Laboratory for Advanced NMR Application and Development
- Location：Yokohama / West NMR Bldg. N108
- E-mail：yoshitaka.ishii[at]riken.jpPlease replace [at] with @.
Based at the internationally renowned NMR research center at the RIKEN Yokohama Campus, we develop world-leading high-field NMR methodologies and conduct advanced application research. In particular, we will work on development of NMR methods to elucidate the structures and functions of biomolecules such as amyloid proteins, RNA, and nano-biomaterials, which are difficult to analyze using conventional structural biology methods. We also develop advanced NMR methods suited for ultra-high-field NMR magnets that are under development at RIKEN as part of a JST-MIRAI project. It is also within our scope to explore novel NMR applications and NMR analysis integrated with electron microscopy and other methods.
- Structural Biochemistry
- Polymer/Fiber material
- Applied Organic Chemistry
Main Publications List
- Wickramasinghe A, Xiao Y, Kobayashi N, et al.
Sensitivity-Enhanced Solid-state NMR Detection of Structural Differences and Unique Polymorphs in Pico- to Nanomolar Amounts of Brain-derived and Synthetic 42-residue Amyloid-β Fibrils.
Journal of the American Chemical Society (2021) doi: 10.1021/jacs.1c03346
- Ohyama T, Takahashi H, Sharma H, et al.
An NMR-based approach reveals the core structure of the functional domain of SINEUP lncRNAs.
Nucleic Acids Research 48, 9346-9360 (2020)
- Koga R, Yamamoto M, Kosugi T, et al.
Robust folding of a de novo designed ideal protein even with most of the core mutated to valine.
Proceedings of the National Academy of Sciences of the United States of America 117, 31149-31156 (2020)
- Matsunaga T, Matsuda I, Yamazaki T, Ishii Y.
Decoherence optimized tilted-angle cross polarization: A novel concept for sensitivity-enhanced solid-state NMR using ultra-fast magic angle spinning.
Journal of Magnetic Resonance 322, 106857 (2021)
- Xiao Y, Matsuda I, Inoue M, et al.
NMR-based site-resolved profiling of β-amyloid misfolding reveals structural transitions from pathologically relevant spherical oligomer to fibril.
Journal of Biological Chemistry 295, 458-467 (2020)
- Oouchi M, Ukawa J, Ishii Y, Maeda H.
Structural Analysis of the Terminal Groups in Commercial Hevea Natural Rubber by 2D-NMR with DOSY Filters and Multiple-WET Methods Using Ultrahigh-Field NMR.
Biomacromolecules 20, 1394-1400 (2019)
- Shi X, Prasanna C, Nagashima T, et al.
Structure and Dynamics in the Nucleosome Revealed by Solid-State NMR.
Angewandte Chemie International Edition 57, 9734-9738 (2018)
- Yoo B, Xiao Y, McElheny D, Ishii Y.
E22G pathogenic mutation of β-amyloid (Aβ) enhances misfolding of Aβ40 by unexpected prion-like cross talk between Aβ42 and Aβ40.
Journal of the American Chemical Society 140, 2781–2784 (2018)
- Xiao Y, Ma B, McElheny D, et al.
Aβ(1–42) fibril structure illuminates self-recognition and replication of amyloid in Alzheimer’s disease.
Nature Structural & Molecular Biology 22, 499-505 (2015)
- Parthasarathy S, Inoue M, Xiao Y, et al.
Structural Insight into an Alzheimer's Brain-Derived Spherical Assembly of Amyloid beta by Solid-State NMR.
Journal of the American Chemical Society 137, 6480-6483 (2015)
- Wickramasinghe NP, Parthasarathy S, Jones CR, et al.
Nanomole-scale protein solid-state NMR by breaking intrinsic H-1 T-1 boundaries.
Nature Methods 6, 215-218 (2009)
|Yoshitaka IshiiTeam Leader|
|Naohiro KobayashiSenior Scientist|
|Toshio NagashimaSenior Scientist|
|Takako OhyamaResearch Scientist|
|Tatsuya MatsunagaPostdoctoral Researcher|
|Kyoko SeimiyaTechnical Staff I|
|Miwa WakabayashiTechnical Staff I|
|Kayoko NagashimaExpert Technician|
*：concurrent / Please replace [at] with @.