Evidence map›Paper›PMID 31729381›Full record

ArticleNature communications2019

Multiple conformations facilitate PilT function in the type IV pilus.

Matthew McCallum, Samir Benlekbir, Sheryl Nguyen, Stephanie Tammam, John L Rubinstein, Lori L Burrows, P Lynne Howell

Open access · greenAbstract read
In one paragraph

Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.1field-weighted citation impact, top 22% 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

21 citing papers in PubMed, 20 citations in OpenAlex.

  1. Structural modeling reveals the mechanism of motor ATPase coordination during type IV pilus retraction.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Article
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  4. Genomic characterization of a pathogenicFrontiers in microbiology · 2026
    Article
  5. Separation ofmBio · 2025
    Article
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  19. Motile ghosts of the halophilic archaeon,Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  20. 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

7 authors at 3 institutions in 1 country.

Matthew McCallumDepartment of Biochemistry, University of Toronto, Toronto, ON, M5S 1A8, Canada.
Samir BenlekbirProgram in Molecular Structure & Function, Peter Gilgan Centre for Research and Learning, The Hospital for Sick Children, Toronto, ON, M5G 0A4, Canada.
Sheryl NguyenProgram in Molecular Structure & Function, Peter Gilgan Centre for Research and Learning, The Hospital for Sick Children, Toronto, ON, M5G 0A4, Canada.
Stephanie TammamProgram in Molecular Structure & Function, Peter Gilgan Centre for Research and Learning, The Hospital for Sick Children, Toronto, ON, M5G 0A4, Canada.
John L RubinsteinDepartment of Biochemistry, University of Toronto, Toronto, ON, M5S 1A8, Canada. john.rubinstein@utoronto.ca.ORCID http://orcid.org/0000-0003-0566-2209
Lori L BurrowsDepartment of Biochemistry and Biomedical Sciences and the Michael G. DeGroote Institute for Infectious Disease Research, McMaster University, Hamilton, ON, L8S 4K1, Canada. burrowl@mcmaster.ca.ORCID http://orcid.org/0000-0003-0838-5040
P Lynne HowellDepartment of Biochemistry, University of Toronto, Toronto, ON, M5S 1A8, Canada. howell@sickkids.ca.ORCID http://orcid.org/0000-0002-2776-062X
Hospital for Sick Children · CAUniversity of Toronto · CAMcMaster University · CA

Funding

Gouvernement du Canada | Canadian Institutes of Health Research (Instituts de Recherche en Santé du Canada) MOP 93585
6 · The paper itself

Abstract

Type IV pilus-like systems are protein complexes that polymerize pilin fibres. They are critical for virulence in many bacterial pathogens. Pilin polymerization and depolymerization are powered by motor ATPases of the PilT/VirB11-like family. This family is thought to operate with C

Indexed as

Adenosine TriphosphatasesBacterial ProteinsCaulobacterCrystallography, X-RayFimbriae, BacterialMultigene FamilyProtein ConformationAdenosine TriphosphatasesBacterial Proteins

Identifiers

PMID31729381
PMCPMC6858323
OpenAlexW2984142937

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.