Evidence map›Paper›PMID 32994330›Full record

ArticlemBio2020

A Key Motif in the Cholesterol-Dependent Cytolysins Reveals a Large Family of Related Proteins.

Jordan C Evans, Bronte A Johnstone, Sara L Lawrence, Craig J Morton, Michelle P Christie, Michael W Parker, Rodney K Tweten

Open access · goldAbstract read
In one paragraph

Article in mBio, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

21 citing papers in PubMed, 30 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Review
  5. TlyC, a conserved hemolysin inMicrobiology spectrum · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. Genomic and metabolic characterization ofApplied and environmental microbiology · 2025
    Article
  10. Article
  11. Article
  12. Isolation and characterization of a novelFrontiers in microbiology · 2023
    Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Bacterial pore-forming toxins.Microbiology (Reading, England) · 2022
    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

7 authors at 2 institutions in 2 countries.

Jordan C Evans *Department of Microbiology and Immunology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma, USA.
Bronte A Johnstone *Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, Victoria, Australia.
Sara L Lawrence *Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, Victoria, Australia.
Craig J Morton *Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, Victoria, Australia.
Michelle P ChristieDepartment of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, Victoria, Australia.
Michael W Parker *Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, Victoria, Australia mparker@svi.edu.au Rod-Tweten@ouhsc.edu.
Rodney K Tweten *Department of Microbiology and Immunology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma, USA mparker@svi.edu.au Rod-Tweten@ouhsc.edu.
University of Melbourne · AUUniversity of Oklahoma Health Sciences Center · US

Funding

Pore Formation by Cholesterol Dependent CytolysinsR01AI037657 · NIAID · UNIVERSITY OF OKLAHOMA HLTH SCIENCES CTR · PI TWETEN, RODNEY K. · 1997 to 2015
$5.4M
Pore Formation by Cholesterol Dependent CytolysinsR37AI037657 · NIAID · UNIVERSITY OF OKLAHOMA HLTH SCIENCES CTR · PI TWETEN, RODNEY K. · 2016 to 2025
$4.8M
NIAID NIH HHS R01 AI037657NIAID NIH HHS R37 AI037657
6 · The paper itself

Abstract

The cholesterol-dependent cytolysins (CDCs) are bacterial, β-barrel, pore-forming toxins. A central enigma of the pore-forming mechanism is how completion of the prepore is sensed to initiate its conversion to the pore. We identified a motif that is conserved between the CDCs and a diverse family of nearly 300 uncharacterized proteins present in over 220 species that span at least 10 bacterial and 2 eukaryotic phyla. Except for this motif, these proteins exhibit little similarity to the CDCs at the primary structure level. Studies herein show this motif is a critical component of the sensor that initiates the prepore-to-pore transition in the CDCs. We further show by crystallography, single particle analysis, and biochemical studies of one of these CDC-like (CDCL) proteins from

Indexed as

Amino Acid MotifsAnimalsCell MembraneCholesterolCrystallography, X-RayCulicidaeCytotoxinsFlavobacteriaceaePore Forming Cytotoxic ProteinsCholesterolCytotoxinsPore Forming Cytotoxic ProteinsBacteroidesBacteroidetesChryseobacteriumDeinococcusElizabethkingiaMACPFpore-formingThalassiosira oceanicatoxin

Identifiers

PMID32994330
PMCPMC7527733
OpenAlexW3091308292

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.