Evidence map›Paper›PMID 24636457›Full record

ReviewTrends in neurosciences2014

Kaleidoscopic protein-protein interactions in the life and death of ataxin-1: new strategies against protein aggregation.

Cesira de Chiara, Annalisa Pastore

Abstract readReview
In one paragraph

Review in Trends in neurosciences, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
–field-weighted citation impact
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

11 citing papers in PubMed.

  1. Review
  2. The bacterial tyrosine kinase system CpsBCD governs the length of capsule polymers.Proceedings of the National Academy of Sciences of the United States of America · 2021
    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

2 authors.

Cesira de ChiaraNational Institute for Medical Research (NIMR), Medical Research Council (MRC), The Ridgeway, London NW7 1AA, UK.
Annalisa PastoreDepartment of Clinical Neurosciences, King's College London, Denmark Hill Campus, London, UK. Electronic address: apastor@nimr.mrc.ac.uk.

Funding

Medical Research Council MC_PC_13054Medical Research Council MC_U117584256Medical Research Council U117584256
6 · The paper itself

Abstract

Understanding how proteins protect themselves from aberrant aggregation is of primary interest for understanding basic biology, protein biochemistry, and human disease. We discuss the paradigmatic example of ataxin-1 (Atx1), the protein responsible for neurodegenerative spinocerebellar ataxia type 1 (SCA1). This disease is part of the increasing family of pathologies caused by protein aggregation and misfolding. We discuss the importance of protein-protein interactions not only in the nonpathological function of Atx1 but also in protecting the protein from aggregation and misfolding. The lessons learned from Atx1 may lead to a more general understanding of the cell's protective strategies against aggregation. The obtained knowledge may suggest a new perspective for designing specific therapeutic strategies for the cure of misfolding diseases.

Indexed as

AnimalsAtaxin-1AtaxinsDNA Repeat ExpansionDrug DesignHeredodegenerative Disorders, Nervous SystemHumansNerve Tissue ProteinsNuclear ProteinsPeptidesProtein AggregatesProtein Aggregation, PathologicalProtein FoldingProtein MultimerizationAtaxin-1AtaxinsATXN1 protein, humanNerve Tissue ProteinsNuclear ProteinsPeptidespolyglutamineProtein Aggregatesmisfolding diseasespolyglutamineprotein aggregationprotein–protein interactions

Identifiers

PMID24636457
PMCPMC3988977

What OpenQuestion holds

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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.