Evidence map›Paper›PMID 33674389›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2021

Charting the sequence-activity landscape of peptide inhibitors of translation termination.

Chetana Baliga, Tyler J Brown, Tanja Florin, Sarah Colon, Vallari Shah, Kornelia J Skowron, Amira Kefi, Teresa Szal, Dorota Klepacki, Terry W Moore and 2 more

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

16 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Proline-Rich Antimicrobial Peptides from Invertebrates.Molecules (Basel, Switzerland) · 2024
    Review
  7. Article
  8. Article
  9. Article
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  13. Article
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  15. Article
  16. The Multifaceted Roles of Proline in Cell Behavior.Frontiers in cell and developmental biology · 2021
    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

12 authors at 1 institution in 1 country.

Chetana BaligaCenter for Biomolecular Sciences, University of Illinois, Chicago, IL 60607.
Tyler J BrownCenter for Biomolecular Sciences, University of Illinois, Chicago, IL 60607.
Tanja FlorinCenter for Biomolecular Sciences, University of Illinois, Chicago, IL 60607.
Sarah ColonCenter for Biomolecular Sciences, University of Illinois, Chicago, IL 60607.
Vallari ShahCenter for Biomolecular Sciences, University of Illinois, Chicago, IL 60607.
Kornelia J SkowronDepartment of Pharmaceutical Sciences, University of Illinois, Chicago, IL 60607.ORCID 0000-0002-0846-6134
Amira KefiCenter for Biomolecular Sciences, University of Illinois, Chicago, IL 60607.ORCID 0000-0001-6703-3796
Teresa SzalCenter for Biomolecular Sciences, University of Illinois, Chicago, IL 60607.
Dorota KlepackiCenter for Biomolecular Sciences, University of Illinois, Chicago, IL 60607.
Terry W MooreDepartment of Pharmaceutical Sciences, University of Illinois, Chicago, IL 60607.ORCID 0000-0002-5410-306X
Nora Vázquez-LaslopCenter for Biomolecular Sciences, University of Illinois, Chicago, IL 60607; nvazquez@uic.edu shura@uic.edu.ORCID 0000-0003-2256-693X
Alexander S MankinCenter for Biomolecular Sciences, University of Illinois, Chicago, IL 60607; nvazquez@uic.edu shura@uic.edu.ORCID 0000-0002-3301-827X
University of Illinois Chicago · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Apidaecin (Api), an unmodified 18-amino-acid-long proline-rich antibacterial peptide produced by bees, has been recently described as a specific inhibitor of translation termination. It invades the nascent peptide exit tunnel of the postrelease ribosome and traps the release factors preventing their recycling. Api binds in the exit tunnel in an extended conformation that matches the placement of a nascent polypeptide and establishes multiple contacts with ribosomal RNA (rRNA) and ribosomal proteins. Which of these interactions are critical for Api's activity is unknown. We addressed this problem by analyzing the activity of all possible single-amino-acid substitutions of the Api variants synthesized in the bacterial cell. By conditionally expressing the engineered

Indexed as

Antimicrobial Cationic PeptidesEscherichia coliProtein Synthesis InhibitorsAmino Acid SubstitutionAnimalsBeesMutation, MissensePeptide Chain Termination, TranslationalRNA, BacterialRNA, RibosomalAntimicrobial Cationic PeptidesapidaecinProtein Synthesis InhibitorsRNA, BacterialRNA, Ribosomalantibioticapidaecinnascent peptide exit tunnelribosometranslation termination

Identifiers

PMID33674389
PMCPMC7958441
OpenAlexW3134196835

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.