Evidence map›Paper›PMID 32727850›Full record

ArticleThe Journal of biological chemistry2020

Long-term effects of the proline-rich antimicrobial peptide Oncocin112 on the

Yanyu Zhu, James C Weisshaar, Mainak Mustafi

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.3field-weighted citation impact, top 22% 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

14 citing papers in PubMed, 17 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Synergistic Action of Antimicrobial Peptides and Antibiotics.International journal of molecular sciences · 2026
    Review
  5. Review
  6. Proline-Modified (RW)ACS omega · 2025
    Article
  7. Proline-Rich Antimicrobial Peptides from Invertebrates.Molecules (Basel, Switzerland) · 2024
    Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Real-Time Fluorescence Microscopy on LivingInternational journal of molecular sciences · 2022
    Article
  14. 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

3 authors at 2 institutions in 1 country.

Yanyu ZhuDepartment of Chemistry, University of Wisconsin-Madison, Madison, Wisconsin, USA.
James C WeisshaarDepartment of Chemistry, University of Wisconsin-Madison, Madison, Wisconsin, USA.
Mainak MustafiDepartment of Chemistry, University of Wisconsin-Madison, Madison, Wisconsin, USA. Electronic address: mm5701@cumc.columbia.edu.
University of Wisconsin–Madison · USUniversity of Wisconsin System · US

Funding

Dynamics of Antimicrobial Peptide Interactions with Bacterial MembranesR01GM094510 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI WEISSHAAR, JAMES C. · 2010 to 2018
$2.2M
NIGMS NIH HHS R01 GM094510
6 · The paper itself

Abstract

Proline-rich antimicrobial peptides (PrAMPs) are cationic antimicrobial peptides unusual for their ability to penetrate bacterial membranes and kill cells without causing membrane permeabilization. Structural studies show that many such PrAMPs bind deep in the peptide exit channel of the ribosome, near the peptidyl transfer center. Biochemical studies of the particular synthetic PrAMP oncocin112 (Onc112) suggest that on reaching the cytoplasm, the peptide occupies its binding site prior to the transition from initiation to the elongation phase of translation, thus blocking further initiation events. We present a superresolution fluorescence microscopy study of the long-term effects of Onc112 on ribosome, elongation factor-Tu (EF-Tu), and DNA spatial distributions and diffusive properties in intact

Indexed as

Antimicrobial Cationic PeptidesCytoplasmEscherichia coliEscherichia coli ProteinsPeptide Elongation Factor TuProtein BiosynthesisRibosome Subunits, Large, BacterialRibosome Subunits, Small, BacterialAntimicrobial Cationic PeptidesEscherichia coli ProteinsoncocinPeptide Elongation Factor Tuantimicrobial peptide (AMP)fluorescencemicroscopyoncocin112 mechanismProline-rich antimicrobial peptidesribosome and EF-Tu diffusionsuperresolution imagingsuperresolution single-molecule localization and trackingtranslation elongation factortranslation regulation

Identifiers

PMID32727850
PMCPMC7504922
OpenAlexW3045739248

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.