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The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.

The Primary Structure and Heterogeneity of Tau Protein from Mouse Brain

Lee, Gloria, Cowan, Nicholas, Kirschner, Marc·1988·Science

Abstract

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 α-helical or β-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.

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Research works printed but not linked: 29

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Cited by

Metadata

Authors
Lee, G., Cowan, N., & Kirschner, M.
Venue
Science
Published
1988-01-15
Volume
239
Issue
4837
Pages
285-288
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2026771024
Cited by
678
References
3
FWCI
39.44
Type
journal article
Language
en
Open access
closed

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