Evidence map›Paper›PMID 34667172›Full record

ArticleNature communications2021

Structural basis of soluble membrane attack complex packaging for clearance.

Anaïs Menny, Marie V Lukassen, Emma C Couves, Vojtech Franc, Albert J R Heck, Doryen Bubeck

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.2field-weighted citation impact, top 23% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

22 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Cerebral proteome adaptations to amyloid angiopathy are prevented by carbonic anhydrase inhibitors.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2025
    Article
  10. Clusterin: structure, function and roles in disease.International journal of medical sciences · 2025
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 2 countries.

Anaïs Menny *Department of Life Sciences, Sir Ernst Chain Building, Imperial College London, London, SW7 2AZ, UK.ORCID 0000-0002-6044-4119
Marie V Lukassen *Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Padulaan 8, 3584 CH, Utrecht, The Netherlands.
Emma C CouvesDepartment of Life Sciences, Sir Ernst Chain Building, Imperial College London, London, SW7 2AZ, UK.
Vojtech FrancBiomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Padulaan 8, 3584 CH, Utrecht, The Netherlands.
Albert J R HeckBiomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Padulaan 8, 3584 CH, Utrecht, The Netherlands.ORCID 0000-0002-2405-4404
Doryen BubeckDepartment of Life Sciences, Sir Ernst Chain Building, Imperial College London, London, SW7 2AZ, UK. d.bubeck@imperial.ac.uk.ORCID 0000-0001-8241-9697
Imperial College London · GBUtrecht University · NL

Funding

Biotechnology and Biological Sciences Research CouncilCancer Research UK C24523/A26234Medical Research CouncilWellcome Trust
6 · The paper itself

Abstract

Unregulated complement activation causes inflammatory and immunological pathologies with consequences for human disease. To prevent bystander damage during an immune response, extracellular chaperones (clusterin and vitronectin) capture and clear soluble precursors to the membrane attack complex (sMAC). However, how these chaperones block further polymerization of MAC and prevent the complex from binding target membranes remains unclear. Here, we address that question by combining cryo electron microscopy (cryoEM) and cross-linking mass spectrometry (XL-MS) to solve the structure of sMAC. Together our data reveal how clusterin recognizes and inhibits polymerizing complement proteins by binding a negatively charged surface of sMAC. Furthermore, we show that the pore-forming C9 protein is trapped in an intermediate conformation whereby only one of its two transmembrane β-hairpins has unfurled. This structure provides molecular details for immune pore formation and helps explain a complement control mechanism that has potential implications for how cell clearance pathways mediate immune homeostasis.

Indexed as

Complement C8Complement C9Complement Membrane Attack ComplexCryoelectron MicroscopyHumansProtein BindingProtein Conformation, alpha-HelicalProtein DomainsComplement C8Complement C9Complement Membrane Attack Complex

Identifiers

PMID34667172
PMCPMC8526713
OpenAlexW3205680673

What Socratic holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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 Socratic graph.