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Despite clinical, genetic and experimental differences, increasing evidence indicates considerable overlap between synucleinopathies, tauopathies and other protein\u2010misfolding diseases. Inclusions, often characteristic hallmarks of these disorders, suggest interactions of pathological proteins enganging common downstream pathways. Novel findings that have shifted our understanding in the role of pathologic proteins in the pathogenesis of<jats:styled-content style=\"fixed-case\">A<\/jats:styled-content>lzheimer,<jats:styled-content style=\"fixed-case\">P<\/jats:styled-content>arkinson,<jats:styled-content style=\"fixed-case\">H<\/jats:styled-content>untington and prion diseases, have confirmed correlations\/overlaps between these and other neurodegenerative disorders. Emerging evidence, in addition to synergistic effects of tau protein, amyloid\u2010\u03b2, \u03b1\u2010synuclein and other pathologic proteins, suggests that prion\u2010like induction and spreading, involving secreted proteins, are major pathogenic mechanisms in various neurodegenerative diseases, depending on genetic backgrounds and environmental factors. The elucidation of the basic molecular mechanisms underlying the interaction and spreading of pathogenic proteins, suggesting a dualism or triad of neurodegeneration in protein\u2010misfolding disorders, is a major challenge for modern neuroscience, to provide a deeper insight into their pathogenesis as a basis of effective diagnosis and treatment.<\/jats:p>","DOI":"10.1111\/j.1582-4934.2011.01507.x","type":"journal-article","created":{"date-parts":[[2011,12,16]],"date-time":"2011-12-16T17:07:28Z","timestamp":1324055248000},"page":"1166-1183","source":"Crossref","is-referenced-by-count":108,"title":["Interaction between pathogenic proteins in neurodegenerative disorders"],"prefix":"10.1111","volume":"16","author":[{"given":"Kurt A.","family":"Jellinger","sequence":"first","affiliation":[{"name":"Institute of Clinical Neurobiology Vienna 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