Evidence map›Paper›PMID 32913243›Full record

ArticleScientific reports2020

Affinity of Skp to OmpC revealed by single-molecule detection.

Sichen Pan, Chen Yang, Xin Sheng Zhao

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2020. 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
0.8field-weighted citation impact, top 28% 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, 12 citations in OpenAlex.

  1. Review
  2. Article
  3. FkpA enhances membrane protein folding using an extensive interaction surface.Protein science : a publication of the Protein Society · 2023
    Article
  4. Article
  5. 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
  6. Article
  7. Article
  8. How do Chaperones Bind (Partly) Unfolded Client Proteins?Frontiers in molecular biosciences · 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

3 authors at 3 institutions in 1 country.

Sichen PanBeijing National Laboratory for Molecular Sciences, State Key Laboratory for Structural Chemistry of Unstable and Stable Species, and Department of Chemical Biology, College of Chemistry and Molecular Engineering, Peking University, Beijing, 100871, China.
Chen YangBeijing National Laboratory for Molecular Sciences, State Key Laboratory for Structural Chemistry of Unstable and Stable Species, and Department of Chemical Biology, College of Chemistry and Molecular Engineering, Peking University, Beijing, 100871, China.
Xin Sheng ZhaoBeijing National Laboratory for Molecular Sciences, State Key Laboratory for Structural Chemistry of Unstable and Stable Species, and Department of Chemical Biology, College of Chemistry and Molecular Engineering, Peking University, Beijing, 100871, China. zhaoxs@pku.edu.cn.
Beijing National Laboratory for Molecular Sciences · CNPeking University · CNState Key Laboratory for Structural Chemistry of Unstable and Stable Species

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Outer membrane proteins (OMPs) are essential to gram-negative bacteria, and molecular chaperones prevent the OMPs from aggregation in the periplasm during the OMPs biogenesis. Skp is one of the molecular chaperones for this purpose. Here, we combined single-molecule fluorescence resonance energy transfer and fluorescence correlation spectroscopy to study the affinity and stoichiometric ratio of Skp in its binding with OmpC at the single-molecule level. The half concentration of the Skp self-trimerization (C

Indexed as

DNA-Binding ProteinsEscherichia coliEscherichia coli ProteinsMolecular ChaperonesPeriplasmPorinsProtein BindingProtein FoldingSingle Molecule ImagingSpectrometry, FluorescenceDNA-Binding ProteinsEscherichia coli ProteinsMolecular ChaperonesOmpC proteinPorinsSkp protein, E coli

Identifiers

PMID32913243
PMCPMC7483523
OpenAlexW3084129096

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.