% IMPORTANT: The following is UTF-8 encoded. This means that in the presence % of non-ASCII characters, it will not work with BibTeX 0.99 or older. % Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or % “biber”. @ARTICLE{Albus:1021436, author = {Albus, Alexandra and Kronimus, Yannick and Burg-Roderfeld, Monika and van der Wurp, Hendrik and Willbold, Dieter and Ziehm, Tamar and Dodel, Richard and Ross, Jean Alexander}, title = {{T}he {A}vidity of {A}utoreactive {A}lpha-{S}ynuclein {A}ntibodies in {L}eucine-{R}ich {R}epeat {K}inase 2 {M}utation {C}arriers {I}s {N}ot {A}ltered {C}ompared to {H}ealthy {C}ontrols or {P}atients with {P}arkinson’s {D}isease}, journal = {Biomolecules}, volume = {13}, number = {9}, issn = {2218-273X}, address = {Basel}, publisher = {MDPI}, reportid = {FZJ-2024-00732}, pages = {1303 -}, year = {2023}, abstract = {The 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. We investigated the serum titers and binding characteristics of nAbs-α-Syn in patients suffering from sporadic Parkinson's disease (n = 38), LRRK2 mutation carriers (n = 25), and healthy controls (n = 22).}, cin = {IBI-7}, ddc = {570}, cid = {I:(DE-Juel1)IBI-7-20200312}, pnm = {5244 - Information Processing in Neuronal Networks (POF4-524)}, pid = {G:(DE-HGF)POF4-5244}, typ = {PUB:(DE-HGF)16}, pubmed = {37759704}, UT = {WOS:001074350200001}, doi = {10.3390/biom13091303}, url = {https://juser.fz-juelich.de/record/1021436}, }