Evidence map›Paper›PMID 35743250›Full record

ReviewInternational journal of molecular sciences2022

LRRK2 and Proteostasis in Parkinson's Disease.

María Dolores Pérez-Carrión, Inmaculada Posadas, Javier Solera, Valentín Ceña

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2022. 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
2.2field-weighted citation impact, top 11% 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

11 citing papers in PubMed, 18 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Article
  6. Review
  7. Article
  8. Review
  9. Review
  10. Review
  11. 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 2 institutions in 1 country.

María Dolores Pérez-CarriónUnidad Asociada Neurodeath, Universidad de Castilla-La Mancha, 02006 Albacete, Spain.ORCID 0000-0002-0178-173X
Inmaculada PosadasUnidad Asociada Neurodeath, Universidad de Castilla-La Mancha, 02006 Albacete, Spain.
Javier SoleraServicio de Medicina Interna, Complejo Hospitalario Universitario de Albacete, 02006 Albacete, Spain.
Valentín CeñaUnidad Asociada Neurodeath, Universidad de Castilla-La Mancha, 02006 Albacete, Spain.ORCID 0000-0001-8928-3681
Instituto de Salud Carlos III · ESComplejo Hospitalario Universitario de Albacete · ES

Funding

Comunidad de Castilla-La Mancha SBPLY/19/180501/000060Comunidad de Castilla-La Mancha SBPLY/19/180501/000067European Cooperation in Science and Technology CA17140Instituto de Salud Carlos III AC19/00075MICINN PID2020-120134RB-I00MICINN PRTR-C17.I1
6 · The paper itself

Abstract

Parkinson's disease is a neurodegenerative condition initially characterized by the presence of tremor, muscle stiffness and impaired balance, with the deposition of insoluble protein aggregates in Lewy's Bodies the histopathological hallmark of the disease. Although different gene variants are linked to Parkinson disease, mutations in the Leucine-Rich Repeat Kinase 2 (LRRK2) gene are one of the most frequent causes of Parkinson's disease related to genetic mutations. LRRK2 toxicity has been mainly explained by an increase in kinase activity, but alternative mechanisms have emerged as underlying causes for Parkinson's disease, such as the imbalance in LRRK2 homeostasis and the involvement of LRRK2 in aggregation and spreading of α-synuclein toxicity. In this review, we recapitulate the main LRRK2 pathological mutations that contribute to Parkinson's disease and the different cellular and therapeutic strategies devised to correct LRRK2 homeostasis. In this review, we describe the main cellular control mechanisms that regulate LRRK2 folding and aggregation, such as the chaperone network and the protein-clearing pathways such as the ubiquitin-proteasome system and the autophagic-lysosomal pathway. We will also address the more relevant strategies to modulate neurodegeneration in Parkinson's disease through the regulation of LRRK2, using small molecules or LRRK2 silencing.

Indexed as

Parkinson Diseasealpha-SynucleinHumansLeucine-Rich Repeat Serine-Threonine Protein Kinase-2LysosomesMutationProteostasisalpha-SynucleinLeucine-Rich Repeat Serine-Threonine Protein Kinase-2LRRK2 protein, humanautophagychaperonesLRRK2LRRK2 silencingParkinson’s diseaseproteostasisα-synuclein

Identifiers

PMID35743250
PMCPMC9224256
OpenAlexW4283121266

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.