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Ryo Kitahara
Ryo Kitahara
Unknown affiliation
Verified email at ph.ritsumei.ac.jp
Title
Cited by
Cited by
Year
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
1922005
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
1182003
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
1092013
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
1072004
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
992002
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
982000
Two folded conformers of ubiquitin revealed by high-pressure NMR
R Kitahara, H Yamada, K Akasaka
Biochemistry 40 (45), 13556-13563, 2001
782001
Exploring the folding energy landscape with pressure
K Akasaka, R Kitahara, YO Kamatari
Archives of biochemistry and biophysics 531 (1-2), 110-115, 2013
772013
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
662013
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
602002
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
542006
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
482019
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
402015
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
392021
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
392012
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
372006
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
332019
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
332011
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
322013
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
312013
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