Evidence map›Paper›PMID 29286490›Full record

ArticleJournal of visualized experiments : JoVE2017

A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli.

Sumana Venkat, Caroline Gregory, Kexin Meng, Qinglei Gan, Chenguang Fan

Abstract readVideo-Audio Media
In one paragraph

Article in Journal of visualized experiments : JoVE, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.6field-weighted citation impact, top 29% 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

11 citing papers in PubMed, 12 citations in OpenAlex.

  1. Expanding the Genetic Code with Lysine Aminoacylation.Journal of the American Chemical Society · 2026
    Article
  2. Article
  3. Article
  4. Characterizing lysine acetylation of glucokinase.Protein science : a publication of the Protein Society · 2024
    Article
  5. Review
  6. Article
  7. Article
  8. A Synthetic Reporter for Probing Mistranslation in Living Cells.Frontiers in bioengineering and biotechnology · 2020
    Article
  9. Review
  10. Article
  11. 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

5 authors at 1 institution in 1 country.

Sumana VenkatDepartment of Chemistry and Biochemistry, University of Arkansas; Cell and Molecular Biology Program, University of Arkansas.
Caroline GregoryDepartment of Biological Sciences, University of Arkansas.
Kexin MengFayetteville High School.
Qinglei GanDepartment of Chemistry and Biochemistry, University of Arkansas.
Chenguang FanDepartment of Chemistry and Biochemistry, University of Arkansas; Cell and Molecular Biology Program, University of Arkansas; cf021@uark.edu.
University of Arkansas at Fayetteville · US

Funding

Expanding the genetic code in SalmonellaR21AI119813 · NIAID · YALE UNIVERSITY · PI FAN, CHENGUANG · 2015 to 2016
$424k
NIAID NIH HHS R21 AI119813
6 · The paper itself

Abstract

Post-translational modifications that occur at specific positions of proteins have been shown to play important roles in a variety of cellular processes. Among them, reversible lysine acetylation is one of the most widely distributed in all domains of life. Although numerous mass spectrometry-based acetylome studies have been performed, further characterization of these putative acetylation targets has been limited. One possible reason is that it is difficult to generate purely acetylated proteins at desired positions by most classic biochemical approaches. To overcome this challenge, the genetic code expansion technique has been applied to use the pair of an engineered pyrrolysyl-tRNA synthetase variant, and its cognate tRNA from Methanosarcinaceae species, to direct the cotranslational incorporation of acetyllysine at the specific site in the protein of interest. After first application in the study of histone acetylation, this approach has facilitated acetylation studies on a variety of proteins. In this work, we demonstrated a facile protocol to produce site-specifically acetylated proteins by using the model bacterium Escherichia coli as the host. Malate dehydrogenase was used as a demonstration example in this work.

Indexed as

Protein Processing, Post-TranslationalAcetylationEscherichia coliEscherichia coli ProteinsEscherichia coli Proteins

Identifiers

PMID29286490
PMCPMC5755542
OpenAlexW2771829904

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.