Evidence map›Paper›PMID 24697492›Full record

ReviewBiochemistry2014

Molecular architecture of the bacterial flagellar motor in cells.

Xiaowei Zhao, Steven J Norris, Jun Liu

Open access · greenAbstract readReview
In one paragraph

Review in Biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers.

0numbers the graph read from it
0cells of the map it votes in
78citing papers in PubMed
6.1field-weighted citation impact, top 3% 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

78 citing papers in PubMed, 127 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Structure and Assembly of theInternational journal of molecular sciences · 2023
    Article
  9. An overview of the structure and function of the flagellar hook FlgE protein.World journal of microbiology & biotechnology · 2023
    Review
  10. Article
  11. Article
  12. Article
  13. The flagellar motor protein FliL forms a scaffold of circumferentially positioned rings required for stator activation.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Review

18 more citing papers are in PubMed but not listed here.

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 1 institution in 1 country.

Xiaowei ZhaoDepartment of Pathology and Laboratory Medicine, University of Texas Medical School at Houston , Houston, Texas 77030, United States.
Steven J Norris
Jun Liu
The University of Texas at Austin · US

Funding

Structure-Function Relationships in the Spirochetal Flagellar MotorR01AI087946 · NIAID · YALE UNIVERSITY · PI LIU, JUN · 2010 to 2025
$6.6M
NIAID NIH HHS R01 AI087946
6 · The paper itself

Abstract

The flagellum is one of the most sophisticated self-assembling molecular machines in bacteria. Powered by the proton-motive force, the flagellum rapidly rotates in either a clockwise or counterclockwise direction, which ultimately controls bacterial motility and behavior. Escherichia coli and Salmonella enterica have served as important model systems for extensive genetic, biochemical, and structural analysis of the flagellum, providing unparalleled insights into its structure, function, and gene regulation. Despite these advances, our understanding of flagellar assembly and rotational mechanisms remains incomplete, in part because of the limited structural information available regarding the intact rotor-stator complex and secretion apparatus. Cryo-electron tomography (cryo-ET) has become a valuable imaging technique capable of visualizing the intact flagellar motor in cells at molecular resolution. Because the resolution that can be achieved by cryo-ET with large bacteria (such as E. coli and S. enterica) is limited, analysis of small-diameter bacteria (including Borrelia burgdorferi and Campylobacter jejuni) can provide additional insights into the in situ structure of the flagellar motor and other cellular components. This review is focused on the application of cryo-ET, in combination with genetic and biophysical approaches, to the study of flagellar structures and its potential for improving the understanding of rotor-stator interactions, the rotational switching mechanism, and the secretion and assembly of flagellar components.

Indexed as

BacteriaBacterial Physiological PhenomenaBacterial ProteinsCryoelectron MicroscopyElectron Microscope TomographyFlagellaProtein ConformationSpecies SpecificitySpirochaetalesBacterial ProteinsFlig protein, BacteriaFliM protein, Bacteria

Identifiers

PMID24697492
PMCPMC4221660
OpenAlexW2057427296

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.