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@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},
}