Evidence map›Paper›PMID 30877199›Full record

ArticleThe Journal of biological chemistry2019

Crystal structure of the TreS:Pep2 complex, initiating α-glucan synthesis in the GlgE pathway of mycobacteria.

Ali A Kermani, Rana Roy, Chai Gopalasingam, Klaudia I Kocurek, Trushar R Patel, Luke J Alderwick, Gurdyal S Besra, Klaus Fütterer

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.6field-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

6 citing papers in PubMed, 11 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

8 authors at 1 institution in 1 country.

Ali A KermaniFrom the Institute of Microbiology & Infection, School of Biosciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, United Kingdom.
Rana RoyFrom the Institute of Microbiology & Infection, School of Biosciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, United Kingdom.
Chai GopalasingamFrom the Institute of Microbiology & Infection, School of Biosciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, United Kingdom.
Klaudia I KocurekFrom the Institute of Microbiology & Infection, School of Biosciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, United Kingdom.
Trushar R PatelFrom the Institute of Microbiology & Infection, School of Biosciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, United Kingdom.ORCID 0000-0003-0627-2923
Luke J AlderwickFrom the Institute of Microbiology & Infection, School of Biosciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, United Kingdom.ORCID 0000-0002-1257-6053
Gurdyal S BesraFrom the Institute of Microbiology & Infection, School of Biosciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, United Kingdom G.Besra@bham.ac.uk.
Klaus FüttererFrom the Institute of Microbiology & Infection, School of Biosciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, United Kingdom k.futterer@bham.ac.uk.ORCID 0000-0001-7445-5372
University of Birmingham · GB

Funding

Medical Research Council MR/K012118/1Medical Research Council MR/S000542/1Wellcome TrustWellcome Trust 084923/B/08/Z
6 · The paper itself

Abstract

A growing body of evidence implicates the mycobacterial capsule, the outermost layer of the mycobacterial cell envelope, in modulation of the host immune response and virulence of mycobacteria. Mycobacteria synthesize the dominant capsule component, α(1→4)-linked glucan, via three interconnected and potentially redundant metabolic pathways. Here, we report the crystal structure of the

Indexed as

Bacterial ProteinsCatalytic DomainCrystallography, X-RayGlucansGlucosyltransferasesMycobacterium smegmatisPhosphotransferases (Alcohol Group Acceptor)Protein ConformationSolutionsBacterial ProteinsGlucansGlucosyltransferasesmaltokinasePhosphotransferases (Alcohol Group Acceptor)Solutionstrehalose synthaseanalytical ultracentrifugationcapsuleenzyme catalysisimmune evasionmaltose kinasemycobacteriapathogenesisprotein complextrehalosetrehalose synthaseX-ray crystallographyα-glucan

Identifiers

PMID30877199
PMCPMC6509496
OpenAlexW2921629006

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.