001021436 001__ 1021436 001021436 005__ 20240226075347.0 001021436 0247_ $$2doi$$a10.3390/biom13091303 001021436 0247_ $$2datacite_doi$$a10.34734/FZJ-2024-00732 001021436 0247_ $$2pmid$$a37759704 001021436 0247_ $$2WOS$$aWOS:001074350200001 001021436 037__ $$aFZJ-2024-00732 001021436 082__ $$a570 001021436 1001_ $$00000-0002-4897-6972$$aAlbus, Alexandra$$b0 001021436 245__ $$aThe Avidity of Autoreactive Alpha-Synuclein Antibodies in Leucine-Rich Repeat Kinase 2 Mutation Carriers Is Not Altered Compared to Healthy Controls or Patients with Parkinson’s Disease 001021436 260__ $$aBasel$$bMDPI$$c2023 001021436 3367_ $$2DRIVER$$aarticle 001021436 3367_ $$2DataCite$$aOutput Types/Journal article 001021436 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article$$bjournal$$mjournal$$s1705586202_20685 001021436 3367_ $$2BibTeX$$aARTICLE 001021436 3367_ $$2ORCID$$aJOURNAL_ARTICLE 001021436 3367_ $$00$$2EndNote$$aJournal Article 001021436 520__ $$aThe accumulation and aggregation of alpha-synuclein (α-Syn) are pathological processes associated with Parkinson's disease, indicating that the regulation of protein is a crucial etiopathological mechanism. Interestingly, human serum and cerebrospinal fluid contain autoantibodies that recognize α-Syn. This potentially demonstrates an already existing, naturally decomposing, and protective system. Thus, quantitative or qualitative alterations, such as the modified antigen binding of so-called naturally occurring autoantibodies against α-Syn (nAbs-α-Syn), may induce disease onset and/or progression. 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