Evidence map›Paper›PMID 34750787›Full record

ReviewMolecular neurobiology2022

An Update on the Critical Role of α-Synuclein in Parkinson's Disease and Other Synucleinopathies: from Tissue to Cellular and Molecular Levels.

Iris N Serratos, Elizabeth Hernández-Pérez, Carolina Campos, Michael Aschner, Abel Santamaría

Abstract readReview
PubMed Publisher
In one paragraph

Review in Molecular neurobiology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
4.1field-weighted citation impact, top 5% 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

33 citing papers in PubMed, 59 citations in OpenAlex.

  1. Review
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  5. Aesculus hippocastanum Extract Exerts Neuroprotective Effects in an MPPJournal of cellular and molecular medicine · 2026
    Article
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  10. Article
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  14. Long noncoding RNAs in ubiquitination, protein degradation, and human diseases.Biochimica et biophysica acta. Gene regulatory mechanisms · 2024
    Review
  15. Review
  16. Article
  17. Review
  18. Liquid-liquid phase separation and conformational strains ofFrontiers in molecular neuroscience · 2024
    Review
  19. 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

5 authors at 3 institutions in 2 countries.

Iris N Serratos *Departamento de Química, Universidad Autónoma Metropolitana-Iztapalapa, 09340, Mexico City, Mexico.
Elizabeth Hernández-Pérez *Departamento de Ciencias de La Salud, Universidad Autónoma Metropolitana-Iztapalapa, 09340, Mexico City, Mexico.
Carolina Campos *Departamento de Ciencias de La Salud, Universidad Autónoma Metropolitana-Iztapalapa, 09340, Mexico City, Mexico. caro@xanum.uam.mx.
Michael AschnerDepartment of Molecular Pharmacology, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY, 10461, USA.
Abel SantamaríaLaboratorio de Aminoácidos Excitadores/Laboratorio de Neurofarmacología Molecular y Nanotecnología, Instituto Nacional de Neurología y Neurocirugía, SSA, 14269, Mexico City, Mexico. absada@yahoo.com.
Universidad Autónoma Metropolitana · MXAlbert Einstein College of Medicine · USInstituto Nacional de Neurología y Neurocirugía · MX

Funding

Mechanisms of Manganese NeurotoxicityR01ES010563 · NIEHS · WAKE FOREST UNIVERSITY HEALTH SCIENCES · PI Michael Aschner, Aaron B Bowman · 2001 to 2026
$11.9M
EFFECTS OF DEHP ON LIVERR01ES003771 · NIEHS · WASHINGTON STATE UNIVERSITY · PI OKITA, RICHARD T. · 1986 to 1997
–
NIEHS NIH HHS R01ES03771NIEHS NIH HHS R01ES10563
6 · The paper itself

Abstract

The aggregation of alpha-synuclein (α-Syn) plays a critical role in the development of Parkinson's disease (PD) and other synucleinopathies. α-Syn, which is encoded by the SNCA gene, is a lysine-rich soluble amphipathic protein normally expressed in neurons. Located in the cytosolic domain, this protein has the ability to remodel itself in plasma membranes, where it assumes an alpha-helix conformation. However, the protein can also adopt another conformation rich in cross-beta sheets, undergoing mutations and post-translational modifications, then leading the protein to an unusual aggregation in the form of Lewy bodies (LB), which are cytoplasmic inclusions constituted predominantly by α-Syn. Pathogenic mechanisms affecting the structural and functional stability of α-Syn - such as endoplasmic reticulum stress, Golgi complex fragmentation, disfunctional protein degradation systems, aberrant interactions with mitochondrial membranes and nuclear DNA, altered cytoskeleton dynamics, disrupted neuronal plasmatic membrane, dysfunctional vesicular transport, and formation of extracellular toxic aggregates - contribute all to the pathogenic progression of PD and synucleinopathies. In this review, we describe the collective knowledge on this topic and provide an update on the critical role of α-Syn aggregates, both at the cellular and molecular levels, in the deregulation of organelles affecting the cellular homeostasis and leading to neuronal cell death in PD and other synucleinopathies.

Indexed as

alpha-SynucleinAnimalsBrainHumansNeuronsParkinson DiseaseSynucleinopathiesalpha-SynucleinLewy bodiesMembrane biological interactionsOrganellesParkinson’s diseasePost-translational modificationsSynucleinopathiesα-Synuclein

Identifiers

PMID34750787
OpenAlexW3213543525

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.