Assembly of Alzheimer-like filaments from full-length tau protein

R. A. Crowther; O. F. Olesen; M. J. Smith; R. Jakes; M. Goedert

doi:10.1016/0014-5793(94)80260-2

Assembly of Alzheimer-like filaments from full-length tau protein

R. A. Crowther, O. F. Olesen, M. J. Smith, R. Jakes, M. Goedert

Afdeling for Global Sundhed

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › peer review

158 Citationer (Scopus)

Abstract

The principal fibrous component of neurofibrillary pathology in Alzheimer's disease, the paired helical filament, is formed from hyperphosphorylated microtubule-associated protein tau. Here we show that recombinant tau protein either in a non-phosphorylated state or following phosphorylation with brain extract can be assembled in vitro into filaments resembling those seen in Alzheimer's disease. © 1994.

Originalsprog	Engelsk
Tidsskrift	FEBS Letters
Vol/bind	337
Udgave nummer	2
Sider (fra-til)	135-138
Antal sider	4
ISSN	0014-5793
DOI	https://doi.org/10.1016/0014-5793(94)80260-2
Status	Udgivet - 10 jan. 1994

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10.1016/0014-5793(94)80260-2

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Citationsformater

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abstract = "The principal fibrous component of neurofibrillary pathology in Alzheimer's disease, the paired helical filament, is formed from hyperphosphorylated microtubule-associated protein tau. Here we show that recombinant tau protein either in a non-phosphorylated state or following phosphorylation with brain extract can be assembled in vitro into filaments resembling those seen in Alzheimer's disease. {\textcopyright} 1994.",

keywords = "Alzheimer's disease, Hyper-phosphorylation, Microtubule-associated protein tau, Paired helical filament",

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AU - Crowther, R. A.

AU - Olesen, O. F.

AU - Smith, M. J.

AU - Jakes, R.

AU - Goedert, M.

PY - 1994/1/10

Y1 - 1994/1/10

N2 - The principal fibrous component of neurofibrillary pathology in Alzheimer's disease, the paired helical filament, is formed from hyperphosphorylated microtubule-associated protein tau. Here we show that recombinant tau protein either in a non-phosphorylated state or following phosphorylation with brain extract can be assembled in vitro into filaments resembling those seen in Alzheimer's disease. © 1994.

AB - The principal fibrous component of neurofibrillary pathology in Alzheimer's disease, the paired helical filament, is formed from hyperphosphorylated microtubule-associated protein tau. Here we show that recombinant tau protein either in a non-phosphorylated state or following phosphorylation with brain extract can be assembled in vitro into filaments resembling those seen in Alzheimer's disease. © 1994.

KW - Alzheimer's disease

KW - Hyper-phosphorylation

KW - Microtubule-associated protein tau

KW - Paired helical filament

UR - https://www.mendeley.com/catalogue/e4805391-b9c4-3708-9029-3966b168742e/

U2 - 10.1016/0014-5793(94)80260-2

DO - 10.1016/0014-5793(94)80260-2

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SN - 0014-5793

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JO - FEBS Letters

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