| http://purl.uniprot.org/citations/16037493 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16037493 | http://www.w3.org/2000/01/rdf-schema#comment | "Recent studies have begun to investigate the role of agrin in brain and suggest that agrin's function likely extends beyond that of a synaptogenic protein. Particularly, it has been shown that agrin is associated with the pathological lesions of Alzheimer's disease (AD) and may contribute to the formation of beta-amyloid (Abeta) plaques in AD. We have extended the analysis of agrin's function in neurodegenerative diseases to investigate its role in Parkinson's disease (PD). Alpha-synuclein is a critical molecular determinant in familial and sporadic PD, with the formation of alpha-synuclein fibrils being enhanced by sulfated macromolecules. In the studies reported here, we show that agrin binds to alpha-synuclein in a heparan sulfate-dependent (HS-dependent) manner, induces conformational changes in this protein characterized by beta-sheet structure, and enhances insolubility of alpha-synuclein. We also show that agrin accelerates the formation of protofibrils by alpha-synuclein and decreases the half-time of fibril formation. The association of agrin with PD lesions was also explored in PD human brain, and these studies shown that agrin colocalizes with alpha-synuclein in neuronal Lewy bodies in the substantia nigra of PD brain. These studies indicate that agrin is capable of accelerating the formation of insoluble protein fibrils in a second common neurodegenerative disease. These findings may indicate shared molecular mechanisms leading to the pathophysiology in these two neurodegenerative disorders."xsd:string |
| http://purl.uniprot.org/citations/16037493 | http://purl.org/dc/terms/identifier | "doi:10.1093/glycob/cwj014"xsd:string |
| http://purl.uniprot.org/citations/16037493 | http://purl.uniprot.org/core/author | "Uversky V.N."xsd:string |
| http://purl.uniprot.org/citations/16037493 | http://purl.uniprot.org/core/author | "Fink A.L."xsd:string |
| http://purl.uniprot.org/citations/16037493 | http://purl.uniprot.org/core/author | "Cole G.J."xsd:string |
| http://purl.uniprot.org/citations/16037493 | http://purl.uniprot.org/core/author | "Halfter W."xsd:string |
| http://purl.uniprot.org/citations/16037493 | http://purl.uniprot.org/core/author | "Liu I.H."xsd:string |
| http://purl.uniprot.org/citations/16037493 | http://purl.uniprot.org/core/author | "Munishkina L.A."xsd:string |
| http://purl.uniprot.org/citations/16037493 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
| http://purl.uniprot.org/citations/16037493 | http://purl.uniprot.org/core/name | "Glycobiology"xsd:string |
| http://purl.uniprot.org/citations/16037493 | http://purl.uniprot.org/core/pages | "1320-1331"xsd:string |
| http://purl.uniprot.org/citations/16037493 | http://purl.uniprot.org/core/title | "Agrin binds alpha-synuclein and modulates alpha-synuclein fibrillation."xsd:string |
| http://purl.uniprot.org/citations/16037493 | http://purl.uniprot.org/core/volume | "15"xsd:string |
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