Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease

TL;DR: In this paper, the authors sequenced tau in FTDP-17 families and identified three missense mutations (G272V, P301L and R406W) and three mutations in the 5' splice site of exon in

TL;DR: It is shown thatLewy bodies and Lewy neurites from Parkinson’s disease and dementia with Lewy bodies are stained strongly by antibodies directed against amino- terminal and carboxyl-terminal sequences of α-synuclein, showing the presence of full- length or close to full-length α- synuclein.

TL;DR: The ongoing molecular dissection of the neurodegenerative pathways is expected to lead to a true understanding of disease pathogenesis.

TL;DR: Tau proteins are the major constituents of intraneuronal and glial fibrillar lesions described in Alzheimer's disease and numerous neurodegenerative disorders referred as 'tauopathies' as discussed by the authors.

TL;DR: The abnormal filaments of neurofibrillary tangles of Alzheimer's disease have been studied by immunocytochemistry with a serum raised against the isolated filaments, and with an antisera containing anti-tau, a microtubule-associated protein.

TL;DR: Although TauR is unable to promote polymerization, it can modify Tau-(187-204)-induced tubulin assembly, and two other peptides tested, TauR and Tau-(250-267), were not able to promote the assembly of tubulin over a range of concentrations up to 800 microM.

TL;DR: This material is additionally characterized by the presence of clusters of new dendrite growth, developing at one or more sites along the dendritic or somal surface, which are provisionally referred to as “lawless.”

TL;DR: It is determined that embryonic tau protein is translated from a 6-kb mRNA that persists throughout brain development, and the different forms appear to result from changes in tau mRNA since in vitro translation products reflect the qualitative and quantitative changes found in vivo.