| NMR snapshots of a fluctuating protein structure: ubiquitin at 30 bar–3 kbar R Kitahara, S Yokoyama, K Akasaka Journal of molecular biology 347 (2), 277-285, 2005 | 192 | 2005 |
| Close identity of a pressure-stabilized intermediate with a kinetic intermediate in protein folding R Kitahara, K Akasaka Proceedings of the National Academy of Sciences 100 (6), 3167-3172, 2003 | 118 | 2003 |
| Aberrant assembly of RNA recognition motif 1 links to pathogenic conversion of TAR DNA-binding protein of 43 kDa (TDP-43) A Shodai, T Morimura, A Ido, T Uchida, T Ayaki, R Takahashi, S Kitazawa, ... Journal of Biological Chemistry 288 (21), 14886-14905, 2013 | 109 | 2013 |
| High-pressure NMR spectroscopy for characterizing folding intermediates and denatured states of proteins YO Kamatari, R Kitahara, H Yamada, S Yokoyama, K Akasaka Methods 34 (1), 133-143, 2004 | 107 | 2004 |
| High pressure NMR reveals that apomyoglobin is an equilibrium mixture from the native to the unfolded R Kitahara, H Yamada, K Akasaka, PE Wright Journal of molecular biology 320 (2), 311-319, 2002 | 99 | 2002 |
| High Pressure NMR Reveals Active-Site Hinge Motion of Folate-Bound Escherichia coli Dihydrofolate Reductase R Kitahara, S Sareth, H Yamada, E Ohmae, K Gekko, K Akasaka Biochemistry 39 (42), 12789-12795, 2000 | 98 | 2000 |
| Two folded conformers of ubiquitin revealed by high-pressure NMR R Kitahara, H Yamada, K Akasaka Biochemistry 40 (45), 13556-13563, 2001 | 78 | 2001 |
| Exploring the folding energy landscape with pressure K Akasaka, R Kitahara, YO Kamatari Archives of biochemistry and biophysics 531 (1-2), 110-115, 2013 | 77 | 2013 |
| Pressure-induced chemical shifts as probes for conformational fluctuations in proteins R Kitahara, K Hata, H Li, MP Williamson, K Akasaka Progress in Nuclear Magnetic Resonance Spectroscopy 71, 35-58, 2013 | 66 | 2013 |
| Equilibrium and pressure-jump relaxation studies of the conformational transitions of P13MTCP1 R Kitahara, C Royer, H Yamada, M Boyer, JL Saldana, K Akasaka, ... Journal of molecular biology 320 (3), 609-628, 2002 | 60 | 2002 |
| Cold denaturation of ubiquitin at high pressure R Kitahara, A Okuno, M Kato, Y Taniguchi, S Yokoyama, K Akasaka Magnetic Resonance in Chemistry 44 (S1), S108-S113, 2006 | 54 | 2006 |
| How internal cavities destabilize a protein M Xue, T Wakamoto, C Kejlberg, Y Yoshimura, TA Nielsen, MW Risør, ... Proceedings of the National Academy of Sciences 116 (42), 21031-21036, 2019 | 48 | 2019 |
| Cavity as a source of conformational fluctuation and high-energy state: High-pressure NMR study of a cavity-enlarged mutant of T4Lysozyme A Maeno, D Sindhikara, F Hirata, R Otten, FW Dahlquist, S Yokoyama, ... Biophysical Journal 108 (1), 133-145, 2015 | 40 | 2015 |
| A delicate interplay of structure, dynamics, and thermodynamics for function: a high pressure NMR study of outer surface protein A R Kitahara, AK Simorellis, K Hata, A Maeno, S Yokoyama, S Koide, ... Biophysical journal 102 (4), 916-926, 2012 | 39 | 2012 |
| Pressure and temperature phase diagram for liquid–liquid phase separation of the RNA-binding protein fused in sarcoma S Li, T Yoshizawa, R Yamazaki, A Fujiwara, T Kameda, R Kitahara The Journal of Physical Chemistry B 125 (25), 6821-6829, 2021 | 38 | 2021 |
| Evolutionally conserved intermediates between ubiquitin and NEDD8 R Kitahara, Y Yamaguchi, E Sakata, T Kasuya, K Tanaka, K Kato, ... Journal of molecular biology 363 (2), 395-404, 2006 | 37 | 2006 |
| Characterization of low-lying excited states of proteins by high-pressure NMR MP Williamson, R Kitahara Biochimica et Biophysica Acta (BBA)-Proteins and Proteomics 1867 (3), 350-358, 2019 | 33 | 2019 |
| Structural plasticity of staphylococcal nuclease probed by perturbation with pressure and pH R Kitahara, K Hata, A Maeno, K Akasaka, MS Chimenti, ... Proteins: Structure, Function, and Bioinformatics 79 (4), 1293-1305, 2011 | 33 | 2011 |
| Solution Structure of the Q41N Variant of Ubiquitin as a Model for the Alternatively Folded N2 State of Ubiquitin S Kitazawa, T Kameda, M Yagi-Utsumi, K Sugase, NJ Baxter, K Kato, ... Biochemistry 52 (11), 1874-1885, 2013 | 32 | 2013 |
| Solvent environments significantly affect the enzymatic function of Escherichia coli dihydrofolate reductase: comparison of wild-type protein and active-site mutant D27E E Ohmae, Y Miyashita, S Tate, K Gekko, S Kitazawa, R Kitahara, ... Biochimica et Biophysica Acta (BBA)-Proteins and Proteomics 1834 (12), 2782-2794, 2013 | 31 | 2013 |
