Ailiken, G.; Kitamura, K.; Hoshino, T.; Satoh, M.; Tanaka, N.; Minamoto, T.; Rahmutulla, B.; Kobayashi, S.; Kano, M.; Tanaka, T.; Kaneda, A.; Nomura, F.; Matsubara, H.; Matsushita, K. Post-Transcriptional Regulation of BRG1 by FIRΔexon2 in Gastric Cancer. Oncogenesis 2020, 9 (2), 26. https://doi.org/10.1038/s41389-020-0205-4. Kitahara, M.; Fudo, S.; Yoneda, T.; Nukaga, M.; Hoshino, T. Anisotropic Distribution of Ammonium Sulfate Ions in Protein Crystallization. Cryst. Growth Des. 2019, 19 (11), 6004–6010. https://doi.org/10.1021/acs.cgd.9b00256. Tsutsumiuchi, M.; Hoshino, H.; Kogami, A.; Tsutsumiuchi, T.; Yokoyama, O.; Akama, T. O.; Kobayashi, M. Preferential Expression of Sialyl 6’-Sulfo N-Acetyllactosamine-Capped O-Glycans on High Endothelial Venules in Human Peripheral Lymph Nodes. Lab. Invest. 2019, 99 (10), 1428–1441. https://doi.org/10.1038/s41374-019-0267-0. Kobayashi, S.; Hiwasa, T.; Ishige, T.; Rahmutulla, B.; Kano, M.; Hoshino, T.; Minamoto, T.; Shimada, H.; Nomura, F.; Matsubara, H.; Matsushita, K. Anti-FIRΔexon2, a Splicing Variant Form of PUF60, Autoantibody Is Detected in the Sera of Esophageal Squamous Cell Carcinoma. Cancer Sci. 2019, 110 (6), 2004–2013. https://doi.org/10.1111/cas.14024. Qu, L.; Fudo, S.; Matsuzaki, K.; Hoshino, T. Computational Study on the Assembly of Amyloid β-Peptides in the Hydrophobic Environment. Chem. Pharm. Bull. 2019, 67 (9), 959–965. https://doi.org/10.1248/cpb.c19-00171. Ogura, Y.; Hoshino, T.; Tanaka, N.; Ailiken, G.; Kobayashi, S.; Kitamura, K.; Rahmutulla, B.; Kano, M.; Murakami, K.; Akutsu, Y.; Nomura, F.; Itoga, S.; Matsubara, H.; Matsushita, K. Disturbed Alternative Splicing of FIR (PUF60) Directed Cyclin E Overexpression in Esophageal Cancers. Oncotarget 2018, 9 (33), 22929–22944. https://doi.org/10.18632/oncotarget.25149. Nukaga, M.; Papp-Wallace, K. M.; Hoshino, T.; Lefurgy, S. T.; Bethel, C. R.; Barnes, M. D.; Zeiser, E. T.; Johnson, J. K.; Bonomo, R. A. Probing the Mechanism of Inactivation of the FOX-4 Cephamycinase by Avibactam. Antimicrob. Agents Chemother. 2018, 62 (5). https://doi.org/10.1128/AAC.02371-17. Neya, S.; Yoneda, T.; Omori, H.; Hoshino, T.; Kawaguchi, A. T.; Suzuki, M. Synthesis of 1,4,5,8-Tetraethyl-2,3,6,7-Tetravinylporphyrin from a Knorr’s Pyrrole Analogue. Tetrahedron 2017, 73 (48), 6780–6785. https://doi.org/10.1016/j.tet.2017.10.035. Fudo, S.; Qi, F.; Nukaga, M.; Hoshino, T. Influence of Precipitants on Molecular Arrangements and Space Groups of Protein Crystals. Cryst. Growth Des. 2017, 17 (2), 534–542. https://doi.org/10.1021/acs.cgd.6b01385. Fuji, H.; Qi, F.; Qu, L.; Takaesu, Y.; Hoshino, T. Prediction of Ligand Binding Affinity to Target Proteins by Molecular Mechanics Theoretical Calculation. Chem. Pharm. Bull. 2017, 65 (5), 461–468. https://doi.org/10.1248/cpb.c16-00913. Kobayashi, S.; Hoshino, T.; Hiwasa, T.; Satoh, M.; Rahmutulla, B.; Tsuchida, S.; Komukai, Y.; Tanaka, T.; Matsubara, H.; Shimada, H.; Nomura, F.; Matsushita, K. Anti-FIRs (PUF60) Auto-Antibodies Are Detected in the Sera of Early-Stage Colon Cancer Patients. Oncotarget 2016, 7 (50), 82493–82503. https://doi.org/10.18632/oncotarget.12696. Urano, E.; Miyauchi, K.; Kojima, Y.; Hamatake, M.; Ablan, S. D.; Fudo, S.; Freed, E. O.; Hoshino, T.; Komano, J. A Triazinone Derivative Inhibits HIV-1 Replication by Interfering with Reverse Transcriptase Activity. ChemMedChem 2016, 11 (20), 2320–2326. https://doi.org/10.1002/cmdc.201600375. Neya, S.; Yoneda, T.; Hoshino, T.; Kawaguchi, A. T.; Suzuki, M. Synthesis of Type III Isomers of Diacetyldeutero-, Hemato-, and Protoporphyrins with the Use of Knorr’s Pyrrole. Tetrahedron 2016, 72 (27), 4022–4026. https://doi.org/10.1016/j.tet.2016.05.030. Fukuda, M.; Takatori, A.; Nakamura, Y.; Suganami, A.; Hoshino, T.; Tamura, Y.; Nakagawara, A. Effects of Novel Small Compounds Targeting TrkB on Neuronal Cell Survival and Depression-like Behavior. Neurochem. Int. 2016, 97, 42–48. https://doi.org/10.1016/j.neuint.2016.04.017. Fudo, S.; Yamamoto, N.; Nukaga, M.; Odagiri, T.; Tashiro, M.; Hoshino, T. Two Distinctive Binding Modes of Endonuclease Inhibitors to the N-Terminal Region of Influenza Virus Polymerase Acidic Subunit. Biochemistry 2016, 55 (18), 2646–2660. https://doi.org/10.1021/acs.biochem.5b01087. Fudo, S.; Yamamoto, N.; Nukaga, M.; Odagiri, T.; Tashiro, M.; Neya, S.; Hoshino, T. Structural and Computational Study on Inhibitory Compounds for Endonuclease Activity of Influenza Virus Polymerase. Bioorg. Med. Chem. 2015, 23 (17), 5466–5475. https://doi.org/10.1016/j.bmc.2015.07.046. Qi, F.; Fudo, S.; Neya, S.; Hoshino, T. A Dominant Factor for Structural Classification of Protein Crystals. J. Chem. Inf. Model. 2015, 55 (8), 1673–1685. https://doi.org/10.1021/acs.jcim.5b00052. Nakamura, Y.; Suganami, A.; Fukuda, M.; Hasan, M. K.; Yokochi, T.; Takatori, A.; Satoh, S.; Hoshino, T.; Tamura, Y.; Nakagawara, A. Identification of Novel Candidate Compounds Targeting TrkB to Induce Apoptosis in Neuroblastoma. Cancer Med. 2014, 3 (1), 25–35. https://doi.org/10.1002/cam4.175. Qi, F.; Fudo, S.; Neya, S.; Hoshino, T. A Cluster Analysis on the Structural Diversity of Protein Crystals, Exemplified by Human Immunodeficiency Virus Type 1 Protease. Chem. Pharm. Bull. 2014, 62 (6), 568–577. https://doi.org/10.1248/cpb.c14-00095. Mahmood, I.; Liu, X.; Neya, S.; Hoshino, T. Influence of Lipid Composition on the Structural Stability of G-Protein Coupled Receptor. Chem. Pharm. Bull. 2013, 61 (4), 426–437. https://doi.org/10.1248/cpb.c12-01059. Yanagita, H.; Yamamoto, N.; Fuji, H.; Liu, X.; Ogata, M.; Yokota, M.; Takaku, H.; Hasegawa, H.; Odagiri, T.; Tashiro, M.; Hoshino, T. Mechanism of Drug Resistance of Hemagglutinin of Influenza Virus and Potent Scaffolds Inhibiting Its Function. ACS Chem. Biol. 2012, 7 (3), 552–562. https://doi.org/10.1021/cb200332k. Yanagita, H.; Fudo, S.; Urano, E.; Ichikawa, R.; Ogata, M.; Yokota, M.; Murakami, T.; Wu, H.; Chiba, J.; Komano, J.; Hoshino, T. Structural Modulation Study of Inhibitory Compounds for Ribonuclease H Activity of Human Immunodeficiency Virus Type 1 Reverse Transcriptase. Chem. Pharm. Bull. 2012, 60 (6), 764–771. https://doi.org/10.1248/cpb.60.764. Yanagita, H.; Urano, E.; Matsumoto, K.; Ichikawa, R.; Takaesu, Y.; Ogata, M.; Murakami, T.; Wu, H.; Chiba, J.; Komano, J.; Hoshino, T. Structural and Biochemical Study on the Inhibitory Activity of Derivatives of 5-Nitro-Furan-2-Carboxylic Acid for RNase H Function of HIV-1 Reverse Transcriptase. Bioorg. Med. Chem. 2011, 19 (2), 816–825. https://doi.org/10.1016/j.bmc.2010.12.011. Fuji, H.; Urano, E.; Futahashi, Y.; Hamatake, M.; Tatsumi, J.; Hoshino, T.; Morikawa, Y.; Yamamoto, N.; Komano, J. Derivatives of 5-Nitro-Furan-2-Carboxylic Acid Carbamoylmethyl Ester Inhibit RNase H Activity Associated with HIV-1 Reverse Transcriptase. J. Med. Chem. 2009, 52 (5), 1380–1387. https://doi.org/10.1021/jm801071m. Hoshino, T.; Iwamoto, K.; Ode, H.; Ohdomari, I. Accurate Evaluation Method of Molecular Binding Affinity from Fluctuation Frequency. Jpn. J. Appl. Phys. 2008, 47 (5), 3719–3725. https://doi.org/10.1143/jjap.47.3719. Fuji, H.; Suzuki, M.; Neya, S.; Hoshino, T. Development of Software Program Predicting the Binding Site and the Binding Mode of Ligands Against a Target Protein. e-Journal of Surface Science and Nanotechnology 2008, 6, 241–245. https://doi.org/10.1380/ejssnt.2008.241. Ode, H.; Matsuyama, S.; Hata, M.; Neya, S.; Kakizawa, J.; Sugiura, W.; Hoshino, T. Computational Characterization of Structural Role of the Non-Active Site Mutation M36I of Human Immunodeficiency Virus Type 1 Protease. J. Mol. Biol. 2007, 370 (3), 598–607. https://doi.org/10.1016/j.jmb.2007.04.081. Ode, H.; Matsuyama, S.; Hata, M.; Hoshino, T.; Kakizawa, J.; Sugiura, W. Mechanism of Drug Resistance due to N88S in CRF01_AE HIV-1 Protease, Analyzed by Molecular Dynamics Simulations. J. Med. Chem. 2007, 50 (8), 1768–1777. https://doi.org/10.1021/jm061158i. Ode, H.; Neya, S.; Hata, M.; Sugiura, W.; Hoshino, T. Computational Simulations of HIV-1 Proteases--Multi-Drug Resistance due to Nonactive Site Mutation L90M. J. Am. Chem. Soc. 2006, 128 (24), 7887–7895. https://doi.org/10.1021/ja060682b. Hata, M.; Fujii, Y.; Tanaka, Y.; Ishikawa, H.; Ishii, M.; Neya, S.; Tsuda, M.; Hoshino, T. Substrate Deacylation Mechanisms of Serine-β-Lactamases. Biol. Pharm. Bull. 2006, 29 (11), 2151–2159. https://doi.org/10.1248/bpb.29.2151. Mori, K.; Hata, M.; Neya, S.; Hoshino, T. Common Semiopen Conformations of Mg2+-Free Ras, Rho, Rab, Arf, and Ran Proteins Combined with GDP and Their Similarity with GEF-Bound Forms. J. Am. Chem. Soc. 2005, 127 (43), 15127–15137. https://doi.org/10.1021/ja0467972. Ode, H.; Ota, M.; Neya, S.; Hata, M.; Sugiura, W.; Hoshino, T. Resistant Mechanism against Nelfinavir of Human Immunodeficiency Virus Type 1 Proteases. J. Phys. Chem. B 2005, 109 (1), 565–574. https://doi.org/10.1021/jp046860+. Mori, K.; Hata, M.; Neya, S.; Hoshino, T. A Study on the Role of Mg2+ in a Ras Protein by MD Simulation. Chem-Bio Inf. J. 2002, 2 (4), 147–155. https://doi.org/10.1273/cbij.2.147.