Evidence map›Paper›PMID 26987594›Full record

ArticleNature communications2016

Structure and mechanism of the essential two-component signal-transduction system WalKR in Staphylococcus aureus.

Quanjiang Ji, Peter J Chen, Guangrong Qin, Xin Deng, Ziyang Hao, Zdzislaw Wawrzak, Won-Sik Yeo, Jenny Winjing Quang, Hoonsik Cho, Guan-Zheng Luo and 8 more

RetractedOpen access · goldAbstract readRetracted Publication
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It has been retracted, and should not be counted. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
4.2field-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

18 citing papers in PubMed, 36 citations in OpenAlex.

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  11. The EMBO journal · 2018
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  14. Frontiers in microbiology · 2018
    Review
  15. Article
  16. Review
  17. Article
  18. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

18 authors at 7 institutions in 2 countries.

Quanjiang JiDepartment of Chemistry, Department of Biochemistry and Molecular Biology, and Institute for Biophysical Dynamics, Howard Hughes Medical Institute, The University of Chicago, 929 East 57th Street, Chicago, Illinois 60637, USA.
Peter J ChenDepartment of Chemistry, Department of Biochemistry and Molecular Biology, and Institute for Biophysical Dynamics, Howard Hughes Medical Institute, The University of Chicago, 929 East 57th Street, Chicago, Illinois 60637, USA.
Guangrong QinState Key Laboratory of Drug Research, Drug Discovery and Design Center, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203, China.
Xin DengDepartment of Chemistry, Department of Biochemistry and Molecular Biology, and Institute for Biophysical Dynamics, Howard Hughes Medical Institute, The University of Chicago, 929 East 57th Street, Chicago, Illinois 60637, USA.
Ziyang HaoDepartment of Chemistry, Department of Biochemistry and Molecular Biology, and Institute for Biophysical Dynamics, Howard Hughes Medical Institute, The University of Chicago, 929 East 57th Street, Chicago, Illinois 60637, USA.
Zdzislaw WawrzakSynchrotron Research Center, LS-CAT, Northwestern University, Argonne, Illinois 60439, USA.
Won-Sik YeoIndiana University School of Medicine-Northwest, Gary, Indiana 46408, USA.
Jenny Winjing QuangHigh-Throughput Analysis Laboratory, Department of Molecular Biosciences, Center for Structural Genomics of Infectious Diseases, Northwestern University, Evanston, Illinois 60208, USA.
Hoonsik ChoIndiana University School of Medicine-Northwest, Gary, Indiana 46408, USA.
Guan-Zheng LuoDepartment of Chemistry, Department of Biochemistry and Molecular Biology, and Institute for Biophysical Dynamics, Howard Hughes Medical Institute, The University of Chicago, 929 East 57th Street, Chicago, Illinois 60637, USA.
Xiaocheng WengDepartment of Chemistry, Department of Biochemistry and Molecular Biology, and Institute for Biophysical Dynamics, Howard Hughes Medical Institute, The University of Chicago, 929 East 57th Street, Chicago, Illinois 60637, USA.
Qiancheng YouDepartment of Chemistry, Department of Biochemistry and Molecular Biology, and Institute for Biophysical Dynamics, Howard Hughes Medical Institute, The University of Chicago, 929 East 57th Street, Chicago, Illinois 60637, USA.
Chi-Hao LuanHigh-Throughput Analysis Laboratory, Department of Molecular Biosciences, Center for Structural Genomics of Infectious Diseases, Northwestern University, Evanston, Illinois 60208, USA.
Xiaojing YangDepartment of Biochemistry and Molecular Biology, University of Chicago, 929 E 57th Street, Chicago, Illinois 60637, USA.
Taeok BaeIndiana University School of Medicine-Northwest, Gary, Indiana 46408, USA.
Kunqian YuState Key Laboratory of Drug Research, Drug Discovery and Design Center, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203, China.
Hualiang JiangState Key Laboratory of Drug Research, Drug Discovery and Design Center, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203, China.
Chuan HeDepartment of Chemistry, Department of Biochemistry and Molecular Biology, and Institute for Biophysical Dynamics, Howard Hughes Medical Institute, The University of Chicago, 929 East 57th Street, Chicago, Illinois 60637, USA.
Howard Hughes Medical Institute · USChinese Academy of Sciences · CNUniversity of Chicago · USIndiana University Northwest · USNorthwestern University · USArgonne National Laboratory · USIndiana University School of Medicine

Funding

Tuning Virulence Determinants in Staphylococcus aureusR01AI074658 · NIAID · UNIVERSITY OF CHICAGO · PI HE, CHUAN · 2007 to 2016
$3.8M
Howard Hughes Medical InstituteNIAID NIH HHS AI074658NIAID NIH HHS R01 AI074658
6 · The paper itself

Abstract

Most low GC Gram-positive bacteria possess an essential walKR two-component system (TCS) for signal transduction involved in regulating cell wall homoeostasis. Despite the well-established intracellular regulatory mechanism, the role of this TCS in extracellular signal recognition and factors that modulate the activity of this TCS remain largely unknown. Here we identify the extracellular receptor of the kinase 'WalK' (erWalK) as a key hub for bridging extracellular signal input and intracellular kinase activity modulation in Staphylococcus aureus. Characterization of the crystal structure of erWalK revealed a canonical Per-Arnt-Sim (PAS) domain for signal sensing. Single amino-acid mutation of potential signal-transduction residues resulted in severely impaired function of WalKR. A small molecule derived from structure-based virtual screening against erWalK is capable of selectively activating the walKR TCS. The molecular level characterization of erWalK will not only facilitate exploration of natural signal(s) but also provide a template for rational design of erWalK inhibitors.

Indexed as

Signal TransductionBacterial ProteinsBenzophenonesCrystallography, X-RayGene Expression Regulation, BacterialMutant ProteinsMutationProtein Structure, TertiarySmall Molecule LibrariesStaphylococcus aureusTranscription, Genetic2,4-dihydroxybenzophenoneBacterial ProteinsBenzophenonesMutant ProteinsSmall Molecule Libraries

Identifiers

PMID26987594
PMCPMC4802049
OpenAlexW2301270613

What OpenQuestion holds

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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.