Cerebrospinal fluid lipoproteins inhibit α-synuclein aggregation by interacting with oligomeric species in seed amplification assays.

Journal Information

Full Title: Mol Neurodegener

Abbreviation: Mol Neurodegener

Country: Unknown

Publisher: Unknown

Language: N/A

Publication Details

Subject Category: Molecular Biology

Available in Europe PMC: Yes

Available in PMC: Yes

PDF Available: No

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50.0% Transparent
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"Declarations Ethics approval and consent to participateAll the procedures involving human subjects were performed following the Helsinki Declaration. All patients and/or their legal representatives gave informed written consent for the lumbar puncture, CSF collection, assessment, analysis, and the inclusion in the study, that was approved by the local Ethics Committee (CEAS n 1287/08), University of Perugia. CSF samples were obtained with the informed consent of all participants. Consent for publicationNot applicable. Competing interestsThe authors declare the following competing financial interest(s): Prof. Parnetti served as Member of Advisory Boards for Fujirebio, IBL, Roche and Merck. Dr. Concha, Ms. Farris, and Mr. Ma are inventors on several patents related to SAA technology (PMCA) and are associated to Amprion Inc., a biotech company focused on the commercial utilization of SAA for diagnosis. All the other authors declare no financial and non-financial competing interests. Competing interests The authors declare the following competing financial interest(s): Prof. Parnetti served as Member of Advisory Boards for Fujirebio, IBL, Roche and Merck. Dr. Concha, Ms. Farris, and Mr. Ma are inventors on several patents related to SAA technology (PMCA) and are associated to Amprion Inc., a biotech company focused on the commercial utilization of SAA for diagnosis. All the other authors declare no financial and non-financial competing interests."

Evidence found in paper:

"Funding GB is supported by the Postdoctoral Fellowship for Basic Scientists grant of the Parkinson’s Foundation (Award ID: PF-PRF-934916). SP is funded by the Associazione Italiana Ricerca Alzheimer Onlus (Airalzh) grant AGYR2020. This work was partially supported by the Italian Ministry of Health (RRC) to FM. This work was also supported by Regione Toscana (CERM-TT and BioEnable), the Italian Ministero dell’Istruzione, dell’Università e della Ricerca through the “Progetto Dipartimenti di Eccellenza 2023–2027 (DICUS 2.0)” to the Department of Chemistry “Ugo Schiff” of the University of Florence, and the Recombinant Proteins JOYNLAB laboratory. The authors acknowledge the support and the use of resources of Instruct-ERIC, a landmark ESFRI project, and specifically the CERM/CIRMMP Italy centre, as well as the project “Potentiating the Italian Capacity for Structural Biology Services in Instruct-ERIC, Acronym “ITACA.SB” (Project no. IR0000009) within the call MUR 3264/2021 PNRR M4/C2/L3.1.1, funded by the European Union – NextGenerationEU. ALW is supported by the Marie Skłodowska-Curie grant agreement No. 86019 – MIRIADE project (European Union’s Horizon 2020 research and innovation program)."

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Last Updated: Aug 05, 2025