title: Potential mechanisms and implications for the formation of tau oligomeric strains.
abstract: The culmination of many years of increasing research into the toxicity of tau aggregation in neurodegenerative disease has led to the consensus that soluble, oligomeric forms of tau are likely the most toxic entities in disease. While tauopathies overlap in the presence of tau pathology, each disease has a unique combination of symptoms and pathological features; however, most study into tau has grouped tau oligomers and studied them as a homogenous population. Established evidence from the prion field combined with the most recent tau and amyloidogenic protein research suggests that tau is a prion-like protein, capable of seeding the spread of pathology throughout the brain. Thus, it is likely that tau may also form prion-like strains or diverse conformational structures that may differ by disease and underlie some of the differences in symptoms and pathology in neurodegenerative tauopathies. The development of techniques and new technology for the detection of tau oligomeric strains may, therefore, lead to more efficacious diagnostic and treatment strategies for neurodegenerative disease. [Formula: see text].
authors.affiliation: a George P. and Cynthia Woods Mitchell Center for Neurodegenerative Diseases, University of Texas Medical Branch , Galveston , TX , USA.|b Departments of Neurology, and Neuroscience and Cell Biology , University of Texas Medical Branch , Galveston , TX , USA.
authors.forename: Julia E
authors.initials: JE
authors.lastname: Gerson
authors.affiliation: c Faculty of Natural and Environmental Sciences , University of Southampton Highfield Campus, Center for Biological Sciences , Southampton , UK.
authors.forename: Amrit
authors.initials: A
authors.lastname: Mudher
authors.affiliation: a George P. and Cynthia Woods Mitchell Center for Neurodegenerative Diseases, University of Texas Medical Branch , Galveston , TX , USA.|b Departments of Neurology, and Neuroscience and Cell Biology , University of Texas Medical Branch , Galveston , TX , USA.
authors.forename: Rakez
authors.initials: R
authors.lastname: Kayed
mesh_terms: D000682:Amyloid / Q000378:metabolism*; D000818:Animals; D001921:Brain / Q000378:metabolism / Q000473:pathology; D006801:Humans; D000072002:Prion Proteins / Q000378:metabolism; D066329:Protein Aggregates; D066263:Protein Aggregation, Pathological / Q000378:metabolism* / Q000473:pathology; D024801:Tauopathies / Q000378:metabolism* / Q000473:pathology; D016875:tau Proteins / Q000378:metabolism*
chemical_list: D000682:Amyloid; D000072002:Prion Proteins; D066329:Protein Aggregates; D016875:tau Proteins
keywords: Tau; aggregation; amyloid; neurodegeneration; oligomer