K
Kiyotoshi Kaneko
Researcher at University of California, San Francisco
Publications - 18
Citations - 2532
Kiyotoshi Kaneko is an academic researcher from University of California, San Francisco. The author has contributed to research in topics: Scrapie & PrPSc Proteins. The author has an hindex of 16, co-authored 18 publications receiving 2488 citations.
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Journal ArticleDOI
Evidence for protein X binding to a discontinuous epitope on the cellular prion protein during scrapie prion propagation
Kiyotoshi Kaneko,Laurence Zulianello,Michael J. Scott,Carol M. Cooper,Wallace Andrew,Thomas L. James,Fred E. Cohen,Stanley B. Prusiner +7 more
TL;DR: The identification of the site at which protein X binds to the cellular isoform of PrP (PrPC) using scrapie-infected mouse (Mo) neuroblastoma cells transfected with chimeric Hu/MoPrP genes even though protein X has not yet been isolated is reported.
Journal ArticleDOI
Solution structure of a 142-residue recombinant prion protein corresponding to the infectious fragment of the scrapie isoform.
Thomas L. James,He Liu,Nikolai B. Ulyanov,Shauna Farr-Jones,Hong Zhang,David G. Donne,Kiyotoshi Kaneko,Darlene Groth,Ingrid Mehlhorn,Stanley B. Prusiner,Fred E. Cohen +10 more
TL;DR: The scrapie prion protein (PrPSc) is the major, and possibly the only, component of the infectious prion; it is generated from the cellular isoform (PrPC) by a conformational change and appears to modulate susceptibility of sheep and humans to prion disease.
Journal ArticleDOI
COOH-terminal sequence of the cellular prion protein directs subcellular trafficking and controls conversion into the scrapie isoform
Kiyotoshi Kaneko,Martin Vey,Michael J. Scott,Susanne Pilkuhn,Frederick Cohen,Stanley B. Prusiner +5 more
TL;DR: It is argued that PrP(Sc) formation is restricted to a specific subcellular compartment and as such, it is likely to involve auxiliary macromolecules found within CLDs.
Journal ArticleDOI
Conformational transitions in peptides containing two putative alpha-helices of the prion protein.
Hong Zhang,Kiyotoshi Kaneko,Jack T. Nguyen,Tatiana L. Livshits,Michael A. Baldwin,Fred E. Cohen,Thomas L. James,Stanley B. Prusiner +7 more
TL;DR: It is suggested that perturbation of the packing environment of the highly conserved residues is a possible mechanism for triggering the conversion of PrPcto PrPsc where α-helices appear to be converted into β-sheets.
Journal ArticleDOI
Mimicking dominant negative inhibition of prion replication through structure-based drug design
Véronique Perrier,Wallace Andrew,Kiyotoshi Kaneko,Jiri G. Safar,Stanley B. Prusiner,Fred E. Cohen +5 more
TL;DR: Mimicking dominant negative inhibition in the design of drugs that inhibit prion replication may provide a more general approach to developing therapeutics for deleterious protein-protein interactions.