Evidence map›Paper›PMID 22923367›Full record

ReviewMolecular neurobiology2013

Recent advances in α-synuclein functions, advanced glycation, and toxicity: implications for Parkinson's disease.

Erika Guerrero, P Vasudevaraju, Muralidhar L Hegde, G B Britton, K S Rao

Abstract readReview
PubMed Publisher
In one paragraph

Review in Molecular neurobiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
4.5field-weighted citation impact, top 6% 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

54 citing papers in PubMed, 113 citations in OpenAlex.

  1. Gut microbes · 2026
    Article
  2. Review
  3. Immune signaling and function in neurodegeneration.The Journal of clinical investigation · 2026
    Review
  4. Review
  5. Review
  6. Article
  7. Review
  8. Review
  9. Review
  10. Article
  11. Posttranslational Modifications ofPharmacological reviews · 2024
    Review
  12. Review
  13. International journal of molecular sciences · 2023
    Review
  14. Role of neuroinflammation in neurodegeneration development.Signal transduction and targeted therapy · 2023
    Review
  15. Article
  16. Review
  17. Review
  18. Review
  19. Review
  20. The association between urinary pentosidine levels and cognition in drug-naïve patients with Parkinson's disease.Neurological sciences : official journal of the Italian Neurological Society and of the Italian Society of Clinical Neurophysiology · 2022
    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

5 authors at 4 institutions in 2 countries.

Erika GuerreroCentre for Neuroscience, Institute for Scientific Research and Technological Services (INDICASAT-AIP), City of Knowledge, Panama, Republic of Panama.
P Vasudevaraju
Muralidhar L Hegde
G B Britton
K S Rao
Instituto de Investigaciones Científicas y Servicios de Alta Tecnología · PACity of Knowledge · PAMedical University of South Carolina · USThe University of Texas Medical Branch at Galveston · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The toxicity of α-synuclein in the neuropathology of Parkinson's disease which includes its hallmark aggregation has been studied scrupulously in the last decade. Although little is known regarding the normal functions of α-synuclein, its association with membrane phospholipids suggests its potential role in signaling pathways. Following extensive evidences for its nuclear localization, we and others recently demonstrated DNA binding activity of α-synuclein that modulates its conformation as well as aggregation properties. Furthermore, we also underscored the similarities among various amyloidogenic proteins involved in neurodegenerative diseases including amyloid beta peptides and tau. Our more recent studies show that α-synuclein is glycated and glycosylated both in vitro and in neurons, significantly affecting its folding, oligomeric, and DNA binding properties. Glycated α-synuclein causes increased genome damage both via its direct interaction with DNA and by increased generation of reactive oxygen species as glycation byproduct. In this review, we discuss the mechanisms of glycation and other posttranslational modifications of α-synuclein, including phosphorylation and nitration, and their role in neuronal death in Parkinson's disease.

Indexed as

alpha-SynucleinAnimalsCell DeathGlycation End Products, AdvancedGlycosylationHumansParkinson DiseasePhosphorylationProtein BindingProtein Foldingalpha-SynucleinGlycation End Products, Advanced

Identifiers

PMID22923367
OpenAlexW2088529103

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.