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Items: 1 to 20 of 267

1.

Alzheimer disease-specific conformation of hyperphosphorylated paired helical filament-Tau is polyubiquitinated through Lys-48, Lys-11, and Lys-6 ubiquitin conjugation.

Cripps D, Thomas SN, Jeng Y, Yang F, Davies P, Yang AJ.

J Biol Chem. 2006 Apr 21;281(16):10825-38. Epub 2006 Jan 27.

2.

Posttranslational modifications of tau in paired helical filaments.

Morishima M, Ihara Y.

Dementia. 1994 Sep-Oct;5(5):282-8. Review.

PMID:
7951685
3.

Mechanisms of neurofibrillary degeneration and the formation of neurofibrillary tangles.

Iqbal K, Alonso AC, Gong CX, Khatoon S, Pei JJ, Wang JZ, Grundke-Iqbal I.

J Neural Transm Suppl. 1998;53:169-80. Review.

PMID:
9700655
4.

Unique Alzheimer's disease paired helical filament specific epitopes involve double phosphorylation at specific sites.

Hoffmann R, Lee VM, Leight S, Varga I, Otvos L Jr.

Biochemistry. 1997 Jul 1;36(26):8114-24.

PMID:
9201960
5.
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7.

Dual modification of Alzheimer's disease PHF-tau protein by lysine methylation and ubiquitylation: a mass spectrometry approach.

Thomas SN, Funk KE, Wan Y, Liao Z, Davies P, Kuret J, Yang AJ.

Acta Neuropathol. 2012 Jan;123(1):105-17. doi: 10.1007/s00401-011-0893-0. Epub 2011 Oct 28.

8.

Proteasome inhibition by paired helical filament-tau in brains of patients with Alzheimer's disease.

Keck S, Nitsch R, Grune T, Ullrich O.

J Neurochem. 2003 Apr;85(1):115-22.

9.

Analysis of microtubule-associated protein tau glycation in paired helical filaments.

Ledesma MD, Bonay P, Colaço C, Avila J.

J Biol Chem. 1994 Aug 26;269(34):21614-9.

10.

Aluminum modifies the properties of Alzheimer's disease PHF tau proteins in vivo and in vitro.

Shin RW, Lee VM, Trojanowski JQ.

J Neurosci. 1994 Nov;14(11 Pt 2):7221-33.

11.

Conformational change as one of the earliest alterations of tau in Alzheimer's disease.

Weaver CL, Espinoza M, Kress Y, Davies P.

Neurobiol Aging. 2000 Sep-Oct;21(5):719-27.

PMID:
11016541
12.

Ubiquitination and abnormal phosphorylation of paired helical filaments in Alzheimer's disease.

Iqbal K, Grundke-Iqbal I.

Mol Neurobiol. 1991;5(2-4):399-410. Review.

PMID:
1726645
14.

A conformation- and phosphorylation-dependent antibody recognizing the paired helical filaments of Alzheimer's disease.

Jicha GA, Lane E, Vincent I, Otvos L Jr, Hoffmann R, Davies P.

J Neurochem. 1997 Nov;69(5):2087-95.

15.

Phosphorylation that detaches tau protein from microtubules (Ser262, Ser214) also protects it against aggregation into Alzheimer paired helical filaments.

Schneider A, Biernat J, von Bergen M, Mandelkow E, Mandelkow EM.

Biochemistry. 1999 Mar 23;38(12):3549-58.

PMID:
10090741
17.

Locations and immunoreactivities of phosphorylation sites on bovine and porcine tau proteins and a PHF-tau fragment.

Poulter L, Barratt D, Scott CW, Caputo CB.

J Biol Chem. 1993 May 5;268(13):9636-44.

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Tyrosine 394 is phosphorylated in Alzheimer's paired helical filament tau and in fetal tau with c-Abl as the candidate tyrosine kinase.

Derkinderen P, Scales TM, Hanger DP, Leung KY, Byers HL, Ward MA, Lenz C, Price C, Bird IN, Perera T, Kellie S, Williamson R, Noble W, Van Etten RA, Leroy K, Brion JP, Reynolds CH, Anderton BH.

J Neurosci. 2005 Jul 13;25(28):6584-93.

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