1. Tau and Neuron Aging
Jesus Avila 1, 2 ;Elena Gomez de Barreda 1, 2 ;Noemi Pallas-Bazarra 1, 2 ;Felix Hernandez 1, 2 ;
1 Centro de Biología Molecular Severo Ochoa, CSIC-UAM, Madrid, Spain. ; 2 Centro de Investigación Biomédica en Red sobre Enfermedades Neurodegenerativas (CIBERNED), Spain. ;
Figure Scheme of tau molecule. Upper part is showing the longest central nervous system human tau isoform. In gray, the presence of two exons 2 and 3 is indicated and, in black, that of the four similar, but not identical R1 to R4 tubulin binding regions. Lower part shows tau molecule divided in four parts. A Indicates the most variable parte of the molecule, when tau molecules from different organism are compared. B Shows a proline rich region that could be highly modified by phosphorylation. C Indicates the tubulin binding region. D Shows the C-terminal region that could be also modified by phosphorylation, at several residues. Inset shows the shortest and longest human tau isoforms. The first is mainly present in fetal F brain whereas the second is present in adult A brain.
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