| First Author | Lee G | Year | 1988 |
| Journal | Science | Volume | 239 |
| Issue | 4837 | Pages | 285-8 |
| PubMed ID | 3122323 | Mgi Jnum | J:27179 |
| Mgi Id | MGI:74596 | Doi | 10.1126/science.3122323 |
| Citation | Lee G, et al. (1988) The primary structure and heterogeneity of tau protein from mouse brain. Science 239(4837):285-8 |
| abstractText | Tau protein is a family of microtubule binding proteins, heterogeneous in molecular weight, that are induced during neurite outgrowth and are found prominently in neurofibrillary tangles in Alzheimer's disease. The predicted amino acid sequences of two forms of tau protein from mouse brain were determined from complementary DNA clones. These forms are identical in their amino-terminal sequences but differ in their carboxyl-terminal domains. Both proteins contain repeated sequences that may be tubulin binding sites. The sequence suggests that tau is an elongated molecule with no extensive alpha-helical or beta-sheet domains. These complementary DNAs should enable the study of various functional domains of tau and the study of tau expression in normal and pathological states. |
