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of 41
pro vyhledávání: '"Gail V.W. Johnson"'
Publikováno v:
Biology, Vol 10, Iss 1047, p 1047 (2021)
Biology
Biology
Simple Summary The spatial progression of most Alzheimer’s Disease (AD) cases follows a well-defined route through the brain, yet research on the disease has yet to determine why this specific pattern of disease progression occurs. Recent developme
Publikováno v:
Brain Research. 1234:206-212
It has been previously reported that an Asp421 cleaved form of tau is toxic when expressed in cells. The purpose of this study was to understand if, and in what manner, the presence of Asp421 cleaved tau in neurons, which is generated by caspase clea
Autor:
Gail V.W. Johnson, Jianwen Zhang
Publikováno v:
Journal of Neurochemistry. 75:2346-2357
Alterations in the status of microtubules contribute to the cytoskeletal rearrangements that occur during apoptosis. The microtubule-associated protein tau regulates microtubule dynamics and thus is likely to play an important role in the cytoskeleta
Autor:
Kaihong Mi, Gail V.W. Johnson
Publikováno v:
Current Alzheimer Research. 3:449-463
The microtubule-associated protein tau, which is abundantly expressed in neurons, is deposited in cells in an abnormally phosphorylated state as fibrillar lesions in numerous neurodegenerative diseases, with the most notable being Alzheimer's disease
Autor:
Gail V.W. Johnson, Tori A. Matthews
Publikováno v:
Neuroscience Letters. 384:211-216
Tau is a neuronal microtubule-associated protein whose function is regulated by site-specific phosphorylation. One protein kinase that is likely to play an important role in regulating the phosphorylation state of tau in vivo is glycogen synthase kin
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease. 1739(2-3):280-297
The microtubule-associated protein tau, abundant in neurons, has gained notoriety due to the fact that it is deposited in cells as fibrillar lesions in numerous neurodegenerative diseases, and most notably Alzheimer's disease. Regulation of microtubu
Autor:
Jae-Hyeon Cho, Gail V.W. Johnson
Publikováno v:
Journal of Neurochemistry. 88:349-358
Site-specific phosphorylation of tau negatively regulates its ability to bind and stabilize microtubule structure. Although tau is a substrate of glycogen synthase kinase 3beta (GSK3beta), the exact sites on tau that are phosphorylated by this kinase
Autor:
Gail V.W. Johnson, Jae-Hyeon Cho
Publikováno v:
Journal of Biological Chemistry. 278:187-193
Glycogen synthase kinase 3β (GSK3β) phosphorylates substrates, including the microtubule-associated protein tau, at both primed and unprimed epitopes. GSK3β phosphorylation of tau negatively regulates tau-microtubule interactions; however the diff
Publikováno v:
Journal of Neurochemistry. 64:1209-1215
tau is a major component of paired helical filaments found in the neurofibrillary tangles of Alzheimer's diseased brain. However, the mechanism or mechanisms responsible for the association of tau to form these aggregates remains unknown. In this stu
Autor:
Teresa M. Cox, Jason P. Brown, Douglas Galasko, Ruth Motter, Gail V.W. Johnson, Peter Seubert
Publikováno v:
Journal of Neurochemistry. 68:430-433
Previous studies have shown that the levels of the microtubule-associated protein tau in the CSF of patients with Alzheimer's disease (AD) are elevated compared with age-matched controls. In spite of these findings, the nature of tau in CSF has not b