Evidence map›Paper›PMID 30125772›Full record

ReviewCurrent opinion in structural biology2018

Advances in cryoEM and its impact on β-pore forming proteins.

Courtney M Boyd, Doryen Bubeck

Abstract readReview
In one paragraph

Review in Current opinion in structural biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
–field-weighted citation impact
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

6 citing papers in PubMed.

  1. Computational and structural biotechnology journal · 2025
    Article
  2. Article
  3. Article
  4. Protein Ligand-Induced Amplification in the 1/Langmuir : the ACS journal of surfaces and colloids · 2020
    Article
  5. Article
  6. 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

2 authors.

Courtney M BoydDepartment of Life Sciences, Imperial College London, South Kensington Campus, London SW7 2AZ, UK.
Doryen BubeckDepartment of Life Sciences, Imperial College London, South Kensington Campus, London SW7 2AZ, UK. Electronic address: d.bubeck@imperial.ac.uk.

Funding

Biotechnology and Biological Sciences Research Council BB/J014575/1Cancer Research UK 16099Cancer Research UK C26409/A16099
6 · The paper itself

Abstract

Deployed by both hosts and pathogens, β-pore-forming proteins (β-PFPs) rupture membranes and lyse target cells. Soluble protein monomers oligomerize on the lipid bilayer where they undergo dramatic structural rearrangements, resulting in a transmembrane β-barrel pore. Advances in electron cryo-microscopy (cryoEM) sample preparation, image detection, and computational algorithms have led to a number of recent structures that reveal a molecular mechanism of pore formation in atomic detail.

Indexed as

Cryoelectron MicroscopyModels, MolecularAntigens, BacterialBacterial ToxinsHumansPore Forming Cytotoxic ProteinsProtein Conformationaerolysinanthrax toxinAntigens, BacterialBacterial ToxinsPore Forming Cytotoxic Proteins

Identifiers

PMID30125772
PMCPMC6302071

What OpenQuestion 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 OpenQuestion graph.