| http://purl.uniprot.org/citations/18541383 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/18541383 | http://www.w3.org/2000/01/rdf-schema#comment | "Aggregation of alpha-synuclein may contribute to neuropathology in Parkinson's disease patients and in transgenic animal models. Natively unfolded alpha-synuclein binds to various proteins and conformational changes due to alpha-synuclein misfolding may alter physiological interactions. In the present study, we used protein arrays spotted with 5000 recombinant human proteins for a large scale interaction analysis of monomeric versus oligomeric alpha-synuclein. Monomeric alpha-synuclein bound to arrayed cAMP regulated phosphoprotein 19 and binding appears to be disrupted by alpha-synuclein oligomerization. Incubation with recombinant alpha-synuclein oligomers lead to the identification of several GTPase activating proteins and Cdc42 effector proteins as binding partners. Protein database searches revealed a Cdc42/Rac interactive binding domain in some interactors. To demonstrate in vivo relevance, we analyzed brainstem protein extracts from alpha-synuclein(A30P) transgenic mice. Pull-down assays using beads conjugated with a Cdc42/Rac interactive binding domain lead to an enrichment of endogenous alpha-synuclein oligomers. Cdc42 effector proteins were also co-immunoprecipitated with alpha-synuclein from brainstem lysates and were colocalized with alpha-synuclein aggregates in brain sections by double immunostaining. By two-dimensional gel electrophoretic analysis of synaptosomal fractions from transgenic mouse brains we detected additional isoforms of septin 6, a downstream target of Cdc42 effector proteins. Small GTPases have recently been identified in a genetic modifier screen to suppress alpha-synuclein toxicity in yeast. Our data indicate that components of small GTPase signal transduction pathways may be directly targeted by alpha-synuclein oligomers which potentially leads to signaling deficits and neurodegeneration."xsd:string |
| http://purl.uniprot.org/citations/18541383 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.neuroscience.2008.02.049"xsd:string |
| http://purl.uniprot.org/citations/18541383 | http://purl.uniprot.org/core/author | "Hengerer B."xsd:string |
| http://purl.uniprot.org/citations/18541383 | http://purl.uniprot.org/core/author | "Danzer K.M."xsd:string |
| http://purl.uniprot.org/citations/18541383 | http://purl.uniprot.org/core/author | "Gillardon F."xsd:string |
| http://purl.uniprot.org/citations/18541383 | http://purl.uniprot.org/core/author | "Schnack C."xsd:string |
| http://purl.uniprot.org/citations/18541383 | http://purl.uniprot.org/core/date | "2008"xsd:gYear |
| http://purl.uniprot.org/citations/18541383 | http://purl.uniprot.org/core/name | "Neuroscience"xsd:string |
| http://purl.uniprot.org/citations/18541383 | http://purl.uniprot.org/core/pages | "1450-1457"xsd:string |
| http://purl.uniprot.org/citations/18541383 | http://purl.uniprot.org/core/title | "Protein array analysis of oligomerization-induced changes in alpha-synuclein protein-protein interactions points to an interference with Cdc42 effector proteins."xsd:string |
| http://purl.uniprot.org/citations/18541383 | http://purl.uniprot.org/core/volume | "154"xsd:string |
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