Publications / 研究実績


45. Amesaka H., Hara M., Sakai Y., Shintani A., Sue K., Yamanaka T., Tanaka S.-i., Furukawa Y.

Engineering a monobody specific to monomeric Cu/Zn-superoxide dismutase associated with amyotrophic lateral sclerosis.

Protein Sci. 33, e4961. (2024)

44. Nishi A., Hirata A., Mukaiyama A., Tanaka S.-i., Nomura R., Nakano K., Takano K.

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.

Physchem 4, 120-130. (2024)

43. Ota C., Konishi T., Tanaka S.-i., Takano K.

Induced Circular Dichroism Analysis of Thermally Induced Conformational Changes on Protein Binding Sites Under a Crowding Environment.

ChemPhysChem 25, e202300593. (2024)

42. Nakamura I., Amesaka H., Hara M., Yonezawa K., Okamoto K., Kamikubo H., Tanaka S.-i., Matsuo T.

Conformation state-specific monobodies regulate the functions of flexible proteins through conformation trapping.

Protein Sci. 32, e4813. (2023)

41. Nishi A., Matsui H., Hirata A., Mukaiyama A., Tanaka S.-i., Yoshizawa T., Matsumura H., Nomura R., Nakano K., Takano K.

Structure, Stability and Binding Properties of Collagen-Binding Domains from Streptococcus mutans.

Chemistry 5, 1911-1920. (2023)

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., Matsumura H.

Structures of a FtsZ single protofilament and a double-helical tube in complex with a monobody.

Nature Commun. 14, 4073. (2023)

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., Noguchi N., Saito Y.

An efficient selenium transport pathway of selenoprotein P utilizing a high-affinity ApoER2 receptor variant and being independent of selenocysteine lyase.

J. Biol. Chem. 299, 105009. (2023)

38. Ota C., Suzuki H., Tanaka S.-i., Takano K.

Dispersion Effect of Molecular Crowding on Ligand-Protein Surface Binding Sites of Escherichia coli RNase HI.

Langmuir 38, 14497-14507. (2022)

37. Nishigaki A., Maruyama M., Tanaka S.-i., Yoshikawa H.Y., Imanishi M., Yoshimura M., Mori Y., Takano K.

Metastable Crystallization by Drop Impact.

Crystals 12, 1104-1104. (2022)

36. Kawahara Y., Kurihara N., Ohno T., Watanabe K., Tanaka S.-i., Yamamoto M., Wakizaka H.

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.

J. Fiber Sci. Technol. 78, 114-120. (2022)

35. Tanaka Y., Maruyama M., Okada A., Furukawa Y., Momma K., Sugiura Y., Tajiri R., Sawada K., Tanaka S.-i., Takano K., Taguchi K., Hamamoto S., Ando R., Tsukamoto K., Yoshimura M., Mori Y., Yasui T.

Multicolor imaging of calcium-binding proteins in human kidney stones for elucidating the effects of proteins on crystal growth.

Sci. Rep. 11, 16841. (2021)

34. Kajiura H., Yoshizawa T., Tokumoto Y., Suzuki N., Takeno S., Takeno K.J., Yamashita T., Tanaka S.-i., Kaneko Y., Fujiyama K., Matsumura H., Nakazawa Y.

Structure-function studies of ultrahigh molecular weight isoprenes provide key insights into their biosynthesis.

Commun. Biol. 4, 215. (2021)

33. Fujita J., Sugiyama S., Terakado H., Miyazaki M., Ozawa M., Ueda N., Kuroda N., Tanaka S.-i., Yoshizawa T., Uchihashi T., Matsumura H.

Dynamic Assembly/Disassembly of Staphylococcus aureus FtsZ Visualized by High-Speed Atomic Force Microscopy.

Int. J. Mol. Sci. 22, 1697. (2021)

32. Nishigaki A., Maruyama M., Tanaka S.-i., Yoshikawa H.Y., Imanishi M., Yoshimura M., Mori Y., Takano K..

Growth of Acetaminophen Polymorphic Crystals and Solution-mediated Phase Transition from Trihydrate to Form II in Agarose Gel.

Crystals 11, 1069. (2021)

31. Ota C., Tanaka S.-i., Takano K.

Revisiting the Rate-Limiting Step of the ANS-Protein Binding at the Protein Surface and Inside the Hydrophobic Cavity.

Molecules 26, 420. (2021)

30. Tanaka S.-i., Tsutaki M., Yamamoto S., Mizutani H., Kurahashi R., Hirata A., Takano K.

Exploring mutable conserved sites and fatal non-conserved sites by random mutation of esterase from Sulfolobus tokodaii and subtilisin from Thermococcus kodakarensis.

Int. J. Biol. Macromol. 170, 343-353. (2021)

29. Uehara R., Dan N., Amesaka H., Yoshizawa T., Koga Y., Kanaya S., Takano K., Matsumura H., Tanaka S.-i.

Insertion loop-mediated folding propagation governs efficient maturation of hyperthermophilic Tk-subtilisin at high temperatures.

FEBS Letters. 595, 452-461. (2021)

28. Ota C., Fukuda Y., Tanaka, S.-i., Takano K.

Spectroscopic Evidence of the Salt-Induced Conformational Change around the Localized Electric Charges on the Protein Surface of Fibronectin Type III.

Langmuir 36, 14243-14254. (2020)

27. Nishigaki A., Maruyama M., Numata M., Kanzaki C., Tanaka S.-i., Yoshikawa H.Y., Imanishi M., Yoshimura M., Mori Y., Takano K.

Microflow system promotes acetaminophen crystal nucleation.

Eng. Life Sci. 20, 395-401. (2020)

26. Kurahashi R., Tanaka S.-i., Takano K.

Highly active enzymes produced by directed evolution with stability-based selection.

Enzyme Microb. Technol. 140, 109626. (2020)

25. Matsumura H., Shiomi K., Yamamoto A., Taketani Y., Kobayashi N., Yoshizawa T., Tanaka S.-i., Yoshikawa H., Endo M., Fukayama H.

Hybrid Rubisco with Complete Replacement of Rice Rubisco Small Subunits by Sorghum Counterparts Confers C4 Plant-like High Catalytic Activity.

Mol. Plant. 13, 1570-1581. (2020)

24. Uehara R., Iwamoto R., Aoki S., Yoshizawa T., Takano K., Matsumura H., Tanaka S.-i.

Crystal structure of a GH1 β-glucosidase from Hamamotoa singularis.

Protein Sci. 29, 2000-2008. (2020)

23. Yoshizawa T., Fujita J., Terakado H., Ozawa M., Kuroda N., Tanaka S.-i., Uehara R., Matsumura H.

Crystal structures of the cell-division protein FtsZ from Klebsiella pneumoniae and Escherichia coli.

Acta Crystallogr. F Struct. Biol. Commun. 76, 86-93. (2020)

22. Ota C., Suzuki H., Tanaka S.-i., Takano K.

Spectroscopic Signature of the Steric Strains in an Escherichia coli RNase HI Cavity-Filling Destabilized Mutant Protein.

J. Phys. Chem. B. 124, 91-100. (2020)

21. Kurahashi R., Tanaka S.-i., Takano K.

Activity-stability trade-off in random mutant proteins.

J. Biosci. Bioeng. 128, 405-409. (2019)

20. Tanaka S.-i., Takahashi T., Koide A., Iwamoto R., Koikeda S., Koide S.

Monobody-mediated alteration of lipase substrate specificity.

ACS Chem. Biol. 13, 1487-1492. (2018)

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

Structural basis for the Serratia marcescens lipase secretion system: Crystal structures of the membrane fusion protein and nucleotide-binding domain.

Biochemistry 56, 6281-6291. (2017) 

18. Tanaka S.-i., Takahashi T., Koide A., Ishihara S., Koikeda S., Koide S.

Monobody-mediated alteration of enzyme specificity.

Nature Chem. Biol. 11, 762-764. (2015) 

17. Mitsuya D., Tanaka S.-i., Matsumura H., Urano N., Takano K., Ogasahara K., Takehira M., Yutani K., Ishida, M.

Strategy for cold adaptation of the tryptophan synthase α subunit from the psychrophile Shewanella frigidimarina K14-2: crystal structure and physicochemical properties.

J. Biochem. 155, 73-82. (2014)

16. Koga Y., Tanaka S.-i., Sakudo A., Tobiume M., Aranishi M., Hirata A., Takano K., Ikuta K., Kanaya S.

Proteolysis of abnormal prion protein with a thermostable protease from Thermococcus kodakarensis KOD1.

Appl. Microbiol. Biotechnol. 98, 2113-2120. (2014)

15. Uehara R., Tanaka S.-i., Takano K., Koga Y., Kanaya, S.

Requirement of insertion sequence IS1 for thermal adaptation of Pro-Tk-subtilisin from hyperthermophilic archaeon.

Extremophiles 16, 841-851. (2012)

14. Uehara R., Takeuchi Y., Tanaka S.-i., Takano K., Koga Y., Kanaya S.

Requirement of Ca2+ ions for the hyperthermostability of Tk-subtilisin from Thermococcus kodakarensis.

Biochemistry 51, 5369-5378. (2012)

13. Takano K., Okamoto T., Okada J., Tanaka S.-i., Angkawidjaja C., Koga Y., Kanaya S.

Stabilization by fusion to the C-terminus of hyperthermophile Sulfolobus tokodaii RNase HI: a possibility of protein stabilization tag.

PLoS One 6, e16226. (2011)

12. Sato A., Yokotani S., Tadokoro T., Tanaka S.-i., Angkawidjaja C., Koga Y., Takano K., Kanaya S.

Crystal structure of stable protein CutA1 from psychrotrophic bacterium Shewanella sp. SIB1.

J. Synchrotron Radiat. 18, 6-10. (2011)

11. Tanaka S.-i., Koga Y., Takano K., Kanaya S.

Inhibition of chymotrypsin- and subtilisin-like serine proteases with Tk-serpin from hyperthermophilic archaeon Thermococcus kodakarensis.

Biochim. Biophys. Acta. 1814, 299-307. (2011)

10. Foophow T., Tanaka S.-i., Koga Y., Takano K., Kanaya S.

Subtilisin-like Serine Protease from Hyperthermophilic Archaeon Thermococcus kodakaraensis with N- and C-terminal Propeptides.

Protein Eng. Des. Sel. 23, 347-355. (2010)

9. Foophow T., Tanaka S.-i., Angkawidjaja C., Koga Y., Takano K., Kanaya S.

Crystal structure of a subtilisin homologue, Tk-SP, from Thermococcus kodakaraensis: requirement of a C-terminal beta-jelly roll domain for hyperstability.

J. Mol. Biol. 400, 865-877. (2010)

8. Takeuchi Y., Tanaka S.-i., Matsumura H., Koga Y., Takano K., Kanaya, S.

Requirement of a unique Ca2+-binding loop for folding of Tk-subtilisin from a hyperthermophilic archaeon.

Biochemistry 48, 10637-10643. (2009)

7. Tanaka S.-i., Matsumura H., Koga Y., Takano K., Kanaya, S.

Identification of the interactions critical for propeptide-catalyzed folding of Tk-subtilisin.

J. Mol. Biol. 394, 306-319. (2009)

6. Tanaka S.-i., Takeuchi Y., Matsumura H., Koga Y., Takano K., Kanaya S.

Crystal structure of Tk-subtilisin folded without propeptide: Requirement of propeptide for acceleration of folding. 

FEBS Letters 582, 3875-3878. (2008)

5. Pulido M., Tanaka S.-i., Sringiew C., You D.-J., Matsumura H., Koga Y., Takano K., Kanaya S.

Requirement of left-handed glycine residue for high stability of the Tk-subtilisin propeptide as revealed by mutational and crystallographic analyses.

J. Mol. Biol. 374, 1359-1373. (2007)

4. Tanaka S.-i., Matsumura H., Koga Y., Takano K., Kanaya S.

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

J. Mol. Biol. 372, 1055-1069. (2007)

3. Tanaka S.-i., Saito K., Chon H., Matsumura H., Koga Y., Takano K., Kanaya S.

Crystal structure of unautoprocessed precursor of subtilisin from a hyperthermophilic archaeon: evidence for Ca2+-induced folding. 

J. Biol. Chem. 282, 8246-8255. (2007) 

2. Tanaka S.-i., Saito K., Chon H., Matsumura H., Koga Y., Takano K., Kanaya S.

Crystallization and preliminary X-ray diffraction study of active-site mutant of pro-Tk-subtilisin from a hyperthermophilic archaeon. 

Acta Cryst. F 62, 901-905. (2006)

1. Pulido M., Saito K., Tanaka S.-i., Koga Y., Morikawa M., Takano K., Kanaya, S.

Ca2+-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. 

Appl. Environ. Microbiol. 72, 4154-4162. (2006)


2. Uehara R., Amesaka H., Koga Y., Takano K., Kanaya S., Tanaka S.-i.

Hyperthermophilic subtilisin-like proteases from Thermococcus Kodakarensis. Biotechnology of Microbial Enzymes: Production, Biocatalysis and Industrial Applications (Second Edition). 

Academic Press pp.89-127. (2023)

1. Tanaka S.-i., Uehara R., Kanaya S.

Maturation and Stabilization Mechanisms of Two Hyperthermostable Subtilisin-Like Serine Proteases from Thermococcus Kodakarensis. Serine Proteases: Mechanism, Structure and Evolution. 

NOVA Publishers pp.1-32. (2012)


4. 石川 英司、田中 俊一

ガラクトオリゴ糖の製造に有用な担子菌酵母のβ-グリコシダーゼ : 遺伝子クローニングと立体構造解析から明らかになった特徴について

『化学と生物(日本農芸化学会誌)』61, 274-280. (2023)

3. 上原 了、田中 俊一


『化学と生物(日本農芸化学会誌)』59, 272-274. (2021)

2. 田中 俊一


『バイオミディア(日本生物工学会誌)』97, 137. (2019)

1. 田中 俊一、小出 昌平

モノボディを介した酵素機能の改変 -酵素工学の新たなアプローチ-

『化学と生物(日本農芸化学会誌)』55, 303-305. (2017)