Evidence map›Paper›PMID 31113900›Full record

ArticlemBio2019

Improper Coordination of BamA and BamD Results in Bam Complex Jamming by a Lipoprotein Substrate.

Muralidhar Tata, Anna Konovalova

Open access · goldAbstract read
In one paragraph

Article in mBio, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

18 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. A mechanism for substrate quality control in outer membrane protein assembly.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. The sacrificial adaptor protein Skp functions to remove stalled substrates from the β-barrel assembly machine.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  11. High-throughput suppressor screen demonstrates that RcsF monitors outer membrane integrity and not Bam complex function.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  12. Homeostasis of the Gram-negative cell envelope.Current opinion in microbiology · 2021
    Review
  13. Article
  14. The gain-of-function alleleProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  15. Review
  16. The big BAM theory: An open and closed case?Biochimica et biophysica acta. Biomembranes · 2020
    Review
  17. Article
  18. 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

2 authors at 1 institution in 1 country.

Muralidhar TataDepartment of Microbiology and Molecular Genetics, McGovern Medical School, The University of Texas Health Science Center at Houston (UTHealth), Houston, Texas, USA.
Anna KonovalovaDepartment of Microbiology and Molecular Genetics, McGovern Medical School, The University of Texas Health Science Center at Houston (UTHealth), Houston, Texas, USA anna.konovalova@uth.tmc.edu.ORCID 0000-0002-2238-8849
The University of Texas Health Science Center at Houston · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The β-barrel assembly machinery, the Bam complex, is central to the biogenesis of integral outer membrane proteins (OMPs) as well as OMP-dependent surface-exposed lipoproteins, such as regulator of capsule synthesis protein F (RcsF). Previous genetic analysis established the model that nonessential components BamE and BamB have overlapping, redundant functions to enhance the kinetics of the highly conserved BamA/BamD core. Here we report that BamE plays a specialized nonredundant role in the Bam complex required for surface exposure of RcsF. We show that the lack of

Indexed as

Protein MultimerizationBacterial Outer Membrane ProteinsEscherichia coliEscherichia coli ProteinsGene DeletionLipoproteinsBacterial Outer Membrane ProteinsBamA protein, E coliBamD protein, E coliBamE protein, E coliEscherichia coli ProteinsLipoproteinsrcsF protein, E coliGram-negative envelope biogenesisRcs phosphorelaysurface-exposed lipoproteins

Identifiers

PMID31113900
PMCPMC6529637
OpenAlexW2946015249

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.