Share This Author
Alpha-synuclein in Lewy bodies.
α-Synuclein in Lewy bodies
- M. Spillantini, M. L. Schmidt, V. Lee, J. Trojanowski, R. Jakes, M. Goedert
- 28 August 1997
Strong staining of Lewy bodies from idiopathic Parkinson's disease with antibodies for α-synuclein, a presynaptic protein of unknown function which is mutated in some familial cases of the disease, indicates that the LewY bodies from these two diseases may have identical compositions.
α-Synuclein in filamentous inclusions of Lewy bodies from Parkinson’s disease and dementia with Lewy bodies
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.
Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease
alpha-Synuclein in filamentous inclusions of Lewy bodies from Parkinson's disease and dementia with lewy bodies.
- M. Spillantini, R. Crowther, R. Jakes, M. Hasegawa, M. Goedert
- BiologyProceedings of the National Academy of Sciences…
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 alpha-synuclein, showing the presence of full- length or close to full-length alpha- synuclein.
Identification of two distinct synucleins from human brain
Expression of separate isoforms of human tau protein: correlation with the tau pattern in brain and effects on tubulin polymerization.
The recombinant tau isoforms were biologically active at micromolar concentrations, as assessed by their ability to promote microtubule assembly and the rates of assembly were 2.5–3.0 times faster for isoforms containing four repeats when compared with three‐repeat containing isoforms, with no significant contribution by the amino‐terminal insertions.
Abundant Tau Filaments and Nonapoptotic Neurodegeneration in Transgenic Mice Expressing Human P301S Tau Protein
The production and characterization of a line of mice transgenic for the 383 aa isoform of human tau with the P301S mutation is reported on, with evidence for apoptosis obtained, despite the extensive colocalization of hyperphosphorylated tau protein with activated MAP kinase family members.
Assembly of microtubule-associated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycans
- M. Goedert, R. Jakes, M. Spillantini, M. Hasegawa, M. J. Smith, R. Crowther
- Biology, ChemistryNature
- 10 October 1996
It is shown that non-phosphorylated recombinant tau iso-forms with three microtubule-binding repeats form paired helical-like filaments under physiological conditions in vitro, when incubated with sulphated glycosaminoglycans such as heparin or heparan sulphate.
Filamentous alpha-synuclein inclusions link multiple system atrophy with Parkinson's disease and dementia with Lewy bodies.
- M. Spillantini, R. Crowther, R. Jakes, N. Cairns, P. Lantos, M. Goedert
- BiologyNeuroscience letters
These findings provide an unexpected link between multiple system atrophy and Lewy body disorders and establish that alpha-synucleinopathies constitute a major class of human neurodegenerative disorder.