Evidence map›Paper›PMID 29991595›Full record

ArticleThe Journal of biological chemistry2018

Three SpoA-domain proteins interact in the creation of the flagellar type III secretion system in

Kwok Ho Lam, Chaolun Xue, Kailei Sun, Huawei Zhang, Wendy Wai Ling Lam, Zeyu Zhu, Juliana Tsz Yan Ng, William E Sause, Paphavee Lertsethtakarn, Kwok Fai Lau and 2 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.8field-weighted citation impact, top 30% 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

5 citing papers in PubMed, 8 citations in OpenAlex.

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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

12 authors at 3 institutions in 2 countries.

Kwok Ho LamFrom the Center for Protein Science and Crystallography, School of Life Sciences, Faculty of Science, Chinese University of Hong Kong, Shatin, Hong Kong.ORCID 0000-0002-7173-6600
Chaolun XueFrom the Center for Protein Science and Crystallography, School of Life Sciences, Faculty of Science, Chinese University of Hong Kong, Shatin, Hong Kong.
Kailei SunFrom the Center for Protein Science and Crystallography, School of Life Sciences, Faculty of Science, Chinese University of Hong Kong, Shatin, Hong Kong.
Huawei ZhangFrom the Center for Protein Science and Crystallography, School of Life Sciences, Faculty of Science, Chinese University of Hong Kong, Shatin, Hong Kong.ORCID 0000-0002-5625-5809
Wendy Wai Ling LamFrom the Center for Protein Science and Crystallography, School of Life Sciences, Faculty of Science, Chinese University of Hong Kong, Shatin, Hong Kong.
Zeyu ZhuFrom the Center for Protein Science and Crystallography, School of Life Sciences, Faculty of Science, Chinese University of Hong Kong, Shatin, Hong Kong.
Juliana Tsz Yan NgFrom the Center for Protein Science and Crystallography, School of Life Sciences, Faculty of Science, Chinese University of Hong Kong, Shatin, Hong Kong.
William E SauseDepartment of Microbiology and Environmental Toxicology, University of California, Santa Cruz, California 95064.
Paphavee LertsethtakarnDepartment of Microbiology and Environmental Toxicology, University of California, Santa Cruz, California 95064.
Kwok Fai LauFrom the Center for Protein Science and Crystallography, School of Life Sciences, Faculty of Science, Chinese University of Hong Kong, Shatin, Hong Kong.
Karen M OttemannDepartment of Microbiology and Environmental Toxicology, University of California, Santa Cruz, California 95064.
Shannon Wing Ngor AuFrom the Center for Protein Science and Crystallography, School of Life Sciences, Faculty of Science, Chinese University of Hong Kong, Shatin, Hong Kong, shannon-au@cuhk.edu.hk.ORCID 0000-0002-3573-9273
Chinese University of Hong Kong · CNUniversity of California, Santa Cruz · USChinese University of Hong Kong, Shenzhen · CN

Funding

Roles for Motility in Helicobactor pylori pathogenesisR01AI050000 · NIAID · UNIVERSITY OF CALIFORNIA SANTA CRUZ · PI OTTEMANN, KAREN M · 2002 to 2011
$3.6M
NIAID NIH HHS R01 AI050000
6 · The paper itself

Abstract

Bacterial flagella are rotary nanomachines that contribute to bacterial fitness in many settings, including host colonization. The flagellar motor relies on the multiprotein flagellar motor-switch complex to govern flagellum formation and rotational direction. Different bacteria exhibit great diversity in their flagellar motors. One such variation is exemplified by the motor-switch apparatus of the gastric pathogen

Indexed as

Protein Interaction Domains and MotifsProtein MultimerizationBacterial ProteinsCrystallography, X-RayFlagellaHelicobacter pyloriMembrane ProteinsMultiprotein ComplexesProtein DomainsType III Secretion SystemsBacterial ProteinsFlig protein, BacteriaFliM protein, BacteriaFliN protein, BacteriaFliY protein, BacteriaMembrane ProteinsMultiprotein ComplexesType III Secretion Systemsbacterial motilityflagellar motor switch complexflagellumFli proteinFliYHelicobacter pylorimolecular motorprotein assemblyprotein exportprotein-protein interactionprotein structureSpoA domaintype III secretion systemvirulence factor

Identifiers

PMID29991595
PMCPMC6130963
OpenAlexW2833412004

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.