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Yoshitaka Ishii
Researcher at Tokyo Institute of Technology
Publications - 64
Citations - 10395
Yoshitaka Ishii is an academic researcher from Tokyo Institute of Technology. The author has contributed to research in topics: Solid-state nuclear magnetic resonance & Magic angle spinning. The author has an hindex of 34, co-authored 63 publications receiving 9437 citations. Previous affiliations of Yoshitaka Ishii include University of Illinois at Chicago & National Institutes of Health.
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Journal ArticleDOI
A structural model for Alzheimer's β-amyloid fibrils based on experimental constraints from solid state NMR
Aneta T. Petkova,Yoshitaka Ishii,John J. Balbach,Oleg N. Antzutkin,Richard D. Leapman,Frank Delaglio,Robert Tycko +6 more
TL;DR: A structural model for amyloid fibrils formed by the 40-residue β-amyloid peptide associated with Alzheimer's disease (Aβ1–40) is presented, based on a set of experimental constraints from solid state NMR spectroscopy and incorporates the cross-β structural motif established by x-ray fiber diffraction.
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Expanded graphite as superior anode for sodium-ion batteries
Yang Wen,Kai He,Yujie Zhu,Fudong Han,Yunhua Xu,Isamu Matsuda,Yoshitaka Ishii,John Cumings,Chunsheng Wang +8 more
TL;DR: Expanded graphite is reported as a Na-ion battery anode, prepared through a process of oxidation and partial reduction on graphite, which has an enlarged interlayer lattice distance yet retains an analogous long-range-ordered layered structure to graphite.
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Synthesis and solid-state NMR structural characterization of 13C-labeled graphite oxide.
Weiwei Cai,Weiwei Cai,Richard D. Piner,Frank J. Stadermann,Sungjin Park,Medhat A. Shaibat,Yoshitaka Ishii,Dongxing Yang,Aruna Velamakanni,Sung Jin An,Meryl D. Stoller,Jinho An,Dongmin Chen,Rodney S. Ruoff +13 more
TL;DR: The detailed chemical structure of graphite oxide (GO), a layered material prepared from graphite almost 150 years ago and a precursor to chemically modified graphenes, has not been previously resolved because of the pseudo-random chemical functionalization of each layer, as well as variations in exact composition.
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Amyloid Fibril Formation by Aβ16-22, a Seven-Residue Fragment of the Alzheimer's β-Amyloid Peptide, and Structural Characterization by Solid State NMR†
John J. Balbach,Yoshitaka Ishii,Oleg N. Antzutkin,Richard D. Leapman,Nancy W. Rizzo,Fred Dyda,Jennifer L. Reed,Robert Tycko +7 more
TL;DR: One-dimensional and two-dimensional spectra of selectively and uniformly labeled samples exhibit 13C NMR line widths of <2 ppm, demonstrating that the peptide, including amino acid side chains, has a well-ordered conformation in the fibrils.
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Aβ(1–42) fibril structure illuminates self-recognition and replication of amyloid in Alzheimer's disease
Yiling Xiao,Buyong Ma,Dan McElheny,Sudhakar Parthasarathy,Fei Long,Minako Hoshi,Ruth Nussinov,Yoshitaka Ishii +7 more
TL;DR: The atomic model of an Aβ(1–42) amyloid fibril, from solid-state NMR (ssNMR) data, is presented, providing insight into the A β(1-42)-selective self-replicating amyloids-propagation machinery in early-stage Alzheimer's disease.