Evidence map›Paper›PMID 34613701›Full record

ArticleBiomacromolecules2021

Cationic Carbosilane Dendrimers Prevent Abnormal α-Synuclein Accumulation in Parkinson's Disease Patient-Specific Dopamine Neurons.

Raquel Ferrer-Lorente, Tania Lozano-Cruz, Irene Fernández-Carasa, Katarzyna Miłowska, Francisco Javier de la Mata, Maria Bryszewska, Antonella Consiglio, Paula Ortega, Rafael Gómez, Angel Raya

Open access · hybridAbstract read
In one paragraph

Article in Biomacromolecules, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.5field-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

7 citing papers in PubMed, 20 citations in OpenAlex.

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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

10 authors at 4 institutions in 3 countries.

Raquel Ferrer-LorenteRegenerative Medicine Program, and Program for Clinical Translation of Regenerative Medicine in Catalonia─P-CMR[C], L'Hospitalet de Llobregat (Barcelona), Institut d'Investigació Biomèdica de Bellvitge─IDIBELL, Barcelona 08907, Spain.
Tania Lozano-CruzUniversity of Alcalá, Department of Organic Chemistry and Inorganic Chemistry and Research Institute in Chemistry "Andrés M. del Río" (IQAR), Madrid 28805, Spain.
Irene Fernández-CarasaDepartment of Pathology and Experimental Therapeutics, Hospitalet de Llobregat (Barcelona), Universitat de Barcelona and Institut d'Investigació Biomèdica de Bellvitge─IDIBELL, Barcelona 08907, Spain.
Katarzyna MiłowskaDepartment of General Biophysics, Faculty of Biology and Environmental Protection, University of Lodz, Pomorska 141/143, Lodz 90-236, Poland.ORCID 0000-0002-4050-2756
Francisco Javier de la MataNetworking Research Center on Bioengineering, Biomaterials and Nanomedicine (CIBER-BBN), Madrid 28029, Spain.ORCID 0000-0003-0418-3935
Maria BryszewskaDepartment of General Biophysics, Faculty of Biology and Environmental Protection, University of Lodz, Pomorska 141/143, Lodz 90-236, Poland.
Antonella ConsiglioDepartment of Pathology and Experimental Therapeutics, Hospitalet de Llobregat (Barcelona), Universitat de Barcelona and Institut d'Investigació Biomèdica de Bellvitge─IDIBELL, Barcelona 08907, Spain.
Paula OrtegaNetworking Research Center on Bioengineering, Biomaterials and Nanomedicine (CIBER-BBN), Madrid 28029, Spain.ORCID 0000-0003-0377-5429
Rafael GómezNetworking Research Center on Bioengineering, Biomaterials and Nanomedicine (CIBER-BBN), Madrid 28029, Spain.ORCID 0000-0001-6448-2414
Angel RayaRegenerative Medicine Program, and Program for Clinical Translation of Regenerative Medicine in Catalonia─P-CMR[C], L'Hospitalet de Llobregat (Barcelona), Institut d'Investigació Biomèdica de Bellvitge─IDIBELL, Barcelona 08907, Spain.
Universidad de Alcalá · ESInstitut d'Investigació Biomédica de Bellvitge · ESUniversity of Łódź · PLInstitució Catalana de Recerca i Estudis Avançats · ES

Funding

NIMHD NIH HHS L60 MD003733
6 · The paper itself

Abstract

Accumulation of misfolded α-synuclein (α-syn) is a hallmark of Parkinson's disease (PD) thought to play important roles in the pathophysiology of the disease. Dendritic systems, able to modulate the folding of proteins, have emerged as promising new therapeutic strategies for PD treatment. Dendrimers have been shown to be effective at inhibiting α-syn aggregation in cell-free systems and in cell lines. Here, we set out to investigate the effects of dendrimers on endogenous α-syn accumulation in disease-relevant cell types from PD patients. For this purpose, we chose cationic carbosilane dendrimers of bow-tie topology based on their performance at inhibiting α-syn aggregation

Indexed as

alpha-SynucleinDendrimersParkinson DiseaseDopaminergic NeuronsHumansLeucine-Rich Repeat Serine-Threonine Protein Kinase-2Silanesalpha-SynucleincarbosilaneDendrimersLeucine-Rich Repeat Serine-Threonine Protein Kinase-2LRRK2 protein, humanSilanesSNCA protein, human

Identifiers

PMID34613701
PMCPMC8906628
OpenAlexW3204679360

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.