PMID: 19149675Jan 20, 2009Paper

Structure solution of misfolded conformations adopted by intrinsically disordered Alzheimer's tau protein

Protein and Peptide Letters
Jozef SevcikMichal Novak

Abstract

Until now it was impossible to obtain atomic structure of intrinsically disordered protein (IDP) tau and/or its assembly in Alzheimer's paired helical filaments as neither of them could have been prepared in the form amenable to X-ray or NMR techniques. Using IDP tau property to attain regular tertiary structure after binding events during self-assembly or when complexed with its target we propose monoclonal antibodies as surrogate tau protein binding partners to form complexes and crystals for structure solution by X-ray technique.

Citations

Mar 24, 2010·The Journal of Biological Chemistry·Umesh K JinwalChad A Dickey
Oct 3, 2012·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·Ondrej CehlarMichal Novak
Oct 3, 2012·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·Rostislav SkrabanaMichal Novak
Jun 6, 2017·Acta Crystallographica. Section F, Structural Biology Communications·Martina MaritanEnrico Malito

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