Evidence map›Paper›PMID 29372905›Full record

ArticleActa crystallographica. Section F, Structural biology communications2018

Production, biophysical characterization and initial crystallization studies of the N- and C-terminal domains of DsbD, an essential enzyme in Neisseria meningitidis.

Roxanne P Smith, Andrew E Whitten, Jason J Paxman, Charlene M Kahler, Martin J Scanlon, Begoña Heras

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Acta crystallographica. Section F, Structural biology communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.2field-weighted citation impact, top 31% 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

1 citing paper in PubMed, 1 citations in OpenAlex.

  1. 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

6 authors at 4 institutions in 1 country.

Roxanne P SmithDepartment of Biochemistry and Genetics, La Trobe Institute for Molecular Science, La Trobe University, Bundoora, Victoria 3086, Australia.
Andrew E WhittenAustralian Centre for Neutron Scattering, Australian Nuclear Science and Technology Organisation, New South Wales 2234, Australia.ORCID 0000-0001-8856-3120
Jason J PaxmanDepartment of Biochemistry and Genetics, La Trobe Institute for Molecular Science, La Trobe University, Bundoora, Victoria 3086, Australia.ORCID 0000-0002-1418-5910
Charlene M KahlerSchool of Pathology and Laboratory Medicine, The University of Western Australia, Crawley, Western Australia 6009, Australia.
Martin J ScanlonMedicinal Chemistry, Monash Institute of Pharmaceutical Sciences, Monash University, Parkville, Victoria 3052, Australia.ORCID 0000-0002-9230-7506
Begoña HerasDepartment of Biochemistry and Genetics, La Trobe Institute for Molecular Science, La Trobe University, Bundoora, Victoria 3086, Australia.ORCID 0000-0003-3469-7988
La Trobe University · AUAustralian Nuclear Science and Technology Organisation · AUMonash University · AUThe University of Western Australia · AU

Funding

Australian Research Council DP150102287Australian Research Council FT130100580National Health and Medical Research Council APP1099151National Health and Medical Research Council APP546003
6 · The paper itself

Abstract

The membrane protein DsbD is a reductase that acts as an electron hub, translocating reducing equivalents from cytoplasmic thioredoxin to a number of periplasmic substrates involved in oxidative protein folding, cytochrome c maturation and oxidative stress defence. DsbD is a multi-domain protein consisting of a transmembrane domain (t-DsbD) flanked by two periplasmic domains (n-DsbD and c-DsbD). Previous studies have shown that DsbD is required for the survival of the obligate human pathogen Neisseria meningitidis. To help understand the structural and functional aspects of N. meningitidis DsbD, the two periplasmic domains which are required for electron transfer are being studied. Here, the expression, purification and biophysical properties of n-NmDsbD and c-NmDsbD are described. The crystallization and crystallographic analysis of n-NmDsbD and c-NmDsbD are also described in both redox states, which differ only in the presence or absence of a disulfide bond but which crystallized in completely different conditions. Crystals of n-NmDsbD

Indexed as

Amino Acid SequenceBacterial ProteinsBiophysical PhenomenaCrystallizationCrystallography, X-RayElectron TransportModels, MolecularNeisseria meningitidisOxidoreductasesProtein DomainsRecombinant ProteinsScattering, Small AngleX-Ray DiffractionBacterial ProteinsOxidoreductasesRecombinant Proteinsdisulfide catalysisDsbDmembrane proteinsNeisseria meningitidis

Identifiers

PMID29372905
PMCPMC5947690
OpenAlexW2780713419

What OpenQuestion holds

Textmetadata
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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.