Evidence map›Paper›PMID 33260377›Full record

ArticleInternational journal of molecular sciences2020

Regulation of the First Committed Step in Lipopolysaccharide Biosynthesis Catalyzed by LpxC Requires the Essential Protein LapC (YejM) and HslVU Protease.

Daria Biernacka, Patrycja Gorzelak, Gracjana Klein, Satish Raina

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

27 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Essential Role of LapD in the Absence of Cardiolipins.International journal of molecular sciences · 2026
    Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Signaling through theJournal of bacteriology · 2024
    Article
  12. Suppressors ofInternational journal of molecular sciences · 2023
    Article
  13. A role for the Gram-negative outer membrane in bacterial shape determination.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  14. Lipopolysaccharides: Regulated Biosynthesis and Structural Diversity.International journal of molecular sciences · 2023
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Regulated Expression ofInternational journal of molecular sciences · 2022
    Article
  20. 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

4 authors at 1 institution in 1 country.

Daria BiernackaUnit of Bacterial Genetics, Gdansk University of Technology, 80-233 Gdansk, Poland.
Patrycja GorzelakUnit of Bacterial Genetics, Gdansk University of Technology, 80-233 Gdansk, Poland.
Gracjana KleinUnit of Bacterial Genetics, Gdansk University of Technology, 80-233 Gdansk, Poland.ORCID 0000-0001-8695-8065
Satish RainaUnit of Bacterial Genetics, Gdansk University of Technology, 80-233 Gdansk, Poland.
Gdańsk University of Technology · PL

Funding

Narodowe Centrum Nauki 2017/25/B/NZ6/02021
6 · The paper itself

Abstract

We previously showed that lipopolysaccharide (LPS) assembly requires the essential LapB protein to regulate FtsH-mediated proteolysis of LpxC protein that catalyzes the first committed step in the LPS synthesis. To further understand the essential function of LapB and its role in LpxC turnover, multicopy suppressors of Δ

Indexed as

BiocatalysisAmidohydrolasesAmino Acid MotifsAmino Acid SequenceATP-Dependent ProteasesConserved SequenceEscherichia coliEscherichia coli ProteinsHeat-Shock ProteinsHydroxamic AcidsLipopolysaccharidesMutationOperonPeriplasmPhospholipidsPromoter Regions, GeneticAmidohydrolasesATP-Dependent ProteasesCHIR 090Escherichia coli ProteinsFtsH protein, E coliHeat-Shock ProteinsHydroxamic AcidsLipopolysaccharidesPhospholipidsThreonineUDP-3-O-acyl-N-acetylglucosamine deacetylaseYejM protein, E coliFabZHslV/U proteaseLapBLapClipopolysaccharideLpxCRpoEYejM

Identifiers

PMID33260377
PMCPMC7730581
OpenAlexW3106878424

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.