Team Leader
Yoshitaka Ishii
Ph.D.
Laboratory for Advanced NMR Application and Development
[Closed Mar. 2025]
E-mailyoshitaka.ishii@riken.jp
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.
Research Theme
- Structural Biochemistry
- Advanced nano-materials/ Polymer
- Molecular mechanisms of Alzheimer's and other diseases
Selected Publications
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
Members
Naohiro Kobayashi
Senior Research Scientist
Masato Takahashi
Senior Research Scientist
Takako Ohyama
Research Scientist
Ayesha Wijalath Pelige
Research Scientist
Kyoko Seimiya
Technical Staff I
