Literature DB >> 8269082

The molecular and cellular biology of tau.

K S Kosik1.   

Abstract

Tau protein was a well-studied molecule before it was discovered in the Alzheimer neurofibrillary tangles. As a microtubule-associated protein (MAP), it continues to be of interest to microtubule biologists who have provided a rather rich knowledge about this protein. Recent work suggests that tau, a neuronal MAP, is capable of generating some features of an axonal shape and an axon-like organization of the cytoskeleton. The importance of tau in pathology stems from its relationship to Alzheimer paired helical filaments and dystrophic neurites. Tau was first believed to be a component of paired helical filaments based upon immunocytochemical grounds (1-6) and then conclusively demonstrated by protein chemical techniques (7-9). Most recently it was shown that bacterially expressed tau fragments from the microtubule-binding domain can self-assemble into paired helical filaments that resemble those from the Alzheimer brain (10).

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Year:  1993        PMID: 8269082     DOI: 10.1111/j.1750-3639.1993.tb00724.x

Source DB:  PubMed          Journal:  Brain Pathol        ISSN: 1015-6305            Impact factor:   6.508


  24 in total

1.  Mechanisms of cell death in cholinergic basal forebrain neurons in chronic alcoholics.

Authors:  K M Cullen; G M Halliday
Journal:  Metab Brain Dis       Date:  1995-03       Impact factor: 3.584

2.  PhIP exposure in rodents produces neuropathology potentially relevant to Alzheimer's disease.

Authors:  Tauqeerunnisa Syeda; Rachel M Foguth; Emily Llewellyn; Jason R Cannon
Journal:  Toxicology       Date:  2020-03-10       Impact factor: 4.221

Review 3.  Probing modifications of the neuronal cytoskeleton.

Authors:  L C Doering
Journal:  Mol Neurobiol       Date:  1993 Fall-Winter       Impact factor: 5.590

4.  Widespread distribution of tau in the astrocytic elements of glial tumors.

Authors:  M Miyazono; T Iwaki; T Kitamoto; R W Shin; M Fukui; J Tateishi
Journal:  Acta Neuropathol       Date:  1993       Impact factor: 17.088

5.  Generalised nuclear and cytoplasmic inclusion disease: a rare case investigated by microscopy and immunohistochemistry.

Authors:  A Ruszkiewicz; K Opeskin; R M Anderson; C W Chow
Journal:  Acta Neuropathol       Date:  1994       Impact factor: 17.088

6.  Twisted tubulofilaments of inclusion body myositis muscle resemble paired helical filaments of Alzheimer brain and contain hyperphosphorylated tau.

Authors:  V Askanas; W K Engel; M Bilak; R B Alvarez; D J Selkoe
Journal:  Am J Pathol       Date:  1994-01       Impact factor: 4.307

7.  Effect of Phosphorylation and O-GlcNAcylation on Proline-Rich Domains of Tau.

Authors:  Lata Rani; Jeetain Mittal; Sairam S Mallajosyula
Journal:  J Phys Chem B       Date:  2020-03-02       Impact factor: 2.991

8.  Ganglioglioma with neurofibrillary tangles (NFTs): neoplastic NFTs share antigenic determinants with NFTs of Alzheimer's disease.

Authors:  D Soffer; F Umansky; J E Goldman
Journal:  Acta Neuropathol       Date:  1995       Impact factor: 17.088

9.  Alzheimer and beta-amyloid-treated fibroblasts demonstrate a decrease in a memory-associated GTP-binding protein, Cp20.

Authors:  C S Kim; Y F Han; R Etcheberrigaray; T J Nelson; J L Olds; T Yoshioka; D L Alkon
Journal:  Proc Natl Acad Sci U S A       Date:  1995-03-28       Impact factor: 11.205

Review 10.  Pathophysiological Function of ADAMTS Enzymes on Molecular Mechanism of Alzheimer's Disease.

Authors:  Murat Serdar Gurses; Mustafa Numan Ural; Mehmet Akif Gulec; Omer Akyol; Sumeyya Akyol
Journal:  Aging Dis       Date:  2016-01-11       Impact factor: 6.745

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