Evidence map›Paper›PMID 24819168›Full record

ArticlePrion

Lipopolysaccharide induced conversion of recombinant prion protein.

Fozia Saleem, Trent C Bjorndahl, Carol L Ladner, Rolando Perez-Pineiro, Burim N Ametaj, David S Wishart

Open access · bronzeAbstract read
In one paragraph

Article in Prion. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

17 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
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  4. Review
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  9. Brain-Gut-Microbiota Axis in Alzheimer's Disease.Journal of neurogastroenterology and motility · 2019
    Review
  10. Review
  11. Article
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  15. Article
  16. Microbial-generated amyloids and Alzheimer's disease (AD).Frontiers in aging neuroscience · 2015
    Article
  17. 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 2 institutions in 2 countries.

Fozia SaleemDepartment of Biological Sciences; University of Alberta; Edmonton, AB Canada.
Trent C BjorndahlDepartment of Computing Science; University of Alberta; Edmonton, AB Canada.
Carol L LadnerDepartment of Computing Science; University of Alberta; Edmonton, AB Canada; National Institute for Nanotechnology; Edmonton, AB Canada.
Rolando Perez-PineiroDepartment of Computing Science; University of Alberta; Edmonton, AB Canada.
Burim N AmetajDepartment of Agricultural, Food and Nutritional Science; University of Alberta; Edmonton, AB Canada.
David S WishartDepartment of Biological Sciences; University of Alberta; Edmonton, AB Canada; Department of Computing Science; University of Alberta; Edmonton, AB Canada; National Institute for Nanotechnology; Edmonton, AB Canada.
University of Alberta · CANational Institute for Nanotechnology · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The conformational conversion of the cellular prion protein (PrP(C)) to the β-rich infectious isoform PrP(Sc) is considered a critical and central feature in prion pathology. Although PrP(Sc) is the critical component of the infectious agent, as proposed in the "protein-only" prion hypothesis, cellular components have been identified as important cofactors in triggering and enhancing the conversion of PrP(C) to proteinase K resistant PrP(Sc). A number of in vitro systems using various chemical and/or physical agents such as guanidine hydrochloride, urea, SDS, high temperature, and low pH, have been developed that cause PrP(C) conversion, their amplification, and amyloid fibril formation often under non-physiological conditions. In our ongoing efforts to look for endogenous and exogenous chemical mediators that might initiate, influence, or result in the natural conversion of PrP(C) to PrP(Sc), we discovered that lipopolysaccharide (LPS), a component of gram-negative bacterial membranes interacts with recombinant prion proteins and induces conversion to an isoform richer in β sheet at near physiological conditions as long as the LPS concentration remains above the critical micelle concentration (CMC). More significant was the LPS mediated conversion that was observed even at sub-molar ratios of LPS to recombinant ShPrP (90-232).

Indexed as

Hot TemperatureHydrogen-Ion ConcentrationLipopolysaccharidesMicroscopy, ElectronPrionsProtein DenaturationRecombinant ProteinsLipopolysaccharidesPrionsRecombinant Proteinsbeta oligomerfibrillipopolysaccharideprion proteinprotein misfolding

Identifiers

PMID24819168
PMCPMC4189894
OpenAlexW2001874106

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.