Evidence map›Paper›PMID 38612739›Full record

ReviewInternational journal of molecular sciences2024

Is There a Place for Lewy Bodies before and beyond Alpha-Synuclein Accumulation? Provocative Issues in Need of Solid Explanations.

Paola Lenzi, Gloria Lazzeri, Michela Ferrucci, Marco Scotto, Alessandro Frati, Stefano Puglisi-Allegra, Carla Letizia Busceti, Francesco Fornai

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.8field-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

6 citing papers in PubMed, 5 citations in OpenAlex.

  1. 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

8 authors at 2 institutions in 1 country.

Paola LenziHuman Anatomy, Department of Translational Research and New Technologies in Medicine and Surgery, University of Pisa, 56126 Pisa, Italy.ORCID 0000-0002-4734-8798
Gloria LazzeriHuman Anatomy, Department of Translational Research and New Technologies in Medicine and Surgery, University of Pisa, 56126 Pisa, Italy.
Michela FerrucciHuman Anatomy, Department of Translational Research and New Technologies in Medicine and Surgery, University of Pisa, 56126 Pisa, Italy.ORCID 0009-0001-1446-715X
Marco ScottoHuman Anatomy, Department of Translational Research and New Technologies in Medicine and Surgery, University of Pisa, 56126 Pisa, Italy.
Alessandro FratiIRCCS-Istituto di Ricovero e Cura a Carattere Scientifico, Neuromed, 86077 Pozzili, Italy.ORCID 0000-0001-8062-614X
Stefano Puglisi-AllegraIRCCS-Istituto di Ricovero e Cura a Carattere Scientifico, Neuromed, 86077 Pozzili, Italy.
Carla Letizia BuscetiIRCCS-Istituto di Ricovero e Cura a Carattere Scientifico, Neuromed, 86077 Pozzili, Italy.
Francesco FornaiHuman Anatomy, Department of Translational Research and New Technologies in Medicine and Surgery, University of Pisa, 56126 Pisa, Italy.ORCID 0000-0002-3883-5084
University of Pisa · ITIstituti di Ricovero e Cura a Carattere Scientifico · IT

Funding

Ministero della Salute Ricerca Corrente 2024PRIN 2017 2017XZ7A37_002
6 · The paper itself

Abstract

In the last two decades, alpha-synuclein (alpha-syn) assumed a prominent role as a major component and seeding structure of Lewy bodies (LBs). This concept is driving ongoing research on the pathophysiology of Parkinson's disease (PD). In line with this, alpha-syn is considered to be the guilty protein in the disease process, and it may be targeted through precision medicine to modify disease progression. Therefore, designing specific tools to block the aggregation and spreading of alpha-syn represents a major effort in the development of disease-modifying therapies in PD. The present article analyzes concrete evidence about the significance of alpha-syn within LBs. In this effort, some dogmas are challenged. This concerns the question of whether alpha-syn is more abundant compared with other proteins within LBs. Again, the occurrence of alpha-syn compared with non-protein constituents is scrutinized. Finally, the prominent role of alpha-syn in seeding LBs as the guilty structure causing PD is questioned. These revisited concepts may be helpful in the process of validating which proteins, organelles, and pathways are likely to be involved in the damage to meso-striatal dopamine neurons and other brain regions involved in PD.

Indexed as

alpha-SynucleinParkinson DiseaseCorpus StriatumDisease ProgressionHumansLewy Bodiesalpha-Synucleinautophagoproteasosomeautophagosomeendosomelysosomemitochondriamultivesicular bodiesphagophorepoly-ubiquitinretromersequestosome (p62)

Identifiers

PMID38612739
PMCPMC11011529
OpenAlexW4393379990

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.