ArticleNature communications2016
Structural basis of complement membrane attack complex formation.
Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 146 papers.
What it found
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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.
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Who cites it
146 citing papers in PubMed, 241 citations in OpenAlex.
- AFM to Study Pore-Forming Proteins.Methods in molecular biology (Clifton, N.J.) · 2027Article
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- Non-Syndromic or Anomaly-Associated Genes (MYH3, GREM1, IRF6) and Their Proteins in Unilateral Right Cleft Tissue.International journal of molecular sciences · 2026Article
- Advances in cryo-EM that have shaped mechanistic models of membrane-attack-complex assembly and regulation.IUCrJ · 2026Review
- Excessive C5 conversion prevents C9 polymerisation and subsequent MAC-dependent killing of Klebsiella pneumoniae.PLoS pathogens · 2026Article
- Article
- Advances in the lectin pathway in systemic lupus erythematosus: from clinical correlations and mechanisms to targeted interventions.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2026Review
- Functional Validation of the Proteome-Identified LIC_13056 Putative Lipoprotein ofInternational journal of molecular sciences · 2026Article
- The subtype identification of colorectal cancer and construction of the risk model based on cholesterol synthesis-related genes to predict prognosis and guide immunotherapy.International journal of colorectal disease · 2026Article
- Bactericidal membrane attack complex formation initiates at the new pole of E. coli.EMBO reports · 2026Article
- Structural Basis of Lipopolysaccharide O-Antigen Chain Length Modality.Research (Washington, D.C.) · 2026Article
- Proteins of the SubB family provide multiple mechanisms of serum resistance inEmerging microbes & infections · 2025Article
- CD59, Disulphide-Locked Human C9 and Horse C9 Inhibit Human Membrane Attack Complex Assembly by Similar Mechanisms.Immunology · 2025Article
- A Targeted Blockade of Terminal C5a Is Critical to Management of Sepsis and Acute Respiratory Distress Syndrome: The Mechanism of Action of Vilobelimab.International journal of molecular sciences · 2025Review
- Disrupting membranes, controlling cell fate: the role of pore-forming proteins in cell death and therapy.Apoptosis : an international journal on programmed cell death · 2025Review
- Multisystem Endothelial Inflammation: A Key Driver of Adverse Events Following mRNA-Containing COVID-19 Vaccines.Vaccines · 2025Review
- Macrocyclic Peptide Probes for Immunomodulatory Protein CD59: Potent Modulators of Bacterial Toxin Activity and Antibody-Dependent Cytotoxicity.Angewandte Chemie (International ed. in English) · 2025Article
- Evasion of serum antibodies and complement by Salmonella Typhi and Paratyphi A.PLoS pathogens · 2025Article
- Structural basis for the pore-forming activity of a complement-like toxin.Science advances · 2025Article
86 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
In response to complement activation, the membrane attack complex (MAC) assembles from fluid-phase proteins to form pores in lipid bilayers. MAC directly lyses pathogens by a 'multi-hit' mechanism; however, sublytic MAC pores on host cells activate signalling pathways. Previous studies have described the structures of individual MAC components and subcomplexes; however, the molecular details of its assembly and mechanism of action remain unresolved. Here we report the electron cryo-microscopy structure of human MAC at subnanometre resolution. Structural analyses define the stoichiometry of the complete pore and identify a network of interaction interfaces that determine its assembly mechanism. MAC adopts a 'split-washer' configuration, in contrast to the predicted closed ring observed for perforin and cholesterol-dependent cytolysins. Assembly precursors partially penetrate the lipid bilayer, resulting in an irregular β-barrel pore. Our results demonstrate how differences in symmetric and asymmetric components of the MAC underpin a molecular basis for pore formation and suggest a mechanism of action that extends beyond membrane penetration.
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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.