Download Molecular biology of Alzheimer's disease : genes and by Christian Haass PDF

By Christian Haass

Highlighting the newest and the main well timed features of Alzheimer's sickness study, this article is going to permit scientists in comparable examine fields, in addition to physicians operating with Alzheimer's sickness sufferers, to acquire a brief and whole review of the present state-of-the-art in a single of the main fascinating fields in neuroscience study. major scientists have contributed articles targeting key advancements during this box. This comprises an summary concerning the pathology, the genetics of familial Alzheimer's illness, proteolytic iteration and aggregation of amyloid -peptide, presenilins, threat components akin to ApoE, and transgenic animal types. the various newest advancements in Alzheimer's sickness learn, together with the influence of presenilin knock outs on amyloid -peptide new release, also are incorporated.

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Additional info for Molecular biology of Alzheimer's disease : genes and mechanisms involved in amyloid generation

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1989) The microtubule binding domain of tau protein. Neuron, 2, 1615–1624. , and Lee, G. (1994) Identification of tau protein regions required for process formation in PC12 cells. J. , 107, 3403–3412. , and Brandt, R. (1997) Conversion of serine to aspartate imitates phosphorylation-induced changes in the structure and function of microtubule-associated protein tau. J. , 272, 8441–8446. V. (1992) Phosphorylation by cAMP-dependent protein kinase inhibits the degradation of tau by calpain. J. , 267, 1563–1568.

An AD-like phosphorylation may cause a relocalization of tau from the axon to the cell body thus contributing to a loss of tau from axonal microtubules and increasing tau accumulation in the cell body. TAU’S ROLE IN AD PATHOLOGY Cell-free Models The development of models for tau pathology has focused on two aspects: on the reproduction of the formation of fibrillar tau aggregates similar to PHFs, and on the identification of pathogenic mechanisms which influence tau pathology. Recently, tau aggregates which morphologically closely resemble PHFs have been produced in cell free assembly reactions.

1993) Phosphorylation of Ser262 strongly reduces binding of tau to microtubules: distinction between PHF-like immunoreactivity and microtubule binding. Neuron, 11, 153–163. I. (1985) The distribution of tau in the mammalian central nervous system. J. Cell Biol, 101, 1371–1378. , and Fischer, I. (1996) Tau is enriched on dynamic microtubules in the distal region of growing axons. J. , 16, 3601–3619. , and Roth, M. (1994) Immunohistochemical staging of neurofibrillary degeneration in Alzheimer’s disease.

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