チームリーダー
石井 佳誉 Ph.D.

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