Phosphorylation sites on tau identified by nanoelectrospray mass spectrometry: Differences in vitro between the mitogen-activated protein kinases ERK2, c-Jun N-terminal kinase and P38, and glycogen synthase kinase- 3β

Journal of Neurochemistry

Volumn 74, Issue 4, 2000, Pages 1587-1595

  Reynolds, C Hugh ^a   Betts, Joanna C ^b   Blackstock, Walter P ^b   Nebreda, Angel R ^c   Anderton, Brian H ^a  

^a KING'S COLLEGE LONDON   (United Kingdom)

^b GLAXOSMITHKLINE   (United Kingdom)

^c EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

Author keywords

Alzheimer's disease; Nonproline sites; Paired helical filaments.; Proline directed sites

Indexed keywords

GLYCOGEN SYNTHASE KINASE 3BETA; MITOGEN ACTIVATED PROTEIN KINASE; PHOSPHATASE; PHOSPHATE; PROLINE; SERINE; STRESS ACTIVATED PROTEIN KINASE; TAU PROTEIN; THREONINE;

ALZHEIMER DISEASE; ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME PHOSPHORYLATION; IN VIVO STUDY; MASS SPECTROMETRY; PHOSPHATE METABOLISM; PRIORITY JOURNAL; PROTEIN PHOSPHORYLATION;

ALZHEIMER DISEASE; AMINO ACID SEQUENCE; ANIMALS; ANTICOAGULANTS; BINDING SITES; CA(2+)-CALMODULIN DEPENDENT PROTEIN KINASE; CELLS, CULTURED; GLYCOGEN SYNTHASE KINASE 3; GLYCOGEN SYNTHASE KINASES; HEPARIN; INSECTS; JNK MITOGEN-ACTIVATED PROTEIN KINASES; MASS SPECTROMETRY; MITOGEN-ACTIVATED PROTEIN KINASE 1; MITOGEN-ACTIVATED PROTEIN KINASES; MOLECULAR SEQUENCE DATA; NEUROFIBRILLARY TANGLES; P38 MITOGEN-ACTIVATED PROTEIN KINASES; PHOSPHORYLATION; PROLINE; SIGNAL TRANSDUCTION; TAU PROTEINS;

EID: 0034067992     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.2000.0741587.x     Document Type: Article

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