Evidence map›Paper›PMID 37871253›Full record

ArticleJournal of the American Chemical Society2023

Elongation Factor P Modulates the Incorporation of Structurally Diverse Noncanonical Amino Acids into

Sasha M Daskalova, Larisa M Dedkova, Rumit Maini, Poulami Talukder, Xiaoguang Bai, Sandipan Roy Chowdhury, Chao Zhang, Ryan C Nangreave, Sidney M Hecht

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.5field-weighted citation impact, top 17% 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

8 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
  2. Biological Regulation StudiedAccounts of chemical research · 2025
    Article
  3. Review
  4. Article
  5. Article
  6. Article
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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

9 authors at 1 institution in 1 country.

Sasha M DaskalovaBiodesign Center for Bioenergetics, and School of Molecular Sciences, Arizona State University, Tempe, Arizona 85287, United States.
Larisa M DedkovaBiodesign Center for Bioenergetics, and School of Molecular Sciences, Arizona State University, Tempe, Arizona 85287, United States.
Rumit MainiBiodesign Center for Bioenergetics, and School of Molecular Sciences, Arizona State University, Tempe, Arizona 85287, United States.
Poulami TalukderBiodesign Center for Bioenergetics, and School of Molecular Sciences, Arizona State University, Tempe, Arizona 85287, United States.
Xiaoguang BaiBiodesign Center for Bioenergetics, and School of Molecular Sciences, Arizona State University, Tempe, Arizona 85287, United States.
Sandipan Roy ChowdhuryBiodesign Center for Bioenergetics, and School of Molecular Sciences, Arizona State University, Tempe, Arizona 85287, United States.
Chao ZhangBiodesign Center for Bioenergetics, and School of Molecular Sciences, Arizona State University, Tempe, Arizona 85287, United States.ORCID 0000-0003-3609-1744
Ryan C NangreaveBiodesign Center for Bioenergetics, and School of Molecular Sciences, Arizona State University, Tempe, Arizona 85287, United States.
Sidney M HechtBiodesign Center for Bioenergetics, and School of Molecular Sciences, Arizona State University, Tempe, Arizona 85287, United States.ORCID 0000-0002-5429-2462
Arizona State University · US

Funding

Biological Regulation Studied In Vitro and In Cellulo with Modified ProteinsR35GM140819 · NIGMS · ARIZONA STATE UNIVERSITY-TEMPE CAMPUS · PI Sidney M. Hecht · 2021 to 2026
$2.9M
Selection of Modified Ribosomes Using Novel PuromycinsR01GM103861 · NIGMS · ARIZONA STATE UNIVERSITY-TEMPE CAMPUS · PI HECHT, SIDNEY M. · 2013 to 2021
$1.6M
Ribosomally Synthesized Proteins Incorporating Modified DipeptidesR01GM121367 · NIGMS · ARIZONA STATE UNIVERSITY-TEMPE CAMPUS · PI HECHT, SIDNEY M. · 2017 to 2020
$1.2M
NIGMS NIH HHS R01 GM103861NIGMS NIH HHS R01 GM121367NIGMS NIH HHS R35 GM140819
6 · The paper itself

Abstract

The introduction of noncanonical amino acids into proteins and peptides has been of great interest for many years and has facilitated the detailed study of peptide/protein structure and mechanism. In addition to numerous nonproteinogenic α-l-amino acids, bacterial ribosome modification has provided the wherewithal to enable the synthesis of peptides and proteins with a much greater range of structural diversity, as has the use of endogenous bacterial proteins in reconstituted protein synthesizing systems. In a recent report, elongation factor P (EF-P), putatively essential for enabling the incorporation of contiguous proline residues into proteins, was shown to facilitate the introduction of an N-methylated amino acid in addition to proline. This finding prompted us to investigate the properties of this protein factor with a broad variety of structurally diverse amino acid analogues using an optimized suppressor tRNA

Indexed as

Amino AcidsEscherichia coliPeptide Elongation FactorsPeptidesProlineTetrahydrofolate DehydrogenaseAmino Acidsfactor EF-PPeptide Elongation FactorsPeptidesProlineTetrahydrofolate Dehydrogenase

Identifiers

PMID37871253
PMCPMC10762953
OpenAlexW4387871582

What OpenQuestion holds

Textmetadata
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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.