チームリーダー
石井佳誉 Ph.D.

先端NMR開発・応用研究チーム

[2025年3月終了]

E-mail yoshitaka.ishii@riken.jp

概要
主要論文
メンバー
ニュース

当チームは理研横浜事業所において世界最高水準のNMR研究拠点を整備・発展してきました。この拠点をベースに世界を先導するNMRの方法論の開発や先端応用研究をおこないます。従来の手法では解析が困難なアミロイドタンパク質やRNA、ナノ生体材料等の生体分子の構造と分子レベルでの機能の解明を目指し、技術開発に取り組みます。更に、JSTのプロジェクト等で開発中の超高磁場NMR磁石に対応した新規NMR法の開発をおこない、従来の限界を超越したNMR技術基盤を確⽴するとともに、新研究領域や複合測定法を積極的に開拓します。

研究テーマ

構造生物化学
先端ナノ材料・高分子
アルツハイマー病等の分子機構

主要論文

Ohyama T, Osawa T, Sekine SI, Ishii Y.
NMR Studies of Genomic RNA in 3' Untranslated Region Unveil Pseudoknot Structure that Initiates Viral RNA Replication in SARS-CoV-2.
JACS Au 4(4), 1323-1333 (2024) doi: 10.1021/jacsau.3c00641

Sakuma K, Kobayashi N, Sugiki T, et al.
Design of complicated all-α protein structures.
Nature Structural & Molecular Biology 31(2), 275-282 (2024) doi: 10.1038/s41594-023-01147-9

Tritrakarn T, Yamamoto K, Takahashi M, Okamura T.
New unifying metric for NMR/MRI probe evaluation based on optimized solenoid coil geometry.
Journal of Magnetic Resonance 358, 107602 (2024) doi: 10.1016/j.jmr.2023.107602

Takatsu K, Kobayashi N, Wu N, et al.
Biophysical analysis of Gaussia luciferase bioluminescence mechanisms using a non-oxidizable coelenterazine.
BBA Advances 3, 100068 (2023) doi: 10.1016/j.bbadva.2022.100068

Minami S, Kobayashi N, Sugiki T, et al.
Exploration of novel αβ-protein folds through de novo design.
Nature Structural & Molecular Biology 30(8), 1132-1140 (2023) doi: 10.1038/s41594-023-01029-0

Kashihara K, Oouchi M, Kodama Y, et al.
High-Field Nuclear Magnetic Resonance Studies Reveal New Structural Landscape of Sulfur-Vulcanized Natural Rubber.
Biomacromolecules 23(11), 4481-4492 (2022) doi: 10.1021/acs.biomac.2c00141

Matsunaga T, Okabe R, Ishii Y.
Efficient solvent suppression with adiabatic inversion for ¹H-detected solid-state NMR.
Journal of Biomolecular NMR (2021) doi: 10.1007/s10858-021-00384-8

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 143(30), 11462-11472 (2021) doi: 10.1021/jacs.1c03346

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) doi: 10.1016/j.jmr.2020.106857

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(49), 31149-31156 (2020) doi: 10.1073/pnas.2002120117

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(16), 9346-9360 (2020) doi: 10.1093/nar/gkaa598

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.
the Journal of Biological Chemistry 295(2), 458-467 (2020) doi: 10.1074/jbc.RA119.008522

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(3), 1394-1400 (2019) doi: 10.1021/acs.biomac.8b01771

Shi X, Prasanna C, Nagashima T, et al.
Structure and Dynamics in the Nucleosome Revealed by Solid-State NMR.
Angewandte Chemie 57(31), 9734-9738 (2018) doi: 10.1002/anie.201804707

Yoo BK, 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(8), 2781-2784 (2018) doi: 10.1021/jacs.7b13660

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(6), 499-505 (2015) doi: 10.1038/nsmb.2991

Parthasarathy S, Inoue M, Xiao Y, et al.
Structural Insight into an Alzheimer's Brain-Derived Spherical Assembly of Amyloid β by Solid-State NMR.
Journal of the American Chemical Society 137(20), 6480-3 (2015) doi: 10.1021/jacs.5b03373

Wickramasinghe NP, Parthasarathy S, Jones CR, et al.
Nanomole-scale protein solid-state NMR by breaking intrinsic ¹HT₁ boundaries.
Nature Methods 6(3), 215-8 (2009) doi: 10.1038/nmeth.1300