The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
The purification of tau protein and the occurrence of two phosphorylation states of tau in brain.
Open accessAbstract
Two newly discovered properties of tau protein are reported; it is soluble in 2.5% perchloric acid and insoluble in 25% glycerol. These properties were exploited in the development of improved methods for the purification of tau. Treatment with perchloric acid did not alter the electrophoretic behavior of tau, and the products of the new isolation method were fully competent in the promotion of microtubule assembly. The application of the new purification techniques to bovine brain tissue demonstrated that tau exists endogenously in the dephosphorylated as well as in a phosphorylated state.
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Cites
Cleveland, D. W., Hwo, S.-Y., & Kirschner, M. W. (1977) · Journal of Molecular Biology · doi:10.1016/0022-2836(77)90213-3 · Cited by 915
Phosphorylation affects the ability of tau protein to promote microtubule assembly.
Lindwall, G., & Cole, R. D. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)42989-9 · Cited by 901
Self-citationPhosphorylation of microtubule-associated proteins regulates their interaction with actin filaments.
Selden, S. C., & Pollard, T. D. (1983) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)32333-0 · Cited by 314
Cited by
Goedert, M., & Jakes, R. (1990) · The EMBO Journal · doi:10.1002/j.1460-2075.1990.tb07870.x · Cited by 929
Arendt, T., Stieler, J. T., & Holzer, M. (2016) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2016.08.018 · Cited by 609
Hydrofluoric acid-treated tau PHF proteins display the same biochemical properties as normal tau.
Greenberg, S. G., Davies, P., Schein, J. D., & Binder, L. I. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)48531-6 · Cited by 543
Nuclear Tau, a Key Player in Neuronal DNA Protection
Sultan, A., Nesslany, F., Violet, M., Bégard, S., Loyens, A., Talahari, S., Mansuroglu, Z., Marzin, D., Sergeant, N., Humez, S., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.199976 · Cited by 421
Analysis of microtubule-associated protein tau glycation in paired helical filaments.
Ledesma, M. D., Bonay, P., Colaço, C., & Avila, J. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31849-5 · Cited by 333
Metadata
- Authors
- Lindwall, G., & Cole, R. D.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1984-10
- Volume
- 259
- Issue
- 19
- Pages
- 12241-12245
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1587065131
- Cited by
- 191
- References
- 3
- FWCI
- 6.51
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Lindwall, G., & Cole, R. D. (1984). The purification of tau protein and the occurrence of two phosphorylation states of tau in brain. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(20)71345-1
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