{"id":178,"date":"2021-09-03T18:30:08","date_gmt":"2021-09-03T09:30:08","guid":{"rendered":"https:\/\/stanaka1.com\/?page_id=178"},"modified":"2025-03-13T15:18:55","modified_gmt":"2025-03-13T06:18:55","slug":"%e7%a0%94%e7%a9%b6%e5%ae%9f%e7%b8%be","status":"publish","type":"page","link":"https:\/\/stanaka1.com\/?page_id=178","title":{"rendered":"Publications \/ \u7814\u7a76\u5b9f\u7e3e"},"content":{"rendered":"\n

<\/p>\n\n\n\n

\u539f\u8457\u8ad6\u6587<\/strong><\/p>\n\n\n\n

48. Amesaka H., Tachibana M., Hara M., Toya S., Nakagawa H., Matsumura H., Hirata A., Fujihashi M., Takano K., Tanaka S.-i.<\/strong><\/p>\n\n\n\n

Heat-sterilizable antibody mimics designed on the cold shock protein scaffold from hyperthermophile Thermotoga maritima<\/em>.<\/p>\n\n\n\n

Protein Sci.<\/em> 34, e70018. (2025)<\/p>\n\n\n\n

47. Takano A., Yano M., Nakamura T., Takano K., Tanaka S.-i.<\/strong><\/p>\n\n\n\n

Secretory expression in Bacillus subtilis<\/em>, purification, and characterization of a persistent protein-degrading enzyme from Nocardiopsis<\/em> sp. TOA-1.<\/p>\n\n\n\n

Biosci. Biotechnol. Biochem.<\/em> 89, 413-416. (2025)<\/p>\n\n\n\n

46. Wakisaka M., Tanaka S.-i.<\/strong>, Takano K.<\/p>\n\n\n\n

Utilization of low-stability variants in protein evolutionary engineering.<\/p>\n\n\n\n

Int. J. Biol. Macromol.<\/em> 272, e132946. (2024)<\/p>\n\n\n\n

45. Amesaka H., Hara M., Sakai Y., Shintani A., Sue K., Yamanaka T., Tanaka S.-i.<\/strong>, Furukawa Y.<\/p>\n\n\n\n

Engineering a monobody specific to monomeric Cu\/Zn-superoxide dismutase associated with amyotrophic lateral sclerosis.<\/p>\n\n\n\n

Protein Sci.<\/em> 33, e4961. (2024)<\/p>\n\n\n\n

44. Nishi A., Hirata A., Mukaiyama A., Tanaka S.-i.<\/strong>, Nomura R., Nakano K., Takano K.<\/p>\n\n\n\n

Role of N1-Domain, Linker, N2-Domain, and Latch in the Binding Activity and Stability of the Collagen-Binding Domain for the Collagen-Binding Protein Cbm from Streptococcus mutans<\/em>.<\/p>\n\n\n\n

Physchem<\/em> 4, 120-130. (2024)<\/p>\n\n\n\n

43. Ota C., Konishi T., Tanaka S.-i.<\/strong>, Takano K.<\/p>\n\n\n\n

Induced Circular Dichroism Analysis of Thermally Induced Conformational Changes on Protein Binding Sites Under a Crowding Environment.<\/p>\n\n\n\n

ChemPhysChem<\/em> 25, e202300593. (2024)<\/p>\n\n\n\n

42. Nakamura I., Amesaka H., Hara M., Yonezawa K., Okamoto K., Kamikubo H., Tanaka S.-i.<\/strong>, Matsuo T.<\/p>\n\n\n\n

Conformation state-specific monobodies regulate the functions of flexible proteins through conformation trapping.<\/p>\n\n\n\n

Protein Sci.<\/em> 32, e4813. (2023)<\/p>\n\n\n\n

41. Nishi A., Matsui H., Hirata A., Mukaiyama A., Tanaka S.-i.<\/strong>, Yoshizawa T., Matsumura H., Nomura R., Nakano K., Takano K.<\/p>\n\n\n\n

Structure, Stability and Binding Properties of Collagen-Binding Domains from Streptococcus mutans<\/em>.<\/p>\n\n\n\n

Chemistry<\/em> 5, 1911-1920. (2023)<\/p>\n\n\n\n

40. Fujita J., Amesaka H., Yoshizawa T., Hibino K., Kamimura N., Kuroda N., Konishi T., Kato Y., Hara M., Inoue T., Namba K., Tanaka S.-i.<\/strong>, Matsumura H.<\/p>\n\n\n\n

Structures of a FtsZ single protofilament and a double-helical tube in complex with a monobody.<\/p>\n\n\n\n

Nature Commun.<\/em> 14, 4073. (2023)<\/p>\n\n\n\n

39. Mizuno A., Toyama T., Ichikawa A., Sakai N., Yoshioka Y., Nishito Y., Toga R., Amesaka H., Kaneko T., Arisawa K., Tsutsumi R., Mita Y., Tanaka S.-i.<\/strong>, Noguchi N., Saito Y.<\/p>\n\n\n\n

An efficient selenium transport pathway of selenoprotein P utilizing a high-affinity ApoER2 receptor variant and being independent of selenocysteine lyase.<\/p>\n\n\n\n

J. Biol. Chem.<\/em> 299, 105009. (2023)<\/p>\n\n\n\n

38. Ota C., Suzuki H., Tanaka S.-i.<\/strong>, Takano K.<\/p>\n\n\n\n

Dispersion Effect of Molecular Crowding on Ligand-Protein Surface Binding Sites of Escherichia coli<\/em> RNase HI.<\/p>\n\n\n\n

Langmuir <\/em>38, 14497-14507. (2022)<\/p>\n\n\n\n

37. Nishigaki A., Maruyama M., Tanaka S.-i.<\/strong>, Yoshikawa H.Y., Imanishi M., Yoshimura M., Mori Y., Takano K.<\/p>\n\n\n\n

Metastable Crystallization by Drop Impact.<\/p>\n\n\n\n

Crystals<\/em> 12, 1104-1104. (2022)<\/p>\n\n\n\n

36. Kawahara Y., Kurihara N., Ohno T., Watanabe K., Tanaka S.-i.<\/strong>, Yamamoto M., Wakizaka H.<\/p>\n\n\n\n

Changes in the physical properties of the feather keratin resin by the enzymatic pre-treatment of the feathers or the slight reinforcement with the wood fibers.<\/p>\n\n\n\n

J. Fiber Sci. Technol.<\/em> 78, 114-120. (2022)<\/p>\n\n\n\n

35. Tanaka Y., Maruyama M., Okada A., Furukawa Y., Momma K., Sugiura Y., Tajiri R., Sawada K., <\/em>Tanaka S.-i.<\/strong>, Takano K., Taguchi K., Hamamoto S., Ando R., Tsukamoto K., Yoshimura M., Mori Y., Yasui T.<\/p>\n\n\n\n

Multicolor imaging of calcium-binding proteins in human kidney stones for elucidating the effects of proteins on crystal growth.<\/p>\n\n\n\n

Sci. Rep.<\/em> 11, 16841. (2021)<\/p>\n\n\n\n

34. Kajiura H., Yoshizawa T., Tokumoto Y., Suzuki N., Takeno S., Takeno K.J., Yamashita T., Tanaka S.-i.<\/strong>, Kaneko Y., Fujiyama K., Matsumura H., Nakazawa Y.<\/p>\n\n\n\n

Structure-function studies of ultrahigh molecular weight isoprenes provide key insights into their biosynthesis.<\/p>\n\n\n\n

Commun. Biol.<\/em> 4, 215. (2021)<\/p>\n\n\n\n

33. Fujita J., Sugiyama S., Terakado H., Miyazaki M., Ozawa M., Ueda N., Kuroda N., Tanaka S.-i.,<\/strong> Yoshizawa T., Uchihashi T., Matsumura H.<\/p>\n\n\n\n

Dynamic Assembly\/Disassembly of Staphylococcus aureus<\/em> FtsZ Visualized by High-Speed Atomic Force Microscopy.<\/p>\n\n\n\n

Int. J. Mol. Sci.<\/em> 22, 1697. (2021)<\/p>\n\n\n\n

32. Nishigaki A., Maruyama M., <\/em>Tanaka S.-i.,<\/strong> Yoshikawa H.Y., Imanishi M., Yoshimura M., Mori Y., Takano K..<\/p>\n\n\n\n

Growth of Acetaminophen Polymorphic Crystals and Solution-mediated Phase Transition from Trihydrate to Form II in Agarose Gel.<\/p>\n\n\n\n

Crystals<\/em> 11, 1069. (2021)<\/p>\n\n\n\n

31. Ota C., Tanaka S.-i.<\/strong>,<\/em> Takano K.<\/p>\n\n\n\n

Revisiting the Rate-Limiting Step of the ANS-Protein Binding at the Protein Surface and Inside the Hydrophobic Cavity.<\/p>\n\n\n\n

Molecules<\/em> 26, 420. (2021)<\/p>\n\n\n\n

30. Tanaka S.-i.<\/strong>, Tsutaki M., Yamamoto S., Mizutani H., Kurahashi R., Hirata A., Takano K.<\/p>\n\n\n\n

Exploring mutable conserved sites and fatal non-conserved sites by random mutation of esterase from Sulfolobus tokodaii<\/em> and subtilisin from Thermococcus kodakarensis<\/em>.<\/p>\n\n\n\n

Int. J. Biol. Macromol.<\/em> 170, 343-353. (2021)<\/p>\n\n\n\n

29. Uehara R., Dan N., Amesaka H., Yoshizawa T., Koga Y., Kanaya S., Takano K., Matsumura H., Tanaka S.-i.<\/em><\/strong><\/p>\n\n\n\n

Insertion loop-mediated folding propagation governs efficient maturation of hyperthermophilic Tk-subtilisin at high temperatures.<\/p>\n\n\n\n

FEBS Letters.<\/em> 595, 452-461. (2021)<\/p>\n\n\n\n

28. Ota C., Fukuda Y., Tanaka, S.-i.<\/strong>, Takano K.<\/p>\n\n\n\n

Spectroscopic Evidence of the Salt-Induced Conformational Change around the Localized Electric Charges on the Protein Surface of Fibronectin Type III.<\/p>\n\n\n\n

Langmuir <\/em>36, 14243-14254. (2020)<\/p>\n\n\n\n

27. Nishigaki A., Maruyama M., Numata M., Kanzaki C., Tanaka S.-i.<\/strong>, Yoshikawa H.Y., Imanishi M., Yoshimura M., Mori Y., Takano K.<\/p>\n\n\n\n

Microflow system promotes acetaminophen crystal nucleation.<\/p>\n\n\n\n

Eng. Life Sci.<\/em> 20, 395-401. (2020)<\/p>\n\n\n\n

26. Kurahashi R., Tanaka S.-i.<\/strong>, Takano K.<\/p>\n\n\n\n

Highly active enzymes produced by directed evolution with stability-based selection.<\/p>\n\n\n\n

Enzyme Microb. Technol.<\/em> 140, 109626. (2020)<\/p>\n\n\n\n

25. Matsumura H., Shiomi K., Yamamoto A., Taketani Y., Kobayashi N., Yoshizawa T., Tanaka S.-i.<\/strong>, Yoshikawa H., Endo M., Fukayama H.<\/p>\n\n\n\n

Hybrid Rubisco with Complete Replacement of Rice Rubisco Small Subunits by Sorghum Counterparts Confers C4 Plant-like High Catalytic Activity.<\/p>\n\n\n\n

Mol. Plant.<\/em> 13, 1570-1581. (2020)<\/p>\n\n\n\n

24. Uehara R., Iwamoto R., Aoki S., Yoshizawa T., Takano K., Matsumura H., Tanaka S.-i.<\/strong><\/p>\n\n\n\n

Crystal structure of a GH1 \u03b2-glucosidase from Hamamotoa singularis<\/em>.<\/p>\n\n\n\n

Protein Sci.<\/em> 29, 2000-2008. (2020)<\/p>\n\n\n\n

23. Yoshizawa T., Fujita J., Terakado H., Ozawa M., Kuroda N., Tanaka S.-i.<\/strong>, Uehara R., Matsumura H.<\/p>\n\n\n\n

Crystal structures of the cell-division protein FtsZ from Klebsiella pneumoniae<\/em> and Escherichia coli<\/em>.<\/p>\n\n\n\n

Acta Crystallogr. F Struct. Biol. Commun.<\/em> 76, 86-93. (2020)<\/p>\n\n\n\n

22. Ota C., Suzuki H., Tanaka S.-i.<\/strong>, Takano K.<\/p>\n\n\n\n

Spectroscopic Signature of the Steric Strains in an Escherichia coli<\/em> RNase HI Cavity-Filling Destabilized Mutant Protein.<\/p>\n\n\n\n

J. Phys. Chem. B.<\/em> 124, 91-100. (2020)<\/p>\n\n\n\n

21. Kurahashi R., Tanaka S.-i.<\/strong>, Takano K.<\/p>\n\n\n\n

Activity-stability trade-off in random mutant proteins.<\/p>\n\n\n\n

J. Biosci. Bioeng.<\/em> 128, 405-409. (2019)<\/p>\n\n\n\n

20. Tanaka S.-i.<\/strong>, Takahashi T., Koide A., Iwamoto R., Koikeda S., Koide S.<\/p>\n\n\n\n

Monobody-mediated alteration of lipase substrate specificity.<\/p>\n\n\n\n

ACS Chem. Biol.<\/em> 13, 1487-1492. (2018)<\/p>\n\n\n\n

19. Murata D., Okano H., Angkawidjaja C., Akutsu M., Tanaka S.-i.<\/strong>, Kitahara K., Yoshizawa T., Matsumura H., Kado Y., Mizohata E., Inoue T., Sano S., Koga Y., Kanaya S., Takano K.<\/p>\n\n\n\n

Structural basis for the Serratia marcescens<\/em> lipase secretion system: Crystal structures of the membrane fusion protein and nucleotide-binding domain.<\/p>\n\n\n\n

Biochemistry<\/em> 56, 6281-6291. (2017) <\/p>\n\n\n\n

18. Tanaka S.-i.<\/strong>, Takahashi T., Koide A., Ishihara S., Koikeda S., Koide S.<\/p>\n\n\n\n

Monobody-mediated alteration of enzyme specificity.<\/p>\n\n\n\n

Nature Chem. Biol.<\/em> 11, 762-764. (2015) <\/p>\n\n\n\n

17. Mitsuya D., Tanaka S.-i.<\/strong>, Matsumura H., Urano N., Takano K., Ogasahara K., Takehira M., Yutani K., Ishida, M.<\/p>\n\n\n\n

Strategy for cold adaptation of the tryptophan synthase \u03b1 subunit from the psychrophile Shewanella frigidimarina<\/em> K14-2: crystal structure and physicochemical properties.<\/p>\n\n\n\n

J. Biochem.<\/em> 155, 73-82. (2014)<\/p>\n\n\n\n

16. Koga Y., Tanaka S.-i.<\/strong>, Sakudo A., Tobiume M., Aranishi M., Hirata A., Takano K., Ikuta K., Kanaya S.<\/p>\n\n\n\n

Proteolysis of abnormal prion protein with a thermostable protease from Thermococcus kodakarensis<\/em> KOD1.<\/p>\n\n\n\n

Appl. Microbiol. Biotechnol.<\/em> 98, 2113-2120. (2014)<\/p>\n\n\n\n

15. Uehara R., Tanaka S.-i.<\/strong>, <\/em>Takano K., Koga Y., Kanaya, S.<\/p>\n\n\n\n

Requirement of insertion sequence IS1 for thermal adaptation of Pro-Tk-subtilisin from hyperthermophilic archaeon.<\/p>\n\n\n\n

Extremophiles<\/em> 16, 841-851. (2012)<\/p>\n\n\n\n

14. Uehara R., Takeuchi Y., Tanaka S.-i.<\/strong>, <\/em>Takano K., Koga Y., Kanaya S.<\/p>\n\n\n\n

Requirement of Ca2+<\/sup> ions for the hyperthermostability of Tk-subtilisin from Thermococcus kodakarensis<\/em>.<\/p>\n\n\n\n

Biochemistry<\/em> 51, 5369-5378. (2012)<\/p>\n\n\n\n

13. Takano K., Okamoto T., Okada J., Tanaka S.-i.<\/strong>, Angkawidjaja C., Koga Y., Kanaya S.<\/p>\n\n\n\n

Stabilization by fusion to the C-terminus of hyperthermophile Sulfolobus tokodaii<\/em> RNase HI: a possibility of protein stabilization tag.<\/p>\n\n\n\n

PLoS One<\/em> 6, e16226. (2011)<\/p>\n\n\n\n

12. Sato A., Yokotani S., Tadokoro T., Tanaka S.-i.<\/strong>, Angkawidjaja C., Koga Y., Takano K., Kanaya S.<\/p>\n\n\n\n

Crystal structure of stable protein CutA1 from psychrotrophic bacterium Shewanella<\/em> sp. SIB1.<\/p>\n\n\n\n

J. Synchrotron Radiat.<\/em> 18, 6-10. (2011)<\/p>\n\n\n\n

11. Tanaka S.-i.<\/strong>, Koga Y., Takano K., Kanaya S.<\/p>\n\n\n\n

Inhibition of chymotrypsin- and subtilisin-like serine proteases with Tk-serpin from hyperthermophilic archaeon Thermococcus kodakarensis<\/em>.<\/p>\n\n\n\n

Biochim. Biophys. Acta<\/em>. 1814, 299-307. (2011)<\/p>\n\n\n\n

10. Foophow T., Tanaka S.-i.<\/strong>, Koga Y., Takano K., Kanaya S.<\/p>\n\n\n\n

Subtilisin-like Serine Protease from Hyperthermophilic Archaeon Thermococcus kodakaraensis<\/em> with N- and C-terminal Propeptides.<\/p>\n\n\n\n

Protein Eng. Des. Sel.<\/em> 23, 347-355. (2010)<\/p>\n\n\n\n

9. Foophow T., Tanaka S.-i.<\/strong>, Angkawidjaja C., Koga Y., Takano K., Kanaya S.<\/p>\n\n\n\n

Crystal structure of a subtilisin homologue, Tk-SP, from Thermococcus kodakaraensis<\/em>: requirement of a C-terminal beta-jelly roll domain for hyperstability.<\/p>\n\n\n\n

J. Mol. Biol.<\/em> 400, 865-877. (2010)<\/p>\n\n\n\n

8. Takeuchi Y., Tanaka S.-i.<\/strong>, Matsumura H., Koga Y., Takano K., Kanaya, S.<\/p>\n\n\n\n

Requirement of a unique Ca2+<\/sup>-binding loop for folding of Tk-subtilisin from a hyperthermophilic archaeon.<\/p>\n\n\n\n

Biochemistry<\/em> 48, 10637-10643. (2009)<\/p>\n\n\n\n

7. Tanaka S.-i.<\/strong>, Matsumura H., Koga Y., Takano K., Kanaya, S.<\/p>\n\n\n\n

Identification of the interactions critical for propeptide-catalyzed folding of Tk-subtilisin.<\/p>\n\n\n\n

J. Mol. Biol.<\/em> 394, 306-319. (2009)<\/p>\n\n\n\n

6. Tanaka S.-i.<\/strong>, Takeuchi Y., Matsumura H., Koga Y., Takano K., Kanaya S.<\/p>\n\n\n\n

Crystal structure of Tk-subtilisin folded without propeptide: Requirement of propeptide for acceleration of folding. <\/p>\n\n\n\n

FEBS Letters<\/em> 582, 3875-3878. (2008)<\/p>\n\n\n\n

5. Pulido M., Tanaka S.-i.<\/strong>, Sringiew C., You D.-J., Matsumura H., Koga Y., Takano K., Kanaya S.<\/p>\n\n\n\n

Requirement of left-handed glycine residue for high stability of the Tk-subtilisin propeptide as revealed by mutational and crystallographic analyses.<\/p>\n\n\n\n

J. Mol. Biol.<\/em> 374, 1359-1373. (2007)<\/p>\n\n\n\n

4. Tanaka S.-i.<\/strong>, Matsumura H., Koga Y., Takano K., Kanaya S.<\/p>\n\n\n\n

Four new crystal structures of Tk-subtilisin in unautoprocessed, autoprocessed and mature forms: insight into structural changes during maturation process. <\/p>\n\n\n\n

J. Mol. Biol.<\/em> 372, 1055-1069. (2007)<\/p>\n\n\n\n

3. Tanaka S.-i.<\/strong>, Saito K., Chon H., Matsumura H., Koga Y., Takano K., Kanaya S.<\/p>\n\n\n\n

Crystal structure of unautoprocessed precursor of subtilisin from a hyperthermophilic archaeon: evidence for Ca2+<\/sup>-induced folding. <\/p>\n\n\n\n

J. Biol. Chem.<\/em> 282, 8246-8255. (2007) <\/p>\n\n\n\n

2. Tanaka S.-i.<\/strong>, Saito K., Chon H., Matsumura H., Koga Y., Takano K., Kanaya S.<\/p>\n\n\n\n

Crystallization and preliminary X-ray diffraction study of active-site mutant of pro-Tk-subtilisin from a hyperthermophilic archaeon. <\/p>\n\n\n\n

Acta Cryst. F<\/em> 62, 901-905. (2006)<\/p>\n\n\n\n

1. Pulido M., Saito K., Tanaka S.-i.<\/strong>, Koga Y., Morikawa M., Takano K., Kanaya, S.<\/p>\n\n\n\n

Ca2+<\/sup>-Dependent Maturation of Tk-subtilisin from a Hyperthermophilic Archaeon: Propeptide is a Potent Inhibitor of the Mature Domain but is not Required for Its Folding. <\/p>\n\n\n\n

Appl. Environ. Microbiol.<\/em> 72, 4154-4162. (2006)<\/p>\n\n\n\n

\u7dcf\u8aac<\/u><\/strong><\/p>\n\n\n\n

2. Uehara R., Amesaka H., Koga Y., Takano K., Kanaya S., Tanaka S.-i.<\/strong><\/p>\n\n\n\n

Hyperthermophilic subtilisin-like proteases from Thermococcus Kodakarensis<\/em>. Biotechnology of Microbial Enzymes: Production, Biocatalysis and Industrial Applications (Second Edition). <\/p>\n\n\n\n

Academic Press<\/em> pp.89-127. (2023)<\/p>\n\n\n\n

1. Tanaka S.-i.<\/strong>, Uehara R., Kanaya S.<\/p>\n\n\n\n

Maturation and Stabilization Mechanisms of Two Hyperthermostable Subtilisin-Like Serine Proteases from Thermococcus Kodakarensis<\/em>. Serine Proteases: Mechanism, Structure and Evolution. <\/p>\n\n\n\n

NOVA Publishers<\/em> pp.1-32. (2012)<\/p>\n\n\n\n

\u8457\u66f8<\/strong><\/p>\n\n\n\n

4. \u77f3\u5ddd \u82f1\u53f8\u3001\u7530\u4e2d \u4fca\u4e00<\/strong><\/p>\n\n\n\n

\u30ac\u30e9\u30af\u30c8\u30aa\u30ea\u30b4\u7cd6\u306e\u88fd\u9020\u306b\u6709\u7528\u306a\u62c5\u5b50\u83cc\u9175\u6bcd\u306e\u03b2-\u30b0\u30ea\u30b3\u30b7\u30c0\u30fc\u30bc : \u907a\u4f1d\u5b50\u30af\u30ed\u30fc\u30cb\u30f3\u30b0\u3068\u7acb\u4f53\u69cb\u9020\u89e3\u6790\u304b\u3089\u660e\u3089\u304b\u306b\u306a\u3063\u305f\u7279\u5fb4\u306b\u3064\u3044\u3066<\/p>\n\n\n\n

\u300e\u5316\u5b66\u3068\u751f\u7269\uff08\u65e5\u672c\u8fb2\u82b8\u5316\u5b66\u4f1a\u8a8c\uff09\u300f61, 274-280. (2023)<\/p>\n\n\n\n

3. \u4e0a\u539f \u4e86\u3001\u7530\u4e2d \u4fca\u4e00<\/strong><\/p>\n\n\n\n

\u8d85\u597d\u71b1\u6027\u30b5\u30c1\u30e9\u30a4\u30b7\u30f3\u3092\u30e2\u30c7\u30eb\u306b\u307f\u308b\u30bf\u30f3\u30d1\u30af\u8cea\u30d5\u30a9\u30fc\u30eb\u30c7\u30a3\u30f3\u30b0\u306e\u9ad8\u6e29\u74b0\u5883\u9069\u5fdc\u6226\u7565\uff5eTk-subtilisin\u30683\u3064\u306e\u633f\u5165\u914d\u5217\uff5e<\/p>\n\n\n\n

\u300e\u5316\u5b66\u3068\u751f\u7269\uff08\u65e5\u672c\u8fb2\u82b8\u5316\u5b66\u4f1a\u8a8c\uff09\u300f59, 272-274. (2021)<\/p>\n\n\n\n

2. \u7530\u4e2d \u4fca\u4e00<\/strong><\/p>\n\n\n\n

\u9175\u7d20\u3082\u300e\u30a2\u30af\u30bb\u300f\u3067\u30aa\u30b7\u30e3\u30ec\u304c\u3057\u305f\u3044\uff1f<\/p>\n\n\n\n

\u300e\u30d0\u30a4\u30aa\u30df\u30c7\u30a3\u30a2\uff08\u65e5\u672c\u751f\u7269\u5de5\u5b66\u4f1a\u8a8c\uff09\u300f97, 137. (2019)<\/p>\n\n\n\n

1. \u7530\u4e2d \u4fca\u4e00<\/strong>\u3001\u5c0f\u51fa \u660c\u5e73<\/p>\n\n\n\n

\u30e2\u30ce\u30dc\u30c7\u30a3\u3092\u4ecb\u3057\u305f\u9175\u7d20\u6a5f\u80fd\u306e\u6539\u5909 -\u9175\u7d20\u5de5\u5b66\u306e\u65b0\u305f\u306a\u30a2\u30d7\u30ed\u30fc\u30c1-<\/p>\n\n\n\n

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\u539f\u8457\u8ad6\u6587 48. Amesaka H., Tachibana M., Hara M., Toya S., Nakagawa H., Matsumura H., Hirata A., Fujihashi M., Takan […]<\/p>\n","protected":false},"author":1,"featured_media":0,"parent":0,"menu_order":0,"comment_status":"closed","ping_status":"closed","template":"page-templates\/page-nosidebars.php","meta":{"footnotes":""},"class_list":["post-178","page","type-page","status-publish","hentry"],"_links":{"self":[{"href":"https:\/\/stanaka1.com\/index.php?rest_route=\/wp\/v2\/pages\/178","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/stanaka1.com\/index.php?rest_route=\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/stanaka1.com\/index.php?rest_route=\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/stanaka1.com\/index.php?rest_route=\/wp\/v2\/users\/1"}],"replies":[{"embeddable":true,"href":"https:\/\/stanaka1.com\/index.php?rest_route=%2Fwp%2Fv2%2Fcomments&post=178"}],"version-history":[{"count":54,"href":"https:\/\/stanaka1.com\/index.php?rest_route=\/wp\/v2\/pages\/178\/revisions"}],"predecessor-version":[{"id":1274,"href":"https:\/\/stanaka1.com\/index.php?rest_route=\/wp\/v2\/pages\/178\/revisions\/1274"}],"wp:attachment":[{"href":"https:\/\/stanaka1.com\/index.php?rest_route=%2Fwp%2Fv2%2Fmedia&parent=178"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}