Evidence map›Paper›PMID 28765223›Full record

ArticlemBio2017

Elongation Factor P Interactions with the Ribosome Are Independent of Pausing.

Rodney Tollerson, Anne Witzky, Michael Ibba

Open access · goldAbstract readComment
In one paragraph

Article in mBio, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.3field-weighted citation impact, top 40% 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

2 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
  2. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Rodney TollersonDepartment of Microbiology, The Ohio State University, Columbus, Ohio, USA.
Anne WitzkyDepartment of Molecular Genetics, The Ohio State University, Columbus, Ohio, USA.
Michael IbbaDepartment of Microbiology, The Ohio State University, Columbus, Ohio, USA ibba.1@osu.edu.
The Ohio State University · US

Funding

Mechanisms of translational controlR01GM065183 · NIGMS · OHIO STATE UNIVERSITY · PI DUNHAM, CHRISTINE M, FREDRICK, KURT L · 2003 to 2020
$4.9M
Cellular, molecular, and biochemical sciences training grantT32GM086252 · NIGMS · OHIO STATE UNIVERSITY · PI JACKMAN, JANE ELIZABETH, MUSIER-FORSYTH, KARIN M · 2011 to 2020
$2.0M
A Systems Biology Approach for Targeted Drug Discovery for LeishmaniasisR21AI127582 · NIAID · OHIO STATE UNIVERSITY · PI IBBA, MICHAEL, SATOSKAR, ABHAY R · 2017 to 2018
$401k
NIAID NIH HHS R21 AI127582NIGMS NIH HHS R01 GM065183NIGMS NIH HHS T32 GM086252
6 · The paper itself

Abstract

Bacterial elongation factor P (EF-P) plays a pivotal role in the translation of polyproline motifs. To stimulate peptide bond formation, EF-P must enter the ribosome via an empty E-site. Using fluorescence-based single-molecule tracking, Mohapatra et al. (S. Mohapatra, H. Choi, X. Ge, S. Sanyal, and J. C. Weisshaar, mBio 8:e00300-17, 2017, https://doi.org/10.1128/mBio.00300-17) monitored the cellular distribution of EF-P and quantified the frequency of association between EF-P and the ribosome under various conditions. Findings from the study showed that EF-P has a localization pattern that is strikingly similar to that of ribosomes. Intriguingly, EF-P was seen to bind ribosomes more frequently than the estimated number of pausing events, indicating that E-site vacancies occur even when ribosomes are not paused. The study provides new insights into the mechanism of EF-P-dependent peptide bond formation and the intricacies of translation elongation.

Indexed as

Escherichia coliPeptide Elongation FactorsProtein BiosynthesisRibosomesfactor EF-PPeptide Elongation Factorselongation factor Ppausingtranslation

Identifiers

PMID28765223
PMCPMC5539428
OpenAlexW2740182356

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.