P2–044: Inducible cell models of tauopathy show that tau aggregation is toxic to cells, but tau pathology can be reversed | Zendy

Biernat Jacek | Zendy; Khlistunova Inna | Zendy; Wang Yipeng | Zendy; Pickhardt Marcus | Zendy; Gazova Zuzana | Zendy; Mandelkow Eva Maria | Zendy

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P2–044: Inducible cell models of tauopathy show that tau aggregation is toxic to cells, but tau pathology can be reversed

Author(s) -

Biernat Jacek,

Khlistunova Inna,

Wang Yipeng,

Pickhardt Marcus,

Gazova Zuzana,

Mandelkow Eva Maria

Publication year - 2006

Publication title -

alzheimer's and dementia

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 6.713

H-Index - 118

eISSN - 1552-5279

pISSN - 1552-5260

DOI - 10.1016/j.jalz.2006.05.881

Subject(s) - tauopathy , neurodegeneration , mutant , tau protein , protein aggregation , chemistry , phosphorylation , microbiology and biotechnology , biophysics , biology , biochemistry , alzheimer's disease , medicine , disease , gene

antibody (detection). 2) Taking advantage of an APP construct containing an N-terminal secreted alkaline phosphatase (SEAP) domain, we have also developed a convenient hybrid ELISA-SEAP assay. This assay utilizes the -site-specific antibody to capture SEAP-tagged sAPP in cell culture media, followed by alkaline phosphatase substrate metabolism for easy colorimetric detection. Conclusions: These methods offer valuable tools to develop a new and potential biomarker of AD and to discover therapeutic agents that target the -cleavage of APP in cell-based assays.

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