How Structures of Complement Complexes Guide Therapeutic Design.

Jasmine K Bickel, Tomas B Voisin, Edward W Tate, Doryen Bubeck

Abstract readReview

In one paragraph

Review in Sub-cellular biochemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it

0cells of the map it votes in

1citing papers in PubMed

–field-weighted citation impact, top 71% 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

1 citing paper in PubMed, 2 citations in OpenAlex.

Cryo-EM analysis of complement C3 reveals a reversible major opening of the macroglobulin ring.Nature structural & molecular biology · 2025
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

4 authors at 1 institution in 1 country.

Jasmine K BickelDepartment of Life Sciences, Imperial College London, Sir Ernst Chain Building, South Kensington Campus, London, SW7 2AZ, UK.

Tomas B VoisinDepartment of Life Sciences, Imperial College London, Sir Ernst Chain Building, South Kensington Campus, London, SW7 2AZ, UK.

Edward W TateDepartment of Chemistry, Molecular Sciences Research Hub, Imperial College London, White City Campus, London, W12 0BZ, UK.

Doryen BubeckDepartment of Life Sciences, Imperial College London, Sir Ernst Chain Building, South Kensington Campus, London, SW7 2AZ, UK. d.bubeck@imperial.ac.uk.

Imperial College London · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The complement system is essential for immune defence against infection and modulation of proinflammatory responses. Activation of the terminal pathway of complement triggers formation of the membrane attack complex (MAC), a multi-protein pore that punctures membranes. Recent advances in structural biology, specifically cryo-electron microscopy (cryoEM), have provided atomic resolution snapshots along the pore formation pathway. These structures have revealed dramatic conformational rearrangements that enable assembly and membrane rupture. Here we review the structural basis for MAC formation and show how soluble proteins transition into a giant β-barrel pore. We also discuss regulatory complexes of the terminal pathway and their impact on structure-guided drug discovery of complement therapeutics.

Indexed as

Drug DesignComplement Membrane Attack ComplexCryoelectron MicroscopyHumansComplement Membrane Attack ComplexC5Complement therapeuticsCryo electron microscopyMACPFMembrane attack complexStructure-guided drug discovery

Identifiers

PMID33252733

DOI10.1038/nrneph.2012.214

OpenAlexW3110374578

What OpenQuestion holds

Textmetadata

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 OpenQuestion graph.