R
Ross Jakes
Researcher at Laboratory of Molecular Biology
Publications - 83
Citations - 27439
Ross Jakes is an academic researcher from Laboratory of Molecular Biology. The author has contributed to research in topics: Tau protein & Alpha-synuclein. The author has an hindex of 59, co-authored 83 publications receiving 25326 citations. Previous affiliations of Ross Jakes include University of Texas Southwestern Medical Center & Medical Research Council.
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Journal ArticleDOI
Alpha-synuclein in Lewy bodies.
Maria Grazia Spillantini,Marie L. Schmidt,Virginia M.-Y. Lee,John Q. Trojanowski,Ross Jakes,Michel Goedert +5 more
TL;DR: 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.
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Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease
TL;DR: Antisera raised against synthetic peptides corresponding to these different human tau isoforms demonstrate that multiple tau protein isoforms are incorporated into the neurofibrillary tangles of Alzheimer's disease.
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Identification of two distinct synucleins from human brain
TL;DR: Two abundant proteins of 140 and 134 amino acids were purified and sequenced from human brain and identified through their reactivity on immunoblots with a partially characterised monoclonal antibody that recognises tau protein in a phosphorylation‐dependent manner, defining a family of human brain synucleins.
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Assembly of microtubule-associated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycans
Michel Goedert,Ross Jakes,Maria Grazia Spillantini,Maria Grazia Spillantini,Masato Hasegawa,Michael J. Smith,R.A. Crowther +6 more
TL;DR: 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.
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Isolation of a fragment of tau derived from the core of the paired helical filament of Alzheimer disease
Claude Michel Wischik,Michal Novak,H C Thøgersen,Patricia C. Edwards,Michael J. Runswick,Ross Jakes,John E. Walker,Cesar Milstein,M Roth,Aaron Klug +9 more
TL;DR: A substantially enriched preparation of Alzheimer paired helical filaments has been used as a starting point for biochemical studies and sequence analysis of these peptides was used to design oligonucleotide probes for cloning a cognate cDNA, which leads to its identification as human microtubule-associated tau protein.