Evidence map›Paper›PMID 28593905›Full record

ReviewBiological chemistry2017

Targeting and inactivation of bacterial toxins by human defensins.

Elena Kudryashova, Stephanie M Seveau, Dmitri S Kudryashov

Abstract readReview
In one paragraph

Review in Biological chemistry, 2017. 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
1.1field-weighted citation impact, top 26% 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, 32 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Effects of Bile on PathogenicBiomolecules · 2025
    Article
  5. Article
  6. Life science alliance · 2024
    Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Human α-Defensin-6 NeutralizesInternational journal of molecular sciences · 2022
    Article
  12. Review
  13. Review
  14. Review
  15. Review
  16. Expert opinion on therapeutic targets · 2021
    Article
  17. Toxins · 2021
    Review
  18. Article
  19. Article
  20. Review
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

3 authors at 2 institutions in 1 country.

Elena Kudryashova
Stephanie M Seveau
Dmitri S Kudryashov
The Ohio State University · USInterface (United States) · US

Funding

Name Molecular mechanisms of bacterial toxins targeting actin cytoskeletonR01GM114666 · NIGMS · OHIO STATE UNIVERSITY · PI KUDRYASHOV, DMITRI · 2015 to 2025
$3.8M
Multifaceted activity of listeriolysin O during host cell invasion by ListeriaR01AI107250 · NIAID · OHIO STATE UNIVERSITY · PI SEVEAU, STEPHANIE M M · 2014 to 2018
$1.9M
NIAID NIH HHS R01 AI107250NIGMS NIH HHS R01 GM114666
6 · The paper itself

Abstract

Defensins, as a prominent family of antimicrobial peptides (AMP), are major effectors of the innate immunity with a broad range of immune modulatory and antimicrobial activities. In particular, defensins are the only recognized fast-response molecules that can neutralize a broad range of bacterial toxins, many of which are among the deadliest compounds on the planet. For a decade, the mystery of how a small and structurally conserved group of peptides can neutralize a heterogeneous group of toxins with little to no sequential and structural similarity remained unresolved. Recently, it was found that defensins recognize and target structural plasticity/thermodynamic instability, fundamental physicochemical properties that unite many bacterial toxins and distinguish them from the majority of host proteins. Binding of human defensins promotes local unfolding of the affected toxins, destabilizes their secondary and tertiary structures, increases susceptibility to proteolysis, and leads to their precipitation. While the details of toxin destabilization by defensins remain obscure, here we briefly review properties and activities of bacterial toxins known to be affected by or resilient to defensins, and discuss how recognized features of defensins correlate with the observed inactivation.

Indexed as

Bacterial ToxinsDefensinsHumansProtein ConformationThermodynamicsBacterial ToxinsDefensinsbacterial toxinsdefensinsthermodynamic instabilityunfolding

Identifiers

PMID28593905
PMCPMC5608644
OpenAlexW2612990889

What OpenQuestion holds

Textmetadata
LicenceTDM
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.