel, Switzerland) · 2023Review
- Could a Non-Cellular Molecular Interactome in the Blood Circulation Influence Pathogens' Infectivity?Cells · 2023Review
- Complement Inhibition in Kidney Transplantation: Where Are We Now?BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2023Review
- Multi-omics investigation of the resistance mechanisms of pomalidomide in multiple myeloma.Frontiers in oncology · 2023Article
- The yin and the yang of early classical pathway complement disorders.Clinical and experimental immunology · 2022Review
- Understanding the contextual functions of C1q and LAIR-1 and their applications.Experimental & molecular medicine · 2022Review
- Multimerin-1 and cancer: a review.Bioscience reports · 2022Review
- The Contribution of Complement Protein C1q in COVID-19 and HIV Infection Comorbid with Preeclampsia: A Review.International archives of allergy and immunology · 2022Review
- The collagen structure of C1q induces wound healing by engaging discoidin domain receptor 2.Molecular medicine (Cambridge, Mass.) · 2021Article
- On-target IgG hexamerisation driven by a C-terminal IgM tail-piece fusion variant confers augmented complement activation.Communications biology · 2021Article
- Dendrimer end-terminal motif-dependent evasion of human complement and complement activation through IgM hitchhiking.Nature communications · 2021Article
15 more citing papers are in PubMed but not listed here.
Corrections and comments
- Erratum issued
Authors and funding
10 authors at 7 institutions in 6 countries.
Funding
Abstract
C1q is the first subcomponent of the classical pathway of the complement system and a major connecting link between innate and acquired immunity. As a versatile charge pattern recognition molecule, C1q is capable of engaging a broad range of ligands via its heterotrimeric globular domain (gC1q) which is composed of the C-terminal regions of its A (ghA), B (ghB) and C (ghC) chains. Recent studies using recombinant forms of ghA, ghB and ghC have suggested that the gC1q domain has a modular organization and each chain can have differential ligand specificity. The crystal structure of the gC1q, molecular modeling and protein engineering studies have combined to illustrate how modular organization, charge distribution and the spatial orientation of the heterotrimeric assembly offer versatility of ligand recognition to C1q. Although the biochemical and structural studies have provided novel insights into the structure-function relationships within the gC1q domain, they have also raised many unexpected issues for debate.
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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.