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Article

FK506 binding protein 12 differentially accelerates fibril formation of wild type alpha-synuclein and its clinical mutants A30P or A53T.

Journal of neurochemistry - 1 Jul 2008

Gerard Melanie, Debyser Zeger, Desender Linda, Baert Johan, Brandt Inger, Baekelandt Veerle, Engelborghs Yves

Abstract excerpt

Aggregation of alpha-synuclein (alpha-SYN) plays a key role in Parkinson's disease. We have previously shown that aggregation of alpha-SYN in vitro is accelerated by addition of FK506 binding proteins (FKBP) and that this effect can be counteracted by FK506, a specific inhibitor of these enzymes....

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Identifiers

PMID: 18346205
DOI: 10.1111/j.1471-4159.2008.05342.x

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-18346205-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

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