Evidence map›Paper›PMID 27664419›Full record

ArticleeLife2016

Bacterial flagellar capping proteins adopt diverse oligomeric states.

Sandra Postel, Daniel Deredge, Daniel A Bonsor, Xiong Yu, Kay Diederichs, Saskia Helmsing, Aviv Vromen, Assaf Friedler, Michael Hust, Edward H Egelman and 3 more

Open access · goldAbstract read
In one paragraph

Article in eLife, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
4.5field-weighted citation impact, top 6% 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

23 citing papers in PubMed, 48 citations in OpenAlex.

  1. Article
  2. Article
  3. FlaG competes with FliS-flagellin complexes for access to FlhA in the flagellar T3SS to controlProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  4. Article
  5. Motility inMicroorganisms · 2023
    Article
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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

13 authors at 5 institutions in 3 countries.

Sandra PostelInstitute of Human Virology, University of Maryland School of Medicine, Baltimore, United States.ORCID 0000-0002-6717-1870
Daniel DeredgeDepartment of Pharmaceutical Sciences, University of Maryland School of Pharmacy, Baltimore, United States.
Daniel A BonsorInstitute of Human Virology, University of Maryland School of Medicine, Baltimore, United States.
Xiong YuDepartment of Biochemistry and Molecular Genetics, University of Virginia, Charlottesville, United States.
Kay DiederichsDepartment of Biology, University of Konstanz, Konstanz, Germany.
Saskia HelmsingDepartment of Biotechnology, Institute of Biochemistry, Biotechnology and Bioinformatics, Technische Universität Braunschweig, Braunschweig, Germany.
Aviv VromenInstitute of Chemistry, The Hebrew University of Jerusalem, Jerusalem, Israel.
Assaf FriedlerInstitute of Chemistry, The Hebrew University of Jerusalem, Jerusalem, Israel.
Michael HustDepartment of Biotechnology, Institute of Biochemistry, Biotechnology and Bioinformatics, Technische Universität Braunschweig, Braunschweig, Germany.
Edward H EgelmanDepartment of Biochemistry and Molecular Genetics, University of Virginia, Charlottesville, United States.ORCID 0000-0003-4844-5212
Dorothy BeckettDepartment of Chemistry and Biochemistry, University of Maryland College Park, Baltimore, United States.
Patrick L WintrodeDepartment of Pharmaceutical Sciences, University of Maryland School of Pharmacy, Baltimore, United States.
Eric J SundbergInstitute of Human Virology, University of Maryland School of Medicine, Baltimore, United States.ORCID 0000-0003-0478-3033
University of Maryland, Baltimore · USHebrew University of Jerusalem · ILTechnische Universität Braunschweig · DEUniversity of Virginia · USUniversity of Konstanz · DE

Funding

Purchase of a Beckman XL-1 Analytical UltracentrifugeS10RR015899 · NCRR · UNIVERSITY OF MARYLAND COLLEGE PK CAMPUS · PI BECKETT, DOROTHY · 2002 to 2002
$215k
NCRR NIH HHS S10 RR15899
6 · The paper itself

Abstract

Flagella are crucial for bacterial motility and pathogenesis. The flagellar capping protein (FliD) regulates filament assembly by chaperoning and sorting flagellin (FliC) proteins after they traverse the hollow filament and exit the growing flagellum tip. In the absence of FliD, flagella are not formed, resulting in impaired motility and infectivity. Here, we report the 2.2 Å resolution X-ray crystal structure of FliD from

Indexed as

Protein MultimerizationBacterial ProteinsCrystallography, X-RayFlagellinModels, MolecularProtein ConformationPseudomonas aeruginosaBacterial ProteinsFlaD protein, BacteriaFlagellinanalytical ultracentrifugationbiophysicsflagellahydrogen-deuterium exchangeinfectious diseasemicrobiologyPseudomonasstructural biologyX-ray crystallography

Identifiers

PMID27664419
PMCPMC5072837
OpenAlexW2522703115

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.