業績 - Publications

2023

  1. P. C. Shih, M. Naganuma, G. Tsuji, Y. Demizu, M. Naito, Development of decoy oligonucleotide-warheaded chimeric molecules targeting STAT3. Bioorg Med Chem. 2023; 95: 117507. doi: 10.1016/j.bmc.2023.117507
  2. P. C. Shih, M. Naganuma, Y. Demizu, M. Naito, Current Status of Oligonucleotide-Based Protein Degraders. Pharmaceutics. 2023; 15 (3): 765. doi: 10.3390/pharmaceutics15030765
  3. W. Sato, M. Naito, Inducing Protein Degradation to Overcome Resistance to Kinase Inhibitors. Biochemistry. 2023; 62 (3): 557-558. doi: 10.1021/acs.biochem.2c00223
  4. H. Yokoo, M. Naito, Y. Demizu, Investigating the cell permeability of proteolysis-targeting chimeras (PROTACs). Expert Opin Drug Discov. 2023; 18 (4): 357-361. doi: 10.1080/17460441.2023.2187047
  5. H. Xu, T. Kurohara, N. Ohoka, G. Tsuji, T. Inoue, M. Naito, Y. Demizu, Development of versatile solid-phase methods for syntheses of PROTACs with diverse E3 ligands. Bioorg Med Chem. 2023; 86: 117293. doi: 10.1016/j.bmc.2023.117293
  6. H. Tsujimura, M. Naganuma, N. Ohoka, T. Inoue, M. Naito, G. Tsuji, Y. Demizu, Development of DNA Aptamer-Based PROTACs That Degrade the Estrogen Receptor. ACS Med Chem Lett. 2023; 14 (6): 827-832. doi: 10.1021/acsmedchemlett.3c00126
  7. M. Naganuma, N. Ohoka, G. Tsuji, T. Inoue, M. Naito, Y. Demizu, Structural Optimization of Decoy Oligonucleotide-Based PROTAC That Degrades the Estrogen Receptor. Bioconjugate chemistry. 2023; 34 (10): 1780-1788. doi: 10.1021/acs.bioconjchem.3c00332
  8. N. Cho, M. Naito, Synthesis of SNIPERs against BCR-ABL with kinase inhibitors and a method to evaluate their growth inhibitory activity derived from BCR-ABL degradation. Methods Enzymol. 2023; 681: 41-60. doi: 10.1016/bs.mie.2022.09.001
  9. Y. Akizuki, M. Morita, Y. Mori, A. Kaiho-Soma, S. Dixit, A. Endo, M. Shimogawa, G. Hayashi, M. Naito, A. Okamoto, K. Tanaka, Y. Saeki, F. Ohtake, cIAP1-based degraders induce degradation via branched ubiquitin architectures. Nat Chem Biol. 2023; 19 (3): 311-322. doi: 10.1038/s41589-022-01178-1

日本語総説

  1. 佐藤和佳、内藤幹彦、分子標的薬の幅を広げるタンパク質分解誘導薬、腫瘍内科 32, 391-396, 2023

2022

  1. N. Shibata, N. Cho, H. Koyama, M. Naito, Development of a degrader against oncogenic fusion protein FGFR3-TACC3. Bioorg Med Chem Lett. 2022; 60: 128584. doi: 10.1016/j.bmcl.2022.128584
  2. N. Ohoka, M. Suzuki, T. Uchida, Y. Tsukumo, M. Yoshida, T. Inoue, H. Ohki, M. Naito, Development of a potent small-molecule degrader against oncogenic BRAF(V600E) protein that evades paradoxical MAPK activation. Cancer Sci. 2022; 113 (8): 2828-2838. doi: 10.1111/cas.15401
  3. N. Ohoka, M. Suzuki, T. Uchida, G. Tsuji, Y. Tsukumo, M. Yoshida, T. Inoue, Y. Demizu, H. Ohki, M. Naito, Development of Gilteritinib-Based Chimeric Small Molecules that Potently Induce Degradation of FLT3-ITD Protein. ACS Med Chem Lett. 2022; 13 (12): 1885-1891. doi: 10.1021/acsmedchemlett.2c00402
  4. M. Naito, Targeted protein degradation and drug discovery. J Biochem. 2022; 172 (2): 61-69. doi: 10.1093/jb/mvac041
  5. N. Ohoka, H. Yokoo, K. Okuhira, Y. Demizu, M. Naito, Molecular Design, Synthesis, and Evaluation of SNIPER (ER) that Induces Targeted Protein Degradation of ERalpha. Methods in molecular biology. 2022; 2418: 363-382. doi: 10.1007/978-1-0716-1920-9_20
  6. S. Yu, L. Wang, D. Che, M. Zhang, M. Li, M. Naito, W. Xin, L. Zhou, Targeting CRABP-II overcomes pancreatic cancer drug resistance by reversing lipid raft cholesterol accumulation and AKT survival signaling. J Exp Clin Cancer Res. 2022; 41 (1): 88. doi: 10.1186/s13046-022-02261-0
  7. M. Naganuma, N. Ohoka, G. Tsuji, H. Tsujimura, K. Matsuno, T. Inoue, M. Naito, Y. Demizu, Development of Chimeric Molecules That Degrade the Estrogen Receptor Using Decoy Oligonucleotide Ligands. ACS medicinal chemistry letters. 2022; 13 (1): 134-139. doi: 10.1021/acsmedchemlett.1c00629
  8. H. Xu, T. Kurohara, R. Takano, H. Yokoo, N. Shibata, N. Ohoka, T. Inoue, M. Naito, Y. Demizu, Development of Rapid and Facile Solid-Phase Synthesis of PROTACs via a Variety of Binding Styles. ChemistryOpen. 2022; 11 (7): e202200131. doi: 10.1002/open.202200131
  9. N. Nakano, K. Fukuda, E. Tashiro, H. Ishikawa, W. Nagano, R. Kawamoto, A. Mori, M. Watanabe, R. Yamazaki, T. Nakane, M. Naito, I. Okamoto, S. Itoh, Hybrid molecule between platanic acid and LCL-161 as a yes-associated protein (YAP) degrader. J Biochem. 2022. doi: 10.1093/jb/mvac021
  10. Y. Murakami, H. Osawa, T. Kurohara, Y. Yanase, T. Ito, H. Yokoo, N. Shibata, M. Naito, K. Aritake, Y. Demizu, Structure-activity relationship study of PROTACs against hematopoietic prostaglandin D(2) synthase. RSC Med Chem. 2022; 13 (12): 1495-1503. doi: 10.1039/d2md00284a

日本語総説

  1. 内藤幹彦、タンパク質分解技術と創薬　〜PROTAC/SNIPER化合物の開発〜 、生化学 第94巻第2号, 1-13, 2022
  2. 内藤幹彦、IAPの医薬品開発ーIAPアンタゴニストとSNIPER、医学のあゆみ 283, 524-530, 2022
  3. 内藤幹彦、標的タンパク質分解誘導薬の開発展望、腫瘍内科 29, 1-6, 2022

2021

  1. M. Naito, S. Murata. Gluing Proteins for Targeted Degradation. Cancer Cell. 2021;39(1):19-21. doi: 10.1016/j.ccell.2020.12.020
  2. Kaiho-Soma, Y. Akizuki, K. Igarashi, A. Endo, T. Shoda, Y. Kawase, Y. Demizu, M. Naito, Y. Saeki, K. Tanaka, F. Ohtake. TRIP12 promotes small-molecule-induced degradation through K29/K48-branched ubiquitin chains. Mol Cell. 2021;81(7):1411-24 e7. doi: 10.1016/j.molcel.2021.01.023
  3. H. Yokoo, N. Shibata, M. Naganuma, Y. Murakami, K. Fujii, T. Ito, K. Aritake, M. Naito, Y. Demizu. Development of a Hematopoietic Prostaglandin D Synthase-Degradation Inducer. ACS medicinal chemistry letters. 2021;12(2):236-41. doi: 10.1021/acsmedchemlett.0c00605
  4. H. Yokoo, N. Ohoka, M. Takyo, T. Ito, K. Tsuchiya, T. Kurohara, K. Fukuhara, T. Inoue, M. Naito, Y. Demizu. Peptide Stapling Improves the Sustainability of a Peptide-Based Chimeric Molecule That Induces Targeted Protein Degradation. Int J Mol Sci. 2021;22(16). doi: 10.3390/ijms22168772
  5. H. Xu, N. Ohoka, H. Yokoo, K. Nemoto, T. Ohtsuki, H. Matsufuji, M. Naito, T. Inoue, G. Tsuji, Y. Demizu. Development of Agonist-Based PROTACs Targeting Liver X Receptor. Front Chem. 2021;9:674967. doi: 10.3389/fchem.2021.674967
  6. Y. Tsukumo, G. Tsuji, H. Yokoo, N. Shibata, N. Ohoka, Y. Demizu, M. Naito. Protocols for Synthesis of SNIPERs and the Methods to Evaluate the Anticancer Effects. Methods in molecular biology. 2021;2365:331-47. doi: 10.1007/978-1-0716-1665-9_18
  7. H. Yokoo, N. Shibata, A. Endo, T. Ito, Y. Yanase, Y. Murakami, K. Fujii, K. Hamamura, Y. Saeki, M. Naito, K. Aritake, Y. Demizu, Discovery of a Highly Potent and Selective Degrader Targeting Hematopoietic Prostaglandin D Synthase via In Silico Design. J Med Chem. 2021; 64 (21): 15868-15882. doi: 10.1021/acs.jmedchem.1c01206
  8. R. Kawamoto, N. Nakano, H. Ishikawa, E. Tashiro, W. Nagano, K. Sano, M. Irie, M. Ikuta, F. Kishi, T. Nakane, M. Naito, S. Itoh, Narciclasine is a novel YAP inhibitor that disturbs interaction between YAP and TEAD4. BBA Adv. 2021; 1: 100008. doi: 10.1016/j.bbadva.2021.100008

日本語総説

  1. 内藤幹彦、ハイブリッド化合物 (PROTAC，SNIPER) 、細胞 53, 136-139, 2021
  2. 内藤幹彦、小松弘嗣、分子間相互作用を基盤とするユビキチン・プロテアソーム創薬、日薬理誌 156, 9-12, 2021

2020

  1. N. Shibata, N. Ohoka, G. Tsuji, Y. Demizu, K. Miyawaza, K. Ui-Tei, T. Akiyama, M. Naito. Deubiquitylase USP25 prevents degradation of BCR-ABL protein and ensures proliferation of Ph-positive leukemia cells. Oncogene. 2020;39(19):3867-78. doi: 10.1038/s41388-020-1253-0
  2. K. Yamano, R. Kikuchi, W. Kojima, R. Hayashida, F. Koyano, J. Kawawaki, T. Shoda, Y. Demizu, M. Naito, K. Tanaka, N. Matsuda. Critical role of mitochondrial ubiquitination and the OPTN-ATG9A axis in mitophagy. J Cell Biol. 2020;219(9):e201912144. doi: 10.1083/jcb.201912144
  3. M. Ishikawa, S. Tomoshige, Y. Demizu, M. Naito. Selective Degradation of Target Proteins by Chimeric Small-Molecular Drugs, PROTACs and SNIPERs. Pharmaceuticals (Basel). 2020;13(4):74. doi: 10.3390/ph13040074
  4. H. Yokoo, N. Ohoka, M. Naito, Y. Demizu. Design and synthesis of peptide-based chimeric molecules to induce degradation of the estrogen and androgen receptors. Bioorg Med Chem. 2020;28(15):115595. doi: 10.1016/j.bmc.2020.115595
  5. T. Shoda, N. Ohoka, G. Tsuji, T. Fujisato, H. Inoue, Y. Demizu, M. Naito, M. Kurihara. Targeted Protein Degradation by Chimeric Compounds using Hydrophobic E3 Ligands and Adamantane Moiety. Pharmaceuticals (Basel). 2020;13(3). doi: 10.3390/ph13030034
  6. Y. Tsukumo, M. Naito, T. Suzuki. Influence of EGFR-activating mutations on sensitivity to tyrosine kinase inhibitors in a KRAS mutant non-small cell lung cancer cell line. PLoS One. 2020;15(3):e0229712. doi: 10.1371/journal.pone.0229712
  7. X. You, S. Thiruppathi, W. Liu, Y. Cao, M. Naito, C. Furihata, M. Honma, Y. Luan, T. Suzuki. Detection of genome-wide low-frequency mutations with Paired-End and Complementary Consensus Sequencing (PECC-Seq) revealed end-repair-derived artifacts as residual errors. Arch Toxicol. 2020;94(10):3475-85. doi: 10.1007/s00204-020-02832-0
  8. T. Suzuki, Y. Tsukumo, C. Furihata, M. Naito, A. Kohara. Preparation of the standard cell lines for reference mutations in cancer gene-panels by genome editing in HEK 293 T/17 cells. Genes Environ. 2020;42:8. doi: 10.1186/s41021-020-0147-2

日本語総説

  1. 内藤幹彦、プロテインノックダウン技術の沿革と今後の展望、実験医学 38, 2300-2304, 2020
  2. 大岡伸通、内藤幹彦、キメラ化合物PROTAC/SNIPERの作用機序と新たな開発の動向、実験医学 38, 2321-2325, 2020
  3. 柴田識人、内藤幹彦、脱ユビキチン化酵素によるプロテインノックダウン、実験医学 38, 2337-2341, 2020
  4. 大岡伸通、内藤幹彦、標的タンパク質を分解する新しい低分子医薬モダリティ、実験医学 38, 2644-2650, 2020
  5. 大岡伸通、内藤幹彦、新しい低分子薬の創薬モダリティPROTAC、ファルマシア 56, 41-45, 2020
  6. 柴田識人、内藤幹彦、選択的な蛋白質分解誘導剤SNIPERsとPROTACs、臨床免疫・アレルギー科 73, 540-546, 2020
  7. 内田恵理子、内藤幹彦、遺伝子治療の現状と課題（世界と日本）、CLINICAL NEUROSCIENCE 38, 299-303, 2020

2019

  1. N. Ohoka, G. Tsuji, T. Shoda, T. Fujisato, M. Kurihara, Y. Demizu, M. Naito. Development of Small Molecule Chimeras That Recruit AhR E3 Ligase to Target Proteins. ACS Chem Biol. 2019;14(12):2822-32. doi: 10.1021/acschembio.9b00704
  2. M. Naito, N. Ohoka, N. Shibata, Y. Tsukumo. Targeted Protein Degradation by Chimeric Small Molecules, PROTACs and SNIPERs. Front Chem. 2019;7:849. doi: 10.3389/fchem.2019.00849
  3. M. Naito, N. Ohoka, N. Shibata. SNIPERs-Hijacking IAP activity to induce protein degradation. Drug Discov Today: Technol. 2019;31:35-42. doi: 10.1016/j.ddtec.2018.12.002
  4. N. Shibata, N. Ohoka, T. Hattori, M. Naito. Development of a Potent Protein Degrader against Oncogenic BCR-ABL Protein. Chem Pharm Bull. 2019;67(3):165-72. doi: 10.1248/cpb.c18-00703
  5. N. Ohoka, O. Ujikawa, K. Shimokawa, T. Sameshima, N. Shibata, T. Hattori, H. Nara, N. Cho, M. Naito. Different Degradation Mechanisms of Inhibitor of Apoptosis Proteins (IAPs) by the Specific and Nongenetic IAP-Dependent Protein Eraser (SNIPER). Chem Pharm Bull. 2019;67(3):203-9. doi: 10.1248/cpb.c18-00567
  6. T. Misawa, N. Ohoka, M. Oba, H. Yamashita, M. Tanaka, M. Naito, Y. Demizu. Development of 2-aminoisobutyric acid (Aib)-rich cell-penetrating foldamers for efficient siRNA delivery. Chem Commun (Camb). 2019;55:7792-5. doi: 10.1039/c9cc02203a
  7. T. Misawa, C. Goto, N. Shibata, M. Hirano, Y. Kikuchi, M. Naito, Y. Demizu. Rational design of novel amphipathic antimicrobial peptides focused on the distribution of cationic amino acid residues. Medchemcomm. 2019;10(6):896-900. doi: 10.1039/c9md00166b
  8. T. Yoshida, Y. Naito, H. Yasuhara, K. Sasaki, H. Kawaji, J. Kawai, M. Naito, H. Okuda, S. Obika, T. Inoue. Evaluation of off-target effects of gapmer antisense oligonucleotides using human cells. Genes Cells. 2019;24(12):827-35. doi: 10.1111/gtc.12730

日本語総説

  1. 内藤幹彦、タンパク質の発現を制御する技術と医薬品開発への応用、衛研報告 137, 1-5, 2019
  2. 内藤幹彦、SNIPERによるプロテインノックダウン技術と創薬、メディカル・サイエンス・ダイジェスト 45, 5-6, 2019
  3. 堀江透、内藤幹彦、質量分析法を用いたタンパク質の絶対定量と標的タンパク質分解誘導薬の開発、ファームステージ 18, 66-71, 2019
  4. 大岡伸通、柴田識人、服部隆行、内藤幹彦、細胞死―抗がん剤と細胞死、化学同人 173-185, 2019
  5. 築茂由則、鈴木孝昌、内藤幹彦、体内診断薬の現状と開発動向、レギュラトリーサイエンス学会誌 9, 5-15, 2019

2018

  1. N. Ohoka, Y. Morita, K. Nagai, K. Shimokawa, O. Ujikawa, I. Fujimori, M. Ito, Y. Hayase, K. Okuhira, N. Shibata, T. Hattori, T. Sameshima, O. Sano, R. Koyama, Y. Imaeda, H. Nara, N. Cho, M. Naito. Derivatization of inhibitor of apoptosis protein (IAP) ligands yields improved inducers of estrogen receptor alpha degradation. J Biol Chem. 2018;293(18):6776-90. doi: 10.1074/jbc.RA117.001091
  2. N. Shibata, K. Nagai, Y. Morita, O. Ujikawa, N. Ohoka, T. Hattori, R. Koyama, O. Sano, Y. Imaeda, H. Nara, N. Cho, M. Naito. Development of Protein Degradation Inducers of Androgen Receptor by Conjugation of Androgen Receptor Ligands and Inhibitor of Apoptosis Protein Ligands. J Med Chem. 2018;61(2):543-75. doi: 10.1021/acs.jmedchem.7b00168
  3. N. Shibata, K. Shimokawa, K. Nagai, N. Ohoka, T. Hattori, N. Miyamoto, O. Ujikawa, T. Sameshima, H. Nara, N. Cho, M. Naito. Pharmacological difference between degrader and inhibitor against oncogenic BCR-ABL kinase. Scientific reports. 2018;8(1):13549. doi: 10.1038/s41598-018-31913-5
  4. K. Okitsu, T. Hattori, T. Misawa, T. Shoda, M. Kurihara, M. Naito, Y. Demizu. Development of a Small Hybrid Molecule That Mediates Degradation of His-Tag Fused Proteins. J Med Chem. 2018;61(2):576-82. doi: 10.1021/acs.jmedchem.7b00413
  5. G. Tsuji, T. Hattori, M. Kato, W. Hakamata, H. Inoue, M. Naito, M. Kurihara, Y. Demizu, T. Shoda. Design and synthesis of cell-permeable fluorescent nitrilotriacetic acid derivatives. Bioorg Med Chem. 2018;26(20):5494-8. doi: 10.1016/j.bmc.2018.09.028
  6. R. Eto, T. Misawa, T. Noguchi-Yachide, N. Ohoka, M. Kurihara, M. Naito, M. Tanaka, Y. Demizu. Design and synthesis of estrogen receptor ligands with a 4-heterocycle-4-phenylheptane skeleton. Bioorg Med Chem. 2018;26(8):1638-42. doi: 10.1016/j.bmc.2018.02.010
  7. T. Hattori, M. Watanabe-Takahashi, K. Nishikawa, M. Naito. Acquired Resistance to Shiga Toxin-Induced Apoptosis by Loss of CD77 Expression in Human Myelogenous Leukemia Cell Line, THP-1. Biological & pharmaceutical bulletin. 2018;41(9):1475-9. doi: 10.1248/bpb.b18-00277
  8. T. Yoshida, Y. Naito, K. Sasaki, E. Uchida, Y. Sato, M. Naito, T. Kawanishi, S. Obika, T. Inoue. Estimated number of off-target candidate sites for antisense oligonucleotides in human mRNA sequences. Genes Cells. 2018;23(6):448-55. doi: 10.1111/gtc.12587
  9. K. Shimasaki, M. Watanabe-Takahashi, M. Umeda, S. Funamoto, Y. Saito, N. Noguchi, K. Kumagai, K. Hanada, F. Tsukahara, Y. Maru, N. Shibata, M. Naito, K. Nishikawa. Pleckstrin homology domain of p210 BCR-ABL interacts with cardiolipin to regulate its mitochondrial translocation and subsequent mitophagy. Genes Cells. 2018;23(1):22-34. doi: 10.1111/gtc.12544

日本語総説

  1. 大岡伸通、内藤幹彦、標的タンパク質を分解する新たな低分子薬の開発技術、実験医学 36, 3125-3132, 2018
  2. 柴田識人、内藤幹彦、標的タンパク質の分解を誘導するハイブリッド化合物SNIPERsとPROTACs、医学のあゆみ 267, 1069-1075, 2018
  3. 大岡伸通、内藤幹彦、蛋白質分解医薬品の開発動向、医薬品医療機器レギュラトリーサイエンス 49, 513-524, 2018

2017

  1. N. Ohoka, K. Okuhira, M. Ito, K. Nagai, N. Shibata, T. Hattori, O. Ujikawa, K. Shimokawa, O. Sano, R. Koyama, H. Fujita, M. Teratani, H. Matsumoto, Y. Imaeda, H. Nara, N. Cho, M. Naito. In Vivo Knockdown of Pathogenic Proteins via Specific and Nongenetic Inhibitor of Apoptosis Protein (IAP)-dependent Protein Erasers (SNIPERs). J Biol Chem. 2017;292(11):4556-70. doi: 10.1074/jbc.M116.768853
  2. K. Okuhira, T. Shoda, R. Omura, N. Ohoka, T. Hattori, N. Shibata, Y. Demizu, R. Sugihara, A. Ichino, H. Kawahara, Y. Itoh, M. Ishikawa, Y. Hashimoto, M. Kurihara, S. Itoh, H. Saito, M. Naito. Targeted Degradation of Proteins Localized in Subcellular Compartments by Hybrid Small Molecules. Mol Pharmacol. 2017;91(3):159-66. doi: 10.1124/mol.116.105569
  3. N. Shibata, N. Miyamoto, K. Nagai, K. Shimokawa, T. Sameshima, N. Ohoka, T. Hattori, Y. Imaeda, H. Nara, N. Cho, M. Naito. Development of protein degradation inducers of oncogenic BCR-ABL protein by conjugation of ABL kinase inhibitors and IAP ligands. Cancer Sci. 2017;108(8):1657-66. doi: 10.1111/cas.13284
  4. K. Shimokawa, N. Shibata, T. Sameshima, N. Miyamoto, O. Ujikawa, H. Nara, N. Ohoka, T. Hattori, N. Cho, M. Naito. Targeting the Allosteric Site of Oncoprotein BCR-ABL as an Alternative Strategy for Effective Target Protein Degradation. ACS medicinal chemistry letters. 2017;8(10):1042-7. doi: 10.1021/acsmedchemlett.7b00247
  5. N. Ohoka, K. Nagai, N. Shibata, T. Hattori, H. Nara, N. Cho, M. Naito. SNIPER(TACC3) induces cytoplasmic vacuolization and sensitizes cancer cells to Bortezomib. Cancer Sci. 2017;108(5):1032-41. doi: 10.1111/cas.13198
  6. N. Ohoka, T. Misawa, M. Kurihara, Y. Demizu, M. Naito. Development of a peptide-based inducer of protein degradation targeting NOTCH1. Bioorg Med Chem Lett. 2017;27(22):4985-8. doi: 10.1016/j.bmcl.2017.10.011
  7. T. Hattori, K. Okitsu, N. Yamazaki, N. Ohoka, N. Shibata, T. Misawa, M. Kurihara, Y. Demizu, M. Naito. Simple and efficient knockdown of His-tagged proteins by ternary molecules consisting of a His-tag ligand, a ubiquitin ligase ligand, and a cell-penetrating peptide. Bioorg Med Chem Lett. 2017;27(18):4478-81. doi: 10.1016/j.bmcl.2017.08.001
  8. H. Yamashita, T. Misawa, M. Oba, M. Tanaka, M. Naito, M. Kurihara, Y. Demizu. Development of helix-stabilized cell-penetrating peptides containing cationic alpha,alpha-disubstituted amino acids as helical promoters. Bioorg Med Chem. 2017;25(6):1846-51. doi: 10.1016/j.bmc.2017.01.044
  9. T. Shoda, M. Kato, T. Fujisato, Y. Demizu, H. Inoue, M. Naito, M. Kurihara. Tamoxifen and Fulvestrant Hybrids Showed Potency as Selective Estrogen Receptor Down-Regulators. Medicinal chemistry. 2017;13(3):206-13. doi: 10.2174/1573406412666160805101408
  10. T. Misawa, T. Fujisato, Y. Kanda, N. Ohoka, T. Shoda, M. Yorioka, M. Makishima, Y. Sekino, M. Naito, Y. Demizu, M. Kurihara. Design and synthesis of novel selective estrogen receptor degradation inducers based on the diphenylheptane skeleton. Medchemcomm. 2017;8(1):239-46. doi: 10.1039/c6md00553e

日本語総説

  1. 内藤幹彦、大岡伸通、柴田識人、服部隆行、ケミカルプロテインノックダウン：標的タンパク質を分解するSNIPER化合物の開発、MEDCHEM NEWS 28, 29-35, 2018
  2. 築茂由則、鈴木孝昌、内藤幹彦、コンパニオン診断薬の現状と今後の課題、レギュラトリーサイエンス学会誌 7, 71-78, 2017

2016

  1. K. Okuhira, Y. Demizu, T. Hattori, N. Ohoka, N. Shibata, M. Kurihara, M. Naito. Molecular Design, Synthesis, and Evaluation of SNIPER(ER) That Induces Proteasomal Degradation of ERalpha. Methods in molecular biology. 2016;1366:549-60. doi: 10.1007/978-1-4939-3127-9_42
  2. N. Ohoka, N. Shibata, T. Hattori, M. Naito. Protein Knockdown Technology: Application of Ubiquitin Ligase to Cancer Therapy. Curr Cancer Drug Targets. 2016;16(2):136-46. doi:
  3. Y. Demizu, N. Shibata, T. Hattori, N. Ohoka, H. Motoi, T. Misawa, T. Shoda, M. Naito, M. Kurihara. Development of BCR-ABL degradation inducers via the conjugation of an imatinib derivative and a cIAP1 ligand. Bioorg Med Chem Lett. 2016;26(20):4865-9. doi: 10.1016/j.bmcl.2016.09.041
  4. Y. Demizu, N. Ohoka, T. Nagakubo, H. Yamashita, T. Misawa, K. Okuhira, M. Naito, M. Kurihara. Development of a peptide-based inducer of nuclear receptors degradation. Bioorg Med Chem Lett. 2016;26(11):2655-8. doi: 10.1016/j.bmcl.2016.04.013
  5. T. Hattori, M. Watanabe-Takahashi, I. Shiina, Y. Ohashi, S. Dan, K. Nishikawa, T. Yamori, M. Naito. M-COPA, a novel Golgi system disruptor, suppresses apoptosis induced by Shiga toxin. Genes Cells. 2016;21(8):901-6. doi: 10.1111/gtc.12386
  6. H. Yamashita, M. Oba, T. Misawa, M. Tanaka, T. Hattori, M. Naito, M. Kurihara, Y. Demizu. A Helix-Stabilized Cell-Penetrating Peptide as an Intracellular Delivery Tool. Chembiochem. 2016;17(2):137-40. doi: 10.1002/cbic.201500468
  7. H. Yamashita, T. Kato, M. Oba, T. Misawa, T. Hattori, N. Ohoka, M. Tanaka, M. Naito, M. Kurihara, Y. Demizu. Development of a Cell-penetrating Peptide that Exhibits Responsive Changes in its Secondary Structure in the Cellular Environment. Scientific reports. 2016;6:33003. doi: 10.1038/srep33003
  8. T. Shoda, M. Kato, T. Fujisato, T. Misawa, Y. Demizu, H. Inoue, M. Naito, M. Kurihara. Synthesis and evaluation of raloxifene derivatives as a selective estrogen receptor down-regulator. Bioorg Med Chem. 2016;24(13):2914-9. doi: 10.1016/j.bmc.2016.04.068

2015

  1. N. Shibata, N. Ohoka, Y. Sugaki, C. Onodera, M. Inoue, Y. Sakuraba, D. Takakura, N. Hashii, N. Kawasaki, Y. Gondo, M. Naito. Degradation of Stop Codon Read-through Mutant Proteins via the Ubiquitin-Proteasome System Causes Hereditary Disorders. J Biol Chem. 2015;290(47):28428-37. doi: 10.1074/jbc.M115.670901
  2. T. Hattori, M. Watanabe-Takahashi, N. Ohoka, T. Hamabata, K. Furukawa, K. Nishikawa, M. Naito. Proteasome inhibitors prevent cell death and prolong survival of mice challenged by Shiga toxin. FEBS open bio. 2015;5:605-14. doi: 10.1016/j.fob.2015.06.005
  3. T. Shoda, M. Kato, R. Harada, T. Fujisato, K. Okuhira, Y. Demizu, H. Inoue, M. Naito, M. Kurihara. Synthesis and evaluation of tamoxifen derivatives with a long alkyl side chain as selective estrogen receptor down-regulators. Bioorg Med Chem. 2015;23(13):3091-6. doi: 10.1016/j.bmc.2015.05.002
  4. T. Misawa, M. Yorioka, Y. Demizu, T. Noguchi-Yachide, N. Ohoka, M. Kurashima-Kinoshita, H. Motoyoshi, H. Nojiri, A. Kittaka, M. Makishima, M. Naito, M. Kurihara. Effects of alkyl side chains and terminal hydrophilicity on vitamin D receptor (VDR) agonistic activity based on the diphenylpentane skeleton. Bioorg Med Chem Lett. 2015;25(22):5362-6. doi: 10.1016/j.bmcl.2015.09.030
  5. Y. Demizu, T. Misawa, T. Nagakubo, Y. Kanda, K. Okuhira, Y. Sekino, M. Naito, M. Kurihara. Structural development of stabilized helical peptides as inhibitors of estrogen receptor (ER)-mediated transcription. Bioorg Med Chem. 2015;23(15):4132-8. doi: 10.1016/j.bmc.2015.06.067
  6. S. Tomoshige, M. Naito, Y. Hashimoto, M. Ishikawa. Degradation of HaloTag-fused nuclear proteins using bestatin-HaloTag ligand hybrid molecules. Org Biomol Chem. 2015;13(38):9746-50. doi: 10.1039/c5ob01395j

2014

  1. R. Kikuchi, H. Ohata, N. Ohoka, A. Kawabata, M. Naito. APOLLON Protein Promotes Early Mitotic CYCLIN A Degradation Independent of the Spindle Assembly Checkpoint. J Biol Chem. 2014;289(6):3457-67. doi: 10.1074/jbc.M113.514430
  2. N. Ohoka, K. Nagai, T. Hattori, K. Okuhira, N. Shibata, N. Cho, M. Naito. Cancer cell death induced by novel small molecules degrading the TACC3 protein via the ubiquitin-proteasome pathway. Cell Death Dis. 2014;5:e1513. doi: 10.1038/cddis.2014.471
  3. T. Hattori, C. Uchida, H. Takahashi, N. Yamamoto, M. Naito, Y. Taya. Distinct and site-specific phosphorylation of the retinoblastoma protein at serine 612 in differentiated cells. PLoS One. 2014;9(1):e86709. doi: 10.1371/journal.pone.0086709
  4. T. Shoda, K. Okuhira, M. Kato, Y. Demizu, H. Inoue, M. Naito, M. Kurihara. Design and synthesis of tamoxifen derivatives as a selective estrogen receptor down-regulator. Bioorg Med Chem Lett. 2014;24(1):87-9. doi: 10.1016/j.bmcl.2013.11.078
  5. T. Nagakubo, Y. Demizu, Y. Kanda, T. Misawa, T. Shoda, K. Okuhira, Y. Sekino, M. Naito, M. Kurihara. Development of cell-penetrating r7 fragment-conjugated helical peptides as inhibitors of estrogen receptor-mediated transcription. Bioconjugate chemistry. 2014;25(11):1921-4. doi: 10.1021/bc500480e
  6. Y. Hashimoto, Y. Takeshita, M. Naito, H. Uchino, M. Matsuoka. Apollon/Bruce is upregulated by Humanin. Molecular and cellular biochemistry. 2014;397(1-2):147-55. doi: 10.1007/s11010-014-2182-4
  7. H. Cui, W. Wu, K. Okuhira, K. Miyazawa, T. Hattori, K. Sai, M. Naito, K. Suzuki, T. Nishimura, Y. Sakamoto, A. Ogata, T. Maeno, A. Inomata, D. Nakae, A. Hirose, T. Nishimaki-Mogami. High-temperature calcined fullerene nanowhiskers as well as long needle-like multi-wall carbon nanotubes have abilities to induce NLRP3-mediated IL-1beta secretion. Biochem Biophys Res Commun. 2014;452(3):593-9. doi: 10.1016/j.bbrc.2014.08.118

2013

  1. K. Okuhira, Y. Demizu, T. Hattori, N. Ohoka, N. Shibata, T. Nishimaki-Mogami, H. Okuda, M. Kurihara, M. Naito. Development of hybrid small molecules that induce degradation of estrogen receptor-alpha and necrotic cell death in breast cancer cells. Cancer Sci. 2013;104(11):1492-8. doi: 10.1111/cas.12272

2012

  1. Y. Itoh, M. Ishikawa, R. Kitaguchi, K. Okuhira, M. Naito, Y. Hashimoto. Double protein knockdown of cIAP1 and CRABP-II using a hybrid molecule consisting of ATRA and IAPs antagonist. Bioorg Med Chem Lett. 2012;22(13):4453-7. doi: 10.1016/j.bmcl.2012.04.134
  2. Y. Demizu, K. Okuhira, H. Motoi, A. Ohno, T. Shoda, K. Fukuhara, H. Okuda, M. Naito, M. Kurihara. Design and synthesis of estrogen receptor degradation inducer based on a protein knockdown strategy. Bioorg Med Chem Lett. 2012;22(4):1793-6. doi: 10.1016/j.bmcl.2011.11.086
  3. N. Ohoka, K. Okuhira, H. Cui, W. Wu, R. Sato, M. Naito, T. Nishimaki-Mogami. HNF4alpha Increases Liver-Specific Human ATP-Binding Cassette Transporter A1 Expression and Cholesterol Efflux to Apolipoprotein A-I in Response to Cholesterol Depletion. Arterioscler Thromb Vasc Biol. 2012;32(4):1005-14. doi: 10.1161/ATVBAHA.111.238360

2011

  1. K. Okuhira, N. Ohoka, K. Sai, T. Nishimaki-Mogami, Y. Itoh, M. Ishikawa, Y. Hashimoto, M. Naito. Specific degradation of CRABP-II via cIAP1-mediated ubiquitylation induced by hybrid molecules that crosslink cIAP1 and the target protein. FEBS Lett. 2011;585(8):1147-52. doi: S10.1016/j.febslet.2011.03.019
  2. Y. Itoh, R. Kitaguchi, M. Ishikawa, M. Naito, Y. Hashimoto. Design, synthesis and biological evaluation of nuclear receptor-degradation inducers. Bioorg Med Chem. 2011;19(22):6768-78. doi: 10.1016/j.bmc.2011.09.041
  3. Y. Itoh, M. Ishikawa, R. Kitaguchi, S. Sato, M. Naito, Y. Hashimoto. Development of target protein-selective degradation inducer for protein knockdown. Bioorg Med Chem. 2011;19(10):3229-41. doi: 10.1016/j.bmc.2011.03.057
  4. H. Cui, K. Okuhira, N. Ohoka, M. Naito, H. Kagechika, A. Hirose, T. Nishimaki-Mogami. Tributyltin chloride induces ABCA1 expression and apolipoprotein A-I-mediated cellular cholesterol efflux by activating LXRalpha/RXR. Biochem Pharmacol. 2011;81(6):819-24. doi: 10.1016/j.bcp.2010.12.023
  5. N. Katori, K. Sai, Y. Saito, H. Fukushima-Uesaka, K. Kurose, C. Yomota, T. Kawanishi, T. Nishimaki-Mogami, M. Naito, J. I. Sawada, H. Kunitoh, H. Nokihara, I. Sekine, Y. Ohe, T. Yoshida, Y. Matsumura, N. Saijo, N. Yamamoto, H. Okuda, T. Tamura. Genetic variations of orosomucoid genes associated with serum alpha-1-acid glycoprotein level and the pharmacokinetics of paclitaxel in Japanese cancer patients. J Pharm Sci. 2011;100:4546-59. doi: 10.1002/jps.22648

2010

  1. Y. Itoh, M. Ishikawa, M. Naito, Y. Hashimoto. Protein knockdown using methyl bestatin-ligand hybrid molecules: design and synthesis of inducers of ubiquitination-mediated degradation of cellular retinoic acid-binding proteins. J Am Chem Soc. 2010;132(16):5820-6. doi: 10.1021/ja100691p
  2. R. Katayama, T. Ishioka, S. Takada, R. Takada, N. Fujita, T. Tsuruo, M. Naito. Modulation of Wnt signaling by the nuclear localization of cellular FLIP-L. J Cell Sci. 2010;123(Pt 1):23-8. doi: 10.1242/jcs.058602
  3. S. Kim, N. Ohoka, K. Okuhira, K. Sai, T. Nishimaki-Mogami, M. Naito. Modulation of RIP1 ubiquitylation and distribution by MeBS to sensitize cancer cells to tumor necrosis factor alpha-induced apoptosis. Cancer Sci. 2010;101(11):2425-9. doi: 10.1111/j.1349-7006.2010.01697.x
  4. K. Okuhira, M. L. Fitzgerald, N. Tamehiro, N. Ohoka, K. Suzuki, J. Sawada, M. Naito, T. Nishimaki-Mogami. Binding of PDZ-RhoGEF to ATP-binding cassette transporter A1 (ABCA1) induces cholesterol efflux through RhoA activation and prevention of transporter degradation. J Biol Chem. 2010;285(21):16369-77. doi: 10.1074/jbc.M109.061424
  5. K. Sai, Y. Saito, N. Tatewaki, M. Hosokawa, N. Kaniwa, T. Nishimaki-Mogami, M. Naito, J. Sawada, K. Shirao, T. Hamaguchi, N. Yamamoto, H. Kunitoh, T. Tamura, Y. Yamada, Y. Ohe, T. Yoshida, H. Minami, A. Ohtsu, Y. Matsumura, N. Saijo, H. Okuda. Association of carboxylesterase 1A genotypes with irinotecan pharmacokinetics in Japanese cancer patients. Br J Clin Pharmacol. 2010;70(2):222-33. doi: 10.1111/j.1365-2125.2010.03695.x
  6. A. Nakamura, M. Naito, H. Arai, N. Fujita. Mitotic phosphorylation of Aki1 at Ser208 by cyclin B1-Cdk1 complex. Biochem Biophys Res Commun. 2010;393(4):872-6. doi: 10.1016/j.bbrc.2010.02.103
  7. K. Maekawa, N. Harakawa, T. Yoshimura, S. R. Kim, Y. Fujimura, F. Aohara, K. Sai, N. Katori, M. Tohkin, M. Naito, R. Hasegawa, H. Okuda, J. Sawada, T. Niwa, Y. Saito. CYP3A4*16 and CYP3A4*18 alleles found in East Asians exhibit differential catalytic activities for seven CYP3A4 substrate drugs. Drug Metab Dispos. 2010;38(12):2100-4. doi: 10.1124/dmd.110.034140
  8. S. Dohgu, N. Sumi, T. Nishioku, F. Takata, T. Watanabe, M. Naito, H. Shuto, A. Yamauchi, Y. Kataoka. Cyclosporin A induces hyperpermeability of the blood-brain barrier by inhibiting autocrine adrenomedullin-mediated up-regulation of endothelial barrier function. Eur J Pharmacol. 2010;644(1-3):5-9. doi: 10.1016/j.ejphar.2010.05.035

Before 2009（抜粋）

  1. K. Sekine, K. Takubo, R. Kikuchi, M. Nishimoto, M. Kitagawa, F. Abe, K. Nishikawa, T. Tsuruo, M. Naito. Small Molecules Destabilize cIAP1 by Activating Auto-ubiquitylation. J Biol Chem. 2008;283(14):8961-8.
  2. Y. Hao, K. Sekine, A. Kawabata, H. Nakamura, T. Ishioka, H. Ohata, R. Katayama, C. Hashimoto, X. Zhang, T. Noda, T. Tsuruo, M. Naito. Apollon ubiquitinates SMAC and caspase-9, and has an essential cytoprotection function. Nat Cell Biol. 2004;6(9):849-60.
  3. M. Naito, R. Katayama, T. Ishioka, A. Suga, K. Takubo, M. Nanjo, C. Hashimoto, M. Taira, S. Takada, R. Takada, M. Kitagawa, S. I. Matsuzawa, J. C. Reed, T. Tsuruo. Cellular FLIP Inhibits {beta}-Catenin Ubiquitylation and Enhances Wnt Signaling. Mol Cell Biol. 2004;24(19):8418-27.
  4. T. Tsuruo, M. Naito, A. Tomida, N. Fujita, T. Mashima, H. Sakamoto, N. Haga. Molecular targeting therapy of cancer: drug resistance, apoptosis and survival signal. Cancer Sci. 2003;94(1):15-21.
  5. M. Naito, Y. Matsuba, S. Sato, H. Hirata, T. Tsuruo. MS-209, a quinoline-type reversal agent, potentiates antitumor efficacy of docetaxel in multidrug-resistant solid tumor xenograft models. Clin Cancer Res. 2002;8(2):582-8.
  6. H. Sakamoto, T. Mashima, A. Kizaki, S. Dan, Y. Hashimoto, M. Naito, T. Tsuruo. Glyoxalase I is involved in resistance of human leukemia cells to antitumor agent-induced apoptosis. Blood. 2000;95(10):3214-8.
  7. T. Mashima, M. Naito, T. Tsuruo. Caspase-mediated cleavage of cytoskeletal actin plays a positive role in the process of morphological apoptosis. Oncogene. 1999;18(15):2423-30.
  8. S. Dan, M. Naito, H. Seimiya, A. Kizaki, T. Mashima, T. Tsuruo. Activation of c-Abl tyrosine kinase requires caspase activation and is not involved in JNK/SAPK activation during apoptosis of human monocytic leukemia U937 cells. Oncogene. 1999;18(6):1277-83.
  9. Z. Chen, H. Seimiya, M. Naito, T. Mashima, A. Kizaki, S. Dan, M. Imaizumi, H. Ichijo, K. Miyazono, T. Tsuruo. ASK1 mediates apoptotic cell death induced by genotoxic stress. Oncogene. 1999;18(1):173-80.
  10. S. Dan, M. Naito, T. Tsuruo. Selective induction of apoptosis in Philadelphia chromosome-positive chronic myelogenous leukemia cells by an inhibitor of BCR - ABL tyrosine kinase, CGP 57148. Cell Death Differ. 1998;5(8):710-5.
  11. T. Watanabe, M. Naito, N. Kokubu, T. Tsuruo. Regression of established tumors expressing P-glycoprotein by combinations of adriamycin, cyclosporin derivatives, and MRK-16 antibodies. J Natl Cancer Inst. 1997;89(7):512-8.
  12. S. Torii, M. Naito, T. Tsuruo. Apoxin I, a novel apoptosis-inducing factor with L-amino acid oxidase activity purified from Western diamondback rattlesnake venom. J Biol Chem. 1997;272(14):9539-42.
  13. M. Naito, K. Shiina, T. Mashima, K. Nagashima, T. Tsuruo. Induction of in vitro nuclear apoptosis activity coincides with the production of 50 kDa cytosolic protein. Cell Death Differ. 1997;4(7):617-22.
  14. M. Naito, K. Nagashima, T. Mashima, T. Tsuruo. Phosphatidylserine externalization is a downstream event of interleukin-1 beta-converting enzyme family protease activation during apoptosis. Blood. 1997;89(6):2060-6.
  15. T. Mashima, M. Naito, K. Noguchi, D. K. Miller, D. W. Nicholson, T. Tsuruo. Actin cleavage by CPP-32/apopain during the development of apoptosis. Oncogene. 1997;14(9):1007-12.
  16. J. Dong, M. Naito, T. Tsuruo. c-Myc plays a role in cellular susceptibility to death receptor-mediated and chemotherapy-induced apoptosis in human monocytic leukemia U937 cells. Oncogene. 1997;15(6):639-47.
  17. K. Noguchi, M. Naito, M. Oshimura, T. Mashima, N. Fujita, S. Yonehara, T. Tsuruo. Chromosome 22 complements apoptosis in Fas-and TNF-resistant mutant UK110 cells. Oncogene. 1996;13(1):39-46.
  18. K. Mikami, M. Naito, A. Tomida, M. Yamada, T. Sirakusa, T. Tsuruo. DT-diaphorase as a critical determinant of sensitivity to mitomycin C in human colon and gastric carcinoma cell lines. Cancer Res. 1996;56(12):2823-6.
  19. T. Ishiguro, M. Nakajima, M. Naito, T. Muto, T. Tsuruo. Identification of genes differentially expressed in B16 murine melanoma sublines with different metastatic potentials. Cancer Res. 1996;56(4):875-9.
  20. Z. Chen, M. Naito, T. Mashima, T. Tsuruo. Activation of actin-cleavable interleukin 1beta-converting enzyme (ICE) family protease CPP-32 during chemotherapeutic agent-induced apoptosis in ovarian carcinoma cells. Cancer Res. 1996;56(22):5224-9.
  21. J. H. Lee, M. Naito, T. Tsuruo. Nonenzymatic reductive activation of 7-N-((2-([2-(gamma-L-glutamylamino)ethyl]dithio)ethyl))mitomycin C by thiol molecules: a novel mitomycin C derivative effective on mitomycin C-resistant tumor cells. Cancer Res. 1994;54(9):2398-403.
  22. M. Naito, H. Tsuge, C. Kuroko, T. Koyama, A. Tomida, T. Tatsuta, Y. Heike, T. Tsuruo. Enhancement of cellular accumulation of cyclosporine by anti-P-glycoprotein monoclonal antibody MRK-16 and synergistic modulation of multidrug resistance. J Natl Cancer Inst. 1993;85(4):311-6.
  23. N. Fujita, S. Kataoka, M. Naito, Y. Heike, N. Boku, M. Nakajima, T. Tsuruo. Suppression of T-lymphoma cell apoptosis by monoclonal antibodies raised against cell surface adhesion molecules. Cancer Res. 1993;53(20):5022-7.
  24. T. Tatsuta, M. Naito, T. Oh-hara, I. Sugawara, T. Tsuruo. Functional involvement of P-glycoprotein in blood-brain barrier. J Biol Chem. 1992;267(28):20383-91.
  25. M. Watanabe, N. Komeshima, M. Naito, T. Isoe, N. Otake, T. Tsuruo. Cellular pharmacology of MX2, a new morpholino anthracycline, in human pleiotropic drug-resistant cells. Cancer Res. 1991;51(1):157-61.
  26. M. Naito, T. Tsuruo. Competitive inhibition by verapamil of ATP-dependent high affinity vincristine binding to the plasma membrane of multidrug-resistant K562 cells without calcium ion involvement. Cancer Res. 1989;49(6):1452-5.
  27. M. Naito, H. Hamada, T. Tsuruo. ATP/Mg2+-dependent binding of vincristine to the plasma membrane of multidrug-resistant K562 cells. J Biol Chem. 1988;263(24):11887-91.