Tauomics and Kinetics in Human Neurons and Biological Fluids

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Tauomics and Kinetics in Human Neurons and Biological Fluids Henrik Zetterberg Neuron Volume 97, Issue 6, Pages 1202-1205 (March 2018) DOI: 10.1016/j.neuron.2018.02.030 Copyright © 2018 Elsevier Inc. Terms and Conditions

Figure 1 Tau Is a Complicated and Heterogeneous Biomarker (A) There are at least six isoforms of tau as a result of alternative splicing of exons two, three, and ten. These isoforms contain three or four microtubule-binding domains (green boxes; the fourth domain is in exon 10; numbers to the right in the panel denote the number of amino acids in each isoform). (B) Numerous threonine and serine phosphorylation sites have been identified in tau. In addition to phosphorylation, tau may also be proteolytically processed and potentially also oxidized and glycosylated, which increases the complexity further. Neuron 2018 97, 1202-1205DOI: (10.1016/j.neuron.2018.02.030) Copyright © 2018 Elsevier Inc. Terms and Conditions