Evidence map›Paper›PMID 30304819›Full record

ReviewInternational journal of molecular sciences2018

Attempt to Untangle the Prion-Like Misfolding Mechanism for Neurodegenerative Diseases.

Daniela Sarnataro

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed, 2 pooled it
2.0field-weighted citation impact, top 12% 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

23 citing papers in PubMed, 2 syntheses or guidelines pooled it, 33 citations in OpenAlex.

  1. Pooled it
  2. Pooled it
  3. Article
  4. Review
  5. Emerging roles of the cellular prion protein (PrPCellular and molecular life sciences : CMLS · 2023
    Review
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  7. Review
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  19. Rationale for the development of an Alzheimer's disease vaccine.Human vaccines & immunotherapeutics · 2020
    Article
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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

1 author at 1 institution in 1 country.

Daniela SarnataroDepartment of Molecular Medicine and Medical Biotechnology, University of Naples Federico II, School of Medicine, Via S. Pansini 5, 80131 Naples, Italy. daniela.sarnataro1@gmail.com.ORCID 0000-0002-6094-8384
University of Naples Federico II · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The misfolding and aggregation of proteins is the neuropathological hallmark for numerous diseases including Alzheimer's disease, Parkinson's disease, and prion diseases. It is believed that misfolded and abnormal β-sheets forms of wild-type proteins are the vectors of these diseases by acting as seeds for the aggregation of endogenous proteins. Cellular prion protein (PrP

Indexed as

Protein FoldingAlzheimer DiseaseAmyloidogenic ProteinsAnimalsCell MembraneDisease SusceptibilityEndoplasmic ReticulumGenetic VariationGolgi ApparatusHumansIntrinsically Disordered ProteinsNeurodegenerative DiseasesPrion ProteinsProtein BindingProtein Processing, Post-TranslationalProteostasis DeficienciesAmyloidogenic ProteinsIntrinsically Disordered ProteinsPrion ProteinsaggregationamyloidAPPAβmisfoldingprion-likeprion proteinPrPseedstau

Identifiers

PMID30304819
PMCPMC6213118
OpenAlexW2896770793

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.