Evidence map›Paper›PMID 31699894›Full record

ArticleThe Journal of biological chemistry2019

The cytoplasmic domain of MxiG interacts with MxiK and directs assembly of the sorting platform in the

Shoichi Tachiyama, Yunjie Chang, Meenakumari Muthuramalingam, Bo Hu, Michael L Barta, Wendy L Picking, Jun Liu, William D Picking

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.7field-weighted citation impact, top 11% 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

17 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
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  6. Article
  7. A Tale aboutMicroorganisms · 2023
    Review
  8. Review
  9. Article
  10. Differential regulation ofFrontiers in cellular and infection microbiology · 2023
    Article
  11. Article
  12. TheMicroorganisms · 2021
    Review
  13. Review
  14. Composition and Biophysical Properties of the Sorting Platform Pods in theFrontiers in cellular and infection microbiology · 2021
    Article
  15. Article
  16. The T3SS ofMicroorganisms · 2020
    Review
  17. 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

8 authors at 3 institutions in 1 country.

Shoichi TachiyamaDepartment of Molecular Biosciences, University of Kansas, Lawrence, Kansas 66045.
Yunjie ChangDepartment of Microbial Pathogenesis, Yale University School of Medicine, New Haven, Connecticut 06516.
Meenakumari MuthuramalingamHiguchi Biosciences Center, University of Kansas, Lawrence, Kansas 66047.ORCID 0000-0001-5635-325X
Bo HuDepartment of Microbiology and Molecular Genetics, University of Texas Health Science Center, Houston, Texas 77030.
Michael L BartaHiguchi Biosciences Center, University of Kansas, Lawrence, Kansas 66047.
Wendy L PickingDepartment of Pharmaceutical Chemistry, University of Kansas, Lawrence, Kansas 66047.
Jun LiuDepartment of Microbial Pathogenesis, Yale University School of Medicine, New Haven, Connecticut 06516 jliu@yale.edu.
William D PickingDepartment of Molecular Biosciences, University of Kansas, Lawrence, Kansas 66045 picking@ku.edu.
University of Kansas · USYale University · USThe University of Texas Health Science Center at Houston · US

Funding

Assembly/function of the sorting platform of the Shigella type III secretion apparatusR01AI123351 · NIAID · UNIVERSITY OF KANSAS LAWRENCE · PI PICKING, WILLIAM D. · 2016 to 2020
$2.2M
NIAID NIH HHS R01 AI123351
6 · The paper itself

Abstract

Many Gram-negative bacteria use type III secretion systems (T3SSs) to inject virulence effector proteins into eukaryotic cells. The T3SS apparatus (T3SA) is structurally conserved among diverse bacterial pathogens and consists of a cytoplasmic sorting platform, an envelope-spanning basal body, and an extracellular needle with tip complex. The sorting platform is essential for effector recognition and powering secretion. Studies using bacterial "minicells" have revealed an unprecedented level of structural detail of the sorting platform; however, many of the structure-function relationships within this complex remain enigmatic. Here, we report on improved cryo-electron tomographic approaches to enhance the resolution of the

Indexed as

Bacterial ProteinsCytoplasmShigella flexneriType III Secretion SystemsBacterial ProteinsType III Secretion Systemsbacteriacryo-electron tomographyeffector proteinMxiGMxiKprotein complexprotein-protein interactionsecretionShigellasorting platformtype III secretion system (T3SS)virulence factor

Identifiers

PMID31699894
PMCPMC6916477
OpenAlexW2983981002

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.