{"id":{"repo_id":"utswmed","oai_identifier":"oai:utswmed-ir.tdl.org:2152.5/10634"},"canonical_url":"https://search.dev.ndltd.org/etd/utswmed/oai:utswmed-ir.tdl.org:2152.5/10634","repository":{"repo_id":"utswmed","name":"University of Texas Southwestern Medical Center","base_url":"https://utswmed-ir.tdl.org/server/oai/request"},"display":{"title":"On the Structure and Function of Tau Assemblies in Neurodegenerative Diseases","abstract":"The general metadata -- e.g., title, author, abstract, subject headings, etc. -- is publicly available, but access to the submitted files is restricted to UT Southwestern campus access and/or authorized UT Southwestern users.","abstract_html":"The general metadata -- e.g., title, author, abstract, subject headings, etc. -- is publicly available, but access to the submitted files is restricted to UT Southwestern campus access and/or authorized UT Southwestern users.","abstract_has_math":false,"creators":["Vaquer Alicea, Jaime, III"],"institution":null,"degree_name":null,"degree_level":null,"degree_discipline":null,"degree_department":null,"school":null,"contributors":["Douglas, Peter","Saelices Gomez, Lorena","Joachimiak, Lukasz","Meeks, Julian P.","Diamond, Marc"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2025,"date_issued":"2025-06-03T19:58:47Z","date_published":"2025-06-03T19:58:47Z","updated_at":"2026-07-24T05:52:17Z","subjects":["tau Proteins","Tauopathies"],"languages":["en"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["1522122388"],"render_values":[{"text":"1522122388","href":null,"code":true}]}]},"links":{"outbound_url":"https://hdl.handle.net/2152.5/10634","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Douglas, Peter","Saelices Gomez, Lorena","Joachimiak, Lukasz","Meeks, Julian P.","Diamond, Marc"]},{"key":"dc:creator","label":"Author","values":["Vaquer Alicea, Jaime, III"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2025-06-03T19:58:47Z","2023-05","May 2023"]},{"key":"dc:type","label":"Dc Type","values":["Thesis","text"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["tau Proteins","Tauopathies"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["en"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["https://hdl.handle.net/2152.5/10634","1522122388"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["The general metadata -- e.g., title, author, abstract, subject headings, etc. -- is publicly available, but access to the submitted files is restricted to UT Southwestern campus access and/or authorized UT Southwestern users.","Tauopathies, a group of neurodegenerative diseases characterized by aggregation of tau protein, are heterogeneous clinically and pathologically. Recent cryo-EM studies of tau filaments derived from diseased brains have confirmed that most tauopathies are associated with a unique fold, or strain, of misfolded and aggregated tau. It is unclear how tau strains form, or how they relate to the pathogenesis of disease. However, inoculation experiments into the brains of mice have shown that distinct strains of tau encode sufficient information to cause unique and transmissible neuropathology. We and others have proposed that this information transfer, in the form of templated aggregation, or seeding, is necessary for disease progression in tauopathies. This model predicts that identifying the conformations of seeding-competent tau in patients with tauopathies may aid in diagnosis and treatment. Here, we address the need for quick and accurate tools that enable the discrimination of tau strains. We develop a method to classify samples containing aggregated tau based on their ability to seed new aggregates of mutated tau in cells. Our findings offer valuable implications for the development of targeted diagnostic and therapeutic approaches for tauopathies and other neurodegenerative disorders."]},{"key":"dc:format","label":"Dc Format","values":["application/pdf"]},{"key":"dc:title","label":"Title","values":["On the Structure and Function of Tau Assemblies in Neurodegenerative Diseases"]}]}],"canonical_facts":{"dc:contributor":["Douglas, Peter","Saelices Gomez, Lorena","Joachimiak, Lukasz","Meeks, Julian P.","Diamond, Marc"],"dc:creator":["Vaquer Alicea, Jaime, III"],"dc:date":["2025-06-03T19:58:47Z","2023-05","May 2023"],"dc:description":["The general metadata -- e.g., title, author, abstract, subject headings, etc. -- is publicly available, but access to the submitted files is restricted to UT Southwestern campus access and/or authorized UT Southwestern users.","Tauopathies, a group of neurodegenerative diseases characterized by aggregation of tau protein, are heterogeneous clinically and pathologically. Recent cryo-EM studies of tau filaments derived from diseased brains have confirmed that most tauopathies are associated with a unique fold, or strain, of misfolded and aggregated tau. It is unclear how tau strains form, or how they relate to the pathogenesis of disease. However, inoculation experiments into the brains of mice have shown that distinct strains of tau encode sufficient information to cause unique and transmissible neuropathology. We and others have proposed that this information transfer, in the form of templated aggregation, or seeding, is necessary for disease progression in tauopathies. This model predicts that identifying the conformations of seeding-competent tau in patients with tauopathies may aid in diagnosis and treatment. Here, we address the need for quick and accurate tools that enable the discrimination of tau strains. We develop a method to classify samples containing aggregated tau based on their ability to seed new aggregates of mutated tau in cells. Our findings offer valuable implications for the development of targeted diagnostic and therapeutic approaches for tauopathies and other neurodegenerative disorders."],"dc:format":["application/pdf"],"dc:identifier":["https://hdl.handle.net/2152.5/10634","1522122388"],"dc:language":["en"],"dc:subject":["tau Proteins","Tauopathies"],"dc:title":["On the Structure and Function of Tau Assemblies in Neurodegenerative Diseases"],"dc:type":["Thesis","text"]},"updated_at":"2026-07-24T05:52:17Z"}