Evidence map›Paper›PMID 22205299›Full record

ReviewMolecular neurobiology2012

Synaptic protein alterations in Parkinson's disease.

Ilse S Pienaar, David Burn, Christopher Morris, David Dexter

Abstract readReview
PubMed Publisher
In one paragraph

Review in Molecular neurobiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed, 2 pooled it
1.9field-weighted citation impact, top 15% 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

14 citing papers in PubMed, 2 syntheses or guidelines pooled it, 29 citations in OpenAlex.

  1. Pooled it
  2. Pooled it
  3. Trial
  4. Review
  5. Article
  6. Article
  7. Impaired synaptic function is linked to cognition in Parkinson's disease.Annals of clinical and translational neurology · 2017
    Article
  8. Cognitive decline in Parkinson disease.Nature reviews. Neurology · 2017
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. 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

4 authors at 4 institutions in 2 countries.

Ilse S PienaarInstitute for Ageing and Health, Department of Neurology, The University of Newcastle, Newcastle-Upon-Tyne, UK. ilse-sanet.pienaar@ncl.ac.uk
David Burn
Christopher Morris
David Dexter
Imperial College London · GBNewcastle Hospitals - Campus for Ageing and Vitality · GBNewcastle University · GBUniversity of Newcastle Australia · AU

Funding

Medical Research Council
6 · The paper itself

Abstract

Alterations occur within distal neuronal compartments, including axons and synapses, during the course of neurodegenerative diseases such as Parkinson's disease (PD). These changes could hold important implications for the functioning of neural networks, especially since research studies have shown a loss of dendritic spines locating to medium spiny projection neurons and impaired axonal transport in PD-affected brains. However, despite ever-increasing awareness of the vulnerability of synapses and axons, inadequate understanding of the independent mechanisms regulating non-somatic neurodegeneration prevails. This has resulted in limited therapeutic strategies capable of targeting these distinct cellular compartments. Deregulated protein synthesis, folding and degrading proteins, and protein quality-control systems have repeatedly been linked with morphological and functional alterations of synapses in the PD-affected brains. Here, we review current understanding concerning the proteins involved in structural and functional changes that affect synaptic contact-points in PD. The collection of studies discussed emphasizes the need for developing therapeutics aimed at deregulated protein synthesis and degradation pathways operating at axonal and dendritic synapses for preserving "normal" circuitry and function, for as long as possible.

Indexed as

alpha-SynucleinAnimalsHumansNerve DegenerationNerve Tissue ProteinsParkinson DiseaseSynapsesSynaptic MembranesSynaptic Transmissionalpha-SynucleinNerve Tissue Proteins

Identifiers

PMID22205299
OpenAlexW2074594911

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.