Evidence map›Paper›PMID 29676205›Full record

ArticlePrion2018

Effects of peptidyl-prolyl isomerase 1 depletion in animal models of prion diseases.

Giuseppe Legname, Tommaso Virgilio, Edoardo Bistaffa, Chiara Maria Giulia De Luca, Marcella Catania, Paola Zago, Elisa Isopi, Ilaria Campagnani, Fabrizio Tagliavini, Giorgio Giaccone and 1 more

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

Article in Prion, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.3field-weighted citation impact, top 43% 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

2 citing papers in PubMed, 4 citations in OpenAlex.

  1. Review
  2. Review
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

11 authors at 2 institutions in 2 countries.

Giuseppe Legnamea Laboratory of Prion Biology, Department of Neuroscience , Scuola Internazionale Superiore di Studi Avanzati (SISSA) , Trieste , Italy.
Tommaso Virgiliob Unit of Neuropathology and Neurology 5 , IRCCS Foundation Carlo Besta Neurological Institute , Milano , Italy.ORCID 0000-0002-9326-8828
Edoardo Bistaffaa Laboratory of Prion Biology, Department of Neuroscience , Scuola Internazionale Superiore di Studi Avanzati (SISSA) , Trieste , Italy.
Chiara Maria Giulia De Lucab Unit of Neuropathology and Neurology 5 , IRCCS Foundation Carlo Besta Neurological Institute , Milano , Italy.ORCID 0000-0002-6233-8272
Marcella Cataniab Unit of Neuropathology and Neurology 5 , IRCCS Foundation Carlo Besta Neurological Institute , Milano , Italy.
Paola Zagoa Laboratory of Prion Biology, Department of Neuroscience , Scuola Internazionale Superiore di Studi Avanzati (SISSA) , Trieste , Italy.
Elisa Isopia Laboratory of Prion Biology, Department of Neuroscience , Scuola Internazionale Superiore di Studi Avanzati (SISSA) , Trieste , Italy.
Ilaria Campagnanib Unit of Neuropathology and Neurology 5 , IRCCS Foundation Carlo Besta Neurological Institute , Milano , Italy.
Fabrizio Tagliavinib Unit of Neuropathology and Neurology 5 , IRCCS Foundation Carlo Besta Neurological Institute , Milano , Italy.
Giorgio Giacconeb Unit of Neuropathology and Neurology 5 , IRCCS Foundation Carlo Besta Neurological Institute , Milano , Italy.
Fabio Modab Unit of Neuropathology and Neurology 5 , IRCCS Foundation Carlo Besta Neurological Institute , Milano , Italy.
Fondazione IRCCS Istituto Neurologico Carlo Besta · ITScuola Internazionale Superiore di Studi Avanzati · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Pin1 is a peptidyl-prolyl isomerase that induces the cis-trans conversion of specific Ser/Thr-Pro peptide bonds in phosphorylated proteins, leading to conformational changes through which Pin1 regulates protein stability and activity. Since down-regulation of Pin1 has been described in several neurodegenerative disorders, including Alzheimer's Disease (AD), Parkinson's Disease (PD) and Huntington's Disease (HD), we investigated its potential role in prion diseases. Animals generated on wild-type (Pin1

Indexed as

AnimalsDisease Models, AnimalNIMA-Interacting Peptidylprolyl IsomerasePeptidylprolyl IsomerasePhosphorylationPrion DiseasesPrion ProteinsNIMA-Interacting Peptidylprolyl IsomerasePeptidylprolyl IsomerasePrion ProteinsneurodegenerationPin1PMCAprion

Identifiers

PMID29676205
PMCPMC6016513
OpenAlexW2802984751

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.