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Titolo:
NEW PHOSPHORYLATION SITES IDENTIFIED IN HYPERPHOSPHORYLATED TAU (PAIRED HELICAL FILAMENT-TAU) FROM ALZHEIMERS-DISEASE BRAIN USING NANOELECTROSPRAY MASS-SPECTROMETRY
Autore:
HANGER DP; BETTS JC; LOVINY TLF; BLACKSTOCK WP; ANDERTON BH;
Indirizzi:
INST PSYCHIAT,DEPT NEUROSCI,DE CRESPIGNY PK, DENMARK HILL LONDON SE5 8AF ENGLAND GLAXO WELLCOME RES & DEV LTD,BIOMOL STRUCT UNIT STEVENAGE SG1 2NY HERTS ENGLAND
Titolo Testata:
Journal of neurochemistry
fascicolo: 6, volume: 71, anno: 1998,
pagine: 2465 - 2476
SICI:
0022-3042(1998)71:6<2465:NPSIIH>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEIN KINASE-I; PROLINE-DIRECTED PHOSPHORYLATION; ABNORMAL PHOSPHORYLATION; FETAL-TAU; PHF-TAU; BIOCHEMICAL-PROPERTIES; MICROTUBULE-BINDING; RAT-BRAIN; SER(262); COMPONENT;
Keywords:
ALZHEIMERS DISEASE; PAIRED HELICAL FILAMENTS; TAU; PHOSPHORYLATION; MASS SPECTROMETRY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
69
Recensione:
Indirizzi per estratti:
Citazione:
D.P. Hanger et al., "NEW PHOSPHORYLATION SITES IDENTIFIED IN HYPERPHOSPHORYLATED TAU (PAIRED HELICAL FILAMENT-TAU) FROM ALZHEIMERS-DISEASE BRAIN USING NANOELECTROSPRAY MASS-SPECTROMETRY", Journal of neurochemistry, 71(6), 1998, pp. 2465-2476

Abstract

Paired helical filaments (PHFs) are the structural constituents of neurofibrillary tangles in Alzheimer's disease and are composed of hyperphosphorylated forms of the microtubule-associated protein tau (PHF-tau). Pathological hyperphosphorylation of tau is believed to be an important contributor to the destabilisation of microtubules and their subsequent disappearance from tangle-bearing neurons in Alzheimer's disease, making elucidation of the mechanisms that regulate tau phosphorylation an important research goal. Thus, it is essential to identify, preferably by direct sequencing, all of the sites in PHF-tau that are phosphorylated, a task that is incomplete because of the difficulty to date of purifying insoluble PHF-tau to homogeneity and in sufficient quantities for structural analysis, Here we describe the solubilisation of PHF-tau followed by its purification by Mono Q chromatography and reversed-phase HPLC, Phosphopeptides from proteolytically digested PHF-tau were sequenced by nanoelectrospray mass spectrometry. We identified 22 phosphorylation sites in PHF-tau, including five sites not previously identified. The combination of our new data with previous reportsshows that PHF-tau can be phosphorylated on at least 25 different sites.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 19/09/20 alle ore 09:17:40