Neurobiology of Disease Inhibition of FK506 Binding Proteins Reduces -Synuclein Aggregation and Parkinson’s Disease-Like Pathology
نویسندگان
چکیده
Melanie Gerard,1,4 Angélique Deleersnijder,1,5 Veronique Daniëls,5 Sarah Schreurs,3 Sebastian Munck,6 Veerle Reumers,5 Hans Pottel,2 Yves Engelborghs,3 Chris Van den Haute,5 Jean-Marc Taymans,5 Zeger Debyser,1,4 and Veerle Baekelandt5 Laboratories of 1Biochemistry and 2Biophysics, Interdisciplinary Research Centre, Katholieke Universiteit Leuven-Kortrijk, B-8500 Kortrijk, Flanders, Belgium, 3Laboratory of Biomolecular Dynamics, Katholieke Universiteit Leuven, B-3001 Leuven, Flanders, Belgium, and Laboratories of 4Molecular Virology and Gene Therapy and 5Neurobiology and Gene Therapy and 6Flanders Institute for Biotechnology Department of Developmental and Molecular Genetics, Katholieke Universiteit Leuven, B-3000 Leuven, Flanders, Belgium
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Clioquinol-induced ordered conformational behavior in alpha-synuclein: promising relevance for therapeutic approach to Parkinson's disease
Parkinson?¦s disease (PD) is a devastating and an intricate complex neurological disorder that results from the progressive degeneration of nerve cells in Substantia nigra that controls movement. The pathological hallmark of PD is the formation of insoluble protein aggregates known as lewey bodies. Alpha-synuclein is the major constituent of these fibrillar structures. Alpha-synuclein a 140 ami...
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Alpha-synuclein (-synuclein) is considered a key player in Parkinson's disease (PD), but the exact relationship between-synuclein aggregation and dopaminergic (DA) neurodegeneration remains unresolved. There is increasing evidence that neuroinflammatory processes are closely linked to DA cell death, but whether the inflammatory process is causally involved in PD or rather reflects secondary con...
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