Evidence map›Paper›PMID 29494603›Full record

ArticlePloS one2018

Lipopolysaccharide-binding protein (LBP) can reverse the amyloid state of fibrin seen or induced in Parkinson's disease.

Etheresia Pretorius, Martin J Page, Sthembile Mbotwe, Douglas B Kell

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed, 1 pooled it
4.1field-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

30 citing papers in PubMed, 1 synthesis or guideline pooled it, 47 citations in OpenAlex.

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  18. Is Porphyromonas gingivalis involved in Parkinson's disease?European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2020
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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

4 authors at 2 institutions in 2 countries.

Etheresia PretoriusDepartment of Physiological Sciences, Faculty of Science, Stellenbosch University, Stellenbosch, South Africa.ORCID 0000-0002-9108-2384
Martin J PageDepartment of Physiological Sciences, Faculty of Science, Stellenbosch University, Stellenbosch, South Africa.ORCID 0000-0002-2479-9182
Sthembile MbotweDepartment of Physiology, Faculty of Health Sciences, University of Pretoria, Arcadia, South Africa.
Douglas B KellDepartment of Physiological Sciences, Faculty of Science, Stellenbosch University, Stellenbosch, South Africa.
Stellenbosch University · ZAUniversity of Pretoria · ZA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The thrombin-induced polymerisation of fibrinogen to form fibrin is well established as a late stage of blood clotting. It is known that Parkinson's Disease (PD) is accompanied by dysregulation in blood clotting, but it is less widely known as a coagulopathy. In recent work, we showed that the presence of tiny amounts of bacterial lipopolysaccharide (LPS) in healthy individuals could cause clots to adopt an amyloid form, and this could be observed via scanning electron microscopy (SEM) or via the fluorescence of thioflavin-T. This could be prevented by the prior addition of lipopolysaccharide-binding protein (LBP). We had also observed by SEM this unusual clotting in the blood of patients with Parkinson's Disease. We hypothesised, and here show, that this too can be prevented by LBP in the context of PD. This adds further evidence implicating inflammatory microbial cell wall products as an accompaniment to the disease, and may be part of its aetiology. This may lead to novel treatment strategies in PD designed to target microbes and their products.

Indexed as

Acute-Phase ProteinsAgedAmyloidBlood CoagulationCarrier ProteinsDrug DiscoveryFemaleFibrinHumansLipopolysaccharide-Binding ProteinLipopolysaccharidesMaleMembrane GlycoproteinsMiddle AgedParkinson DiseaseAcute-Phase ProteinsAmyloidCarrier ProteinsFibrinLipopolysaccharide-Binding ProteinLipopolysaccharidesMembrane Glycoproteins

Identifiers

PMID29494603
PMCPMC5832207
OpenAlexW2789710373

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.