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（ *:corresponding author）

2021
114. Miwa T, *Taguchi, H.
Novel self-regulation strategy of a small heat shock protein for prodigious and rapid expression on demand (review).
Current Genetics 2020 (2021) in press

113. Deschoenmaeker F, Mihara S, Niwa T, Taguchi H, Wakabayashi KI, Toyoshima M, Shimizu H, *Hisabori T.
Thioredoxin pathway in Anabaena sp. PCC 7120: activity of NADPH-thioredoxin reductase C.
J Biochem (2021) in press

112. Luu Trinh MD, Miyazaki D, Ono S, Nomata J, Kono M, Mino H, Niwa T, Okegawa Y, Motohashi K, Taguchi H, Hisabori T, *Masuda S
The evolutionary conserved iron-sulfur protein TCR controls P700 oxidation in photosystem I.
iScience 2021 Jan 13;24(2):102059. doi: 10.1016/j.isci.2021.102059.

2020
111. Miwa T, Chadani Y, *Taguchi, H.
Escherichia coli small heat shock protein IbpA is an aggregation-sensor that self-regulates its own expression at post-transcriptional levels.
Mol Microbiol 2020 Sep 21. doi: 10.1111/mmi.14606

110. Tatsuki Masuzawa *Shinichi Sato, Tatsuya Niwa, Hideki Taguchi, Hiroyuki Nakamura, and *Takanori Oyoshi
G-Quadruplex-Proximity Protein Labeling Based on Peroxidase Activity.
Chem Commun 56(78):11641-11644 (2020)

109. Kashiwagi D, Shen HK, Sim S, Sano K, Ishida Y, Kimura A, Niwa T, Taguchi H, *Aida T.
Molecularly engineered "Janus GroEL": Application to supramolecular copolymerization with a higher level of sequence control.
J Am Chem Soc 142, 13310-13315 (2020)

108. †Konno H, †Watanabe-Nakayama T†, Uchihashi T, Okuda M, Zhu L, Kodera N, Kikuchi Y, *Ando T, *Taguchi, H. † equally contributed authors
Dynamics of oligomer and amyloid fibril formation by yeast prion Sup35 observed by high-speed atomic force microscopy.
PNAS 117, 7831-7836 (2020)

107. Muta M, Iizuka R*, Niwa T, Guo Y, Taguchi H and Funatsu T*
Nascent SecM chain interacts with outer ribosomal surface to stabilize translation arrest.
Biochem J 477, 557-566 (2020)

2019
106. Tsushima M, Sato S*, Niwa T, Taguchi, H, Nakamura H*
Catalyst-Proximity Protein Chemical Labelling on Affinity Beads Targeting Endogenous Lectins.
Chem Commun 55, 13275-13278 (2019)

105. Fukuda, T, Kawai-Noma, S., Pack, C-G., Taguchi H*
Large-scale analysis of diffusional dynamics of proteins in living yeast cells using fluorescence correlation spectroscopy.
Biochem Biophys Res Commun 520, 237-242 (2019)

104. Niwa T, Uemura E, Matsuno Y, *Taguchi, H.
Translation-coupled protein folding assay using a protease to monitor the folding status.
Protein Science 28, 1252-1261 (2019)
[selected as Protein Science Best Paper award 2019]

103. Deschoenmaeker F, Mihara S, Niwa T, Taguchi, H, Wakabayashi KI, *Hisabori T.
Disruption of the gene trx-m1 impedes the growth of Anabaena sp. PCC 7120 under nitrogen starvation.
Plant Cell Physiol. 60, 1504-1513 (2019)

102. *Nojima T, Niwa T, *Taguchi H.
Proteome analysis of phase-separated condensed proteins with ionic surfactants revealed versatile formation of artificial biomolecular condensate.
Biomacromolecules 20, 539-545 (2019)

2018
101. Furuki T, Niwa T, Taguchi H, Hatanaka R, Kikawada T, *Sakurai M.
A LEA model peptide protects the function of a red fluorescent protein in the dry state.
Biochem Biophys Rep 17: 27-31 (2018)

100. Sugita S, Watanabe K, Hashimoto K, Niwa T, Uemura E, Taguchi H, *Watanabe YH
Electrostatic interactions between middle domain motif-1 and the AAA1 module of the bacterial ClpB chaperone are essential for protein disaggregation.
J Biol Chem 293, 19228-19239 (2018)

99. Deschoenmaeker F, Mihara S, Niwa T, Taguchi H, Wakabayashi KI, *Hisabori T.
The absence of thioredoxin m1 and thioredoxin C in Anabaena sp. PCC 7120 leads to oxidative stress.
Plant Cell Physiol 59: 2432-2441 (2018)

98. Uemura E, Niwa T, Minami S, Takemoto K, Fukuchi S, Machida K, Imataka H, Ueda T, Ota M, Taguchi, H*
Large-scale aggregation analysis of eukaryotic proteins reveals an involvement of intrinsically disordered regions in protein folding.
Sci. Rep. 8:678. doi: 10.1038/s41598-017-18977-5. (2018)

97. Kashiwagi D, Sim S, Niwa T, Taguchi, H, Aida, T.*
Protein Nanotube Selectively Cleavable with DNA: Supramolecular Polymerization of "DNA-Appended Molecular Chaperones.
J. Am. Chem. Soc. 140, 26-29 (2018)

2017
96. Chadani Y, Niwa T, Izumi, T., Sugata, N., Nagao, A., Suzuki, T., Chiba S, , Ito K.* and Taguchi, H.*
Intrinsic ribosome destabilization underlies translation and provides an organism with a strategy of environmental sensing.
Mol. Cell 68, 528-539 (2017)

95. Fujiwara, K.*, Sawamura, T., Niwa, T., Deyama, T., Nomura, M. S.,, Taguchi, H., Doi, N.
In vitro transcription-translation using bacterial genome as a template to reconstitute intracellular profile.
Nucleic Acids Res. 45, 11449-11458 (2017)

94. Pack CG*, Inoue Y, Higurashi T, Kawai-Noma S, Hayashi D, Craig E, Taguchi, H
Heterogeneous interaction network of yeast prions and remodeling factors detected in live cells.
BMB Rep. 50, 478-483 (2017)

 2016
93. Sim, S.H., Niwa, T., Taguchi, H., Aida, T.*
Supramolecular Nanotube of Chaperonin GroEL: Length Control for Cellular Uptake Using Single-Ring GroEL Mutant as End-Capper.
J. Am. Chem. Soc. 138, 11152-11155 (2016)

92. Chadani Y, Niwa T, Chiba S, Taguchi, H.*, Ito K.*
Integrated in vivo and in vitro nascent chain profiling reveals widespread translational pausing.
Proc Natl Acad Sci USA. 113, E829-38 (2016)

91. Niwa. T, Fujiwara,, K., Taguchi, H.*
Identification of novel in vivo obligate GroEL/ES substrates based on data from a cell-free proteomics approach.
FEBS Lett. 590, 251-257 (2016)

90. Niwa T, Sasaki Y, Uemura E. Nakamura, S., Akiyama, M., Ando, M., Sawada, S., Mukai, S., Ueda, T., Taguchi, H.* and Akiyoshi, K.*
Comprehensive study of liposome-assisted synthesis of membrane proteins using a reconstituted cell-free translation system.
Sci. Rep. Dec 15;5:18025. doi: 10.1038/srep18025. (2016)


2015
89. Niwa T, Sugimoto R, Watanabe L, Nakamura S, Ueda T, Taguchi, H.*
Large-scale analysis of macromolecular crowding effects on protein aggregation using a reconstituted cell-free translation system
Front Microbiol. 6, 1113 (2015) doi: 10.3389/fmicb.2015.01113. eCollection 2015

88. Ishino, S, Kawata, Y., Taguchi, H., Kajimura, N., Matsuzaki, K., *Hoshino, M.
Effects of C-terminal truncation of chaperonin GroEL on the yield of in-cage folding of the green fluorescent protein.
J. Biol. Chem. 290, 15042-15051 (2015)

87. Sim, S.H., Miyajima, D., Niwa, T., Taguchi, H., *Aida, T.
Tailoring micrometer-long high-integrity 1D array of superparamagnetic nanoparticles in a nanotubular protein jacket and its lateral magnetic assembling behavior.
J. Am. Chem. Soc. 137, 4568-4561 (2015)

86. *Taguchi, H.,
Reaction cycle of chaperonin GroEL via symmetric "football" intermediate (review).
J. Mol. Biol. 427, 2912-2918 (2015)

85. Okuda, M, Niwa, T., *Taguchi, H.,
Single-Molecule Analyses on the Dynamics of Heat Shock Protein 104 (Hsp104) and Protein Aggregates.
J. Biol. Chem. 290, 7833-7840 (2015)

84. Odani, W, Urata, K, Okuda, M, Okuma, S, Koyama, H, Pack, CG, Fujiwara, K, Nojima, T, Kinjo, M, Kawai-Noma, S, *Taguchi, H.,
Peptide sequences converting polyglutamine into a prion in yeast.
FEBS J. 282, 477-490 (2015)

84. Odani, W, Urata, K, Okuda, M, Okuma, S, Koyama, H, Pack, CG, Fujiwara, K, Nojima, T, Kinjo, M, Kawai-Noma, S, Taguchi, H.*
Peptide sequences converting polyglutamine into a prion in yeast.
FEBS J. 282, 477-490 (2015)

2014
83. Ishimoto, T., Fujiwara, K., Niwa, T., Taguchi, H.*
Conversion of a chaperonin GroEL-independent protein into an obligate substrate.
J. Biol. Chem. 289 32073-32080 (2014)

82. Koike-Takeshita, A., Mitsuoka, K., Taguchi, H.*
Asp52 in combination with Asp398 plays a critical role in ATP hydrolysis of chaperonin GroEL.
J. Biol. Chem. 289 30005-30011 (2014)

81. Koike-Takeshita, A., Arakawa, T, Taguchi, H.*, Shimamura, T.*
Crystal structure of a symmetric football-shaped GroEL:GroES2 complex determined at 3.8Å reveals rearrangement between two GroEL rings.
J. Mol. Biol. 426, 3634-3641 (2014)

2013
80. Ohta, S., Kawai-Noma, S., Kitamura, A., Pack, C-G., *Kinjo, M. & Taguchi, H.*
The interaction of Hsp104 with yeast prion Sup35 as analyzed by fluorescence cross-correlation spectroscopy
Biochem. Biophys. Res. Commun. 442, 28-32 (2013)

79. Yamakawa, K., Furuki, T., Furuta, T., Hatanaka, R., Kikawada, T., Niwa, T. Taguchi, H. Furusawa H., Okahata, Y., and Sakurai, M.*
Experimental study on the mechanism underlying the anti-aggregation function of a group3LEA peptide.
Cryobiol. Cryotechnol. 59, 95-99 (2013)

78. Biswas, S., Kinbara, K., Niwa, T., Taguchi, H., Ishii, N., Watanabe, S., Miyata, K., Kataoka, K., Aida, T.*
Biomolecular Robotics for Chemomechanically Driven Guest Delivery Fueled by Intracellular ATP
Nature Chemistry 5, 613-620 (2013)

2012

77. Nojima, T.*, Konno, H., Kodera, N., Seio, K., Taguchi, H. and Yoshida, M.
Nano-scale alignment of proteins on a flexible DNA back-bone
PLoS One 7, e52534 (2012)

76. Nojima, T., Ikegami, T., Taguchi, H. and Yoshida, M.*
Flexibility of GroES mobile loop is required for efficient chaperonin function.
J. Mol. Biol. 422, 291-299, 2012

75. Niwa, T., Kanamori T., Ueda, T.*, Taguchi, H.*
Global Analysis of Chaperone Effects Using a Reconstituted Cell-Free Translation System
Proc. Natl. Acad. Sci. U.S.A. 109, 8937-8942 (2012) download PDF , Supplement (.pdf 1.8MB) , Datasets (.zip 1.7Mb)

74. Fujiwara K*, Taguchi H.
Mechanism of methionine synthase overexpression in chaperonin-depleted Escherichia coli
Microbiology 158, 917-924 (2012) abstract (PubMed)

2011
73. Takemoto K*, Niwa T, Taguchi H.
Difference in the distribution pattern of substrate enzymes in the metabolic network of Escherichia coli, according to chaperonin requirement.
BMC Syst Biol. 5, 98 (2011) abstract (PubMed) full text free

72. Sasaki, Y, Asayama, W., Niwa, T., Sawada, S., Ueda, T., Taguchi, H., Akiyoshi, K.*
Amphiphilic Polysaccharide Nanogels as Artificial Chaperones in Cell-Free Protein Synthesis
Macromol. Biosci. 11, 814-820 (2011) abstract (PubMed)

71. Inoue, Y., Kawai-Noma, S., Koike-Takeshita, A., Taguchi, H. and Yoshida, M.*
Yeast prion protein New1 can break Sup35 amyloid fibrils into fragments in an ATP-dependent manner.
Genes to Cells 16, 545-556 (2011) abstract (PubMed)

70. Tsuji, T., Kawai-Noma, S., Pack, C-G., Terajima, H., Yajima, J., Nishizaka, T., Kinjo, M. & Taguchi, H.*
Single-particle tracking of quantum dot-conjugated prion proteins inside yeast cells.
Biochem. Biophys. Res. Commun. 405, 638-643 (2011) abstract (PubMed)

69. Zhou, Z-P., Shimizu, Y., Tadakuma, H.*, Taguchi, H., Ito, K. and Ueda, T.
Single molecule imaging of the trans-translation entry process via anchoring of the tagged ribosome.
J. Biochem. 149, 609-618 (2011) abstract (PubMed)

2010
68. Kawai-Noma, S., Pack, C-G., Kojidani, T., Asakawa, H., Hiraoka, Y., Kinjo, M., Haraguchi, T., Taguchi, H.*, and Hirata, A.
In vivo evidence for the fibrillar structures of Sup35 prions in yeast cells.
J. Cell Biol. 190, 223-231 (2010) abstract (PubMed) fulltext free

67. Fujiwara, K., Ishihama, Y., Nakahigashi, K., Soga, T. and Taguchi, H.*
A systematic survey of in vivo obligate chaperonin-dependent substrates.
EMBO J. 29, 1552-1564 (2010) abstract (PubMed) fulltext free

66. Taguchi, H.* and Kawai-Noma, S.
Diffuse oligomer-based transmission of yeast prions. (Review)
FEBS J. 277, 1359-1368 (2010) abstract (PubMed)

2009
65. Kubota, H., Mikhailenko, S. V., Okabe, H., Taguchi, H., and Ishiwata, S.*
D-loop of actin differently regulates the motor function of myosins II And V.
J. Biol. Chem. 284, 35251-35258 (2009) abstract (PubMed) free pdf

64. Kawai-Noma, S., Pack, C-G., Tsuji, T., Kinjo, M., Taguchi, H.*
Single mother-daughter pair analysis to analyze the diffusion properties of yeast prion Sup35 in guanidine-HCl treated [PSI+] cells.
Genes to Cells 14, 1045-1054 (2009) abstract (PubMed)

63. Biswas, S., Kinbara, K., Oya, N., Ishii, N., Taguchi, H., Aida, T.*
A tubular biocontainer: Metal ion-induced 1D assembly of a molecularly engineered chaperonin.
J. Am. Chem. Soc. 131, 7556-7557 (2009) abstract (PubMed)

62. Niwa, T., Ying, B.-W., Saito, K., Jin, W. Z., Takada, S., Ueda, T.*, Taguchi, H.*
Bimodal protein solubility distribution revealed by an aggregation analysis of the entire ensemble of Escherichia coli proteins.
Proc. Natl. Acad. Sci. U.S.A. 106, 4201-4206 (2009)
download PDF , Supplement (.pdf, 1.2Mb) , Raw data (.xls, 0.8Mb)

61. Kanno, R., Koike-Takeshita, A., Yokoyama, K., Taguchi, H., Mitsuoka, K.*
Cryo-EM structure of the native GroEL-GroES complex from Thermus thermophilus encapsulating substrate inside the cavity.
Structure 17, 287-293 (2009) abstract (PubMed)


 2008
60. Hosono, K., Ueno, T., Taguchi, H., Motojima, F., Zako, T., Yoshida, M., Funatsu, T.*
Kinetic analysis of conformational changes of GroEL based on the fluorescence of tyrosine 506.
Protein J. 27, 461-468 (2008) abstract (PubMed)


59. Koike-Takeshita, A., Yoshida, M., Taguchi, H.*
Revisiting the GroEL-GroES reaction cycle via the symmetrical intermediate implied by novel aspects of the GroEL (D398A) mutant.
J. Biol. Chem. 283, 23774-23781 (2008) abstract (PubMed) free pdf
 Selected as JBC Papers of the Week

58. Uemura, S., Iizuka, R., Ueno, T., Shimizu, Y., Taguchi, H., Ueda, T., Puglisi, J., Funatsu, T.*
Single molecule imaging of full protein synthesis by immobilized ribosomes.
Nucleic Acids Research 36 e70 (2008)

57. Asayama, W., Sawada, S., Taguchi, H., Akiyoshi, K.*
Comparison of refolding activities between nanogel artificial chaperone and GroEL systems
Int. J. Biol. Macromol. 42, 241-246 (2008)

2007
56. Fujiwara, K. and Taguchi, H.*
Filamentous morphology in GroE-depleted Escherichia coli induced by impaired folding of FtsE.
J. Bacteriol. (2007) 189, 5860-5866 (2007) free PDF

55. Suzuki, H. Ueda, T., Taguchi, H. Takeuchi, N.*
Chaperone properties of mammalian mitochondrial translation factor Tu.
J. Biol. Chem. 282, 4076-4054 (2007)

2006
54. Kawai-Noma, S., Ayano, S., Pack, C-G., Kinjo, M., Yoshida, M., Yasuda, K., Taguchi, H.*
Dynamics of yeast prion aggregates in single living cells.
Genes to Cells 11, 1085-1096 (2006) abstract

53. Ying, B.-W. Taguchi, H.*, Ueda, T.*
Co-translational binding of GroEL to nascent polypeptides is followed by post-translational encapsulation by GroES to mediate protein folding.
J. Biol. Chem. 281, 21813-21819 (2006) free PDF

52. Muramatsu, S., Kinbara, K., Taguchi, H., Ishii, N., Aida, T.*
Semibiological molecular machine with an implemented “AND” logic gate for regulation of protein folding.
J. Am. Chem. Soc. 128, 3764-3769 (2006)

51. Koike-Takeshita, A, Shimamura, T., Yokoyama, K., Yoshida, M., Taguchi, H.*
Leu-309 plays a critical role in the encapsulation of substrate protein into the internal cavity of GroEL.
J. Biol. Chem. 281, 962-967 (2006) free PDF

2005

50. Taguchi, H.*
Chaperonin GroEL Meets the Substrate Protein as a "Load" of the Rings (review)
J. Biochem. 137, 543 - 549 (2005)


49. Ying, B.-W. Taguchi, H., Kondo, M., Ueda, T.*
Co-translational involvement of the chaperonin GroEL in the folding of newly translated polypeptides
J. Biol. Chem. 280, 12035-12040 (2005) free PDF

2004
48. Inoue, Y., Taguchi, H., Kishimoto, A., Yoshida, M.*
Hsp104 binds to yeast sup35 prion fiber but needs other factor(s) to sever it.
J. Biol. Chem. 279, 52319-52323 (2004) free PDF

47. Ayano, S.#, Noma, S.#, Yoshida, M., Taguchi, H., Yasuda, K.* [# equally contributed]
On-chip single-cell observation assay for propagation dynamics of yeast Sup35 prion-like proteins
Jpn. J.Appl. Phys. 43, 1429-1432 (2004)

46. Taguchi, H., Tsukuda, K., Motojima, F., Koike-Takeshita, A., Yoshida, M.*
BeFx stops chaperonin cycle of GroEL/GroES and generates a complex with double folding chambers
J. Biol. Chem. 279, 45737-45743 (2004) free PDF

45. Ying, B.W., Taguchi, H., Ueda, H., Ueda, T.*
Chaperone-assisted folding of a single-chain antibody in a reconstituted translation system.
Biochem. Biophys. Res. Commun. 320, 1359-1364 (2004)

44. Shimamura, T., Koike-Takeshita, A., Yokoyama, K., Masui, R., Murai, N., Yoshida, M., Taguchi H., Iwata, S.*
Crystal structure of the native chaperonin complex from Thermus thermophilus revealed unexpected asymmetry at the cis-cavity.
Structure 12, 1471-1480 (2004) free PDF

43. Ueno, T.#, Taguchi, H.#, Tadakuma, H., Yoshida, M.*, Funatsu, T.*[# equally contributed]
GroEL mediates protein folding with a two successive timer mechanism.
Mol. Cell 14, 423-434 (2004) free PDF

42. Kishimoto, A., Hasegawa, K., Suzuki, H., Taguchi, H., Namba, K.*, Yoshida, M.*
Beta-helix is a likely core structure of yeast prion Sup35 amyloid fibers.
Biochem. Biophys. Res. Commun. 315, 739-745 (2004)

41. Suno, R., Taguchi, H., Masui, R., Odaka, M., Yoshida, M.*
Trigger factor from Thermus themophilus is a Zn2+-dependent chaperone.
J. Biol. Chem. 279, 6380-6384 (2004) free PDF

2003
40. Shimamura, T., Koike-Takeshita, A., Yokoyama, K., Yoshida, M., Taguchi H., Iwata, S.*
Crystallization of the chaperonin GroEL-GroES complex from Thermus thermophilus HB8.
Acta Crystallogr D Biol Crystallogr. 59, 1632-1634 (2003)

39. Fay, N., Inoue, Y., Bousset, L., Taguchi H., Melki, R.*
Assembly of the yeast prion Ure2p into protein fibrils: Thermodynamic and kinetic characterization.
J. Biol. Chem. 278, 30199-30205(2003) free PDF

38. Sekiguchi, H., Arakawa, H., Taguchi H., Ito, T., Kokawa, R., Ikai, A.*
Specific interaction between GroEL and denatured protein measured by compression-free force spectroscopy.
Biophys. J. 85, 484-490 (2003)

2002
37. Makyio H, Niwa H, Motohashi K, Taguchi H., Yoshida M.*
Stabilization of FtsH-unfolded protein complex by binding of ATP and blocking of protease.
Biochem. Biophys. Res. Commun. 296, 8-12 (2002)

36. Yoshida, T., Kawaguchi, R., Taguchi, H, Yoshida, M., Yasunaga, T., Wakabayashi, T., Yohda, M., Maruyama, T.*
Archaeal group II chaperonin mediates protein folding in the cis-cavity without a detachable GroES-like co-chaperonin.
J. Mol. Biol. 315, 73-85 (2002)

2001
35. Fukami, T. A., Yohda, M., Taguchi, H., Yoshida, M., Miki, K.*
Crystal Structure of Chaperonin-60 from Paracoccus denitrificans.
J. Mol. Biol. 312, 501-509 (2001)

34. Inoue, Y., Kishimoto, A., Hirao, J., Yoshida, M.*, Taguchi, H.,
Strong growth polarity of yeast prion-fiber revealed by single fiber imaging. [Accelerated publication]
J. Biol. Chem. 276, 35227-35230 (2001) free PDF

33. Taguchi, H.#, Ueno, T.#, Tadakuma, H.#, Yoshida, M.*, Funatsu, T.* [# equally contributed]
Single-molecule observation of protein-protein interactions in the chaperonin system.
Nat. Biotechnol. 19, 861-865 (2001) free PDF

32. Takada, K.*, Hirakawa, T., Yokosawa, H., Okawa, Y., Taguchi, H., Ohkawa, K.,
Isolation of Ubiquitin-E2 (Ubiquitin-Conjugating Enzyme) Complexes from Erythroleukemia Cells using Immunoaffinity Techniques.
Biochemical J. 356, 199-206 (2001)

31. Shiseki, K., Murai, N., Motojima, F., Hisabori, T., Yoshida, M., Taguchi, H.*
Synchronized domain opening motion of GroEL is essential for communication between the two rings.
J. Biol. Chem. 276, 11335-11338 (2001) free PDF

2000
30. Yokoyama, K.*, Ohkuma, S., Taguchi, H., Yasunaga, T, Wakabayashi, T., Yoshida, M.
V-Type H+-ATPase/synthase from a thermophilic eubacterium, Thermus Thermophilus; Subunit Structure And Operon.
J. Biol. Chem. 275, 13955-13961 (2000) free PDF

29. Watanabe, Y., Motohashi, K., Taguchi, H., Yoshida, M.*
Heat-inactivated proteins managed by DnaKJ-GrpE-ClpB chaperones are released as a chaperonin-recognizable nonnative form.
J. Biol. Chem. 275, 12388-12392 (2000) free PDF

28. Teshima, T., Kohda, J., Kondo, A.*, Taguchi, H., Yohda, M., Fukuda, H.,
Preparation of Thermus thermophilus holo-chaperonin-immobilized microspheres with high ability to facilitate protein refolding.
Biotechnol Bioeng. 68, 184-190 (2000).

27. Asahara, Y., Atsuta, K., Motohashi, K., Taguchi, H., Yohda, M., Yoshida, M.*
FtsH recognizes unfolded proteins and hydrolyzes carboxyl side of hydrophobic residues.
J. Biochem. 127, 931-937 (2000)

26. Aoki, K., Motojima, F., Taguchi, H., Yomo, T., Yoshida, M.*
GroEL binds artificial proteins with random sequences.
J. Biol. Chem., 275, 13755-13758 (2000) free PDF

25. Pack, C-G.*, Aoki, K., Taguchi, H., Yoshida, M., Kinjo, M., Tamura, M.
Effect of electrostatic interactions on the binding of charged substrate to GroEL studied by highly sensitive fluorescence correlation spectroscopy.
Biochem. Biophys. Res. Commun., 267, 300-304 (2000)

1999
24. Sakikawa, C., Taguchi, H., Makino, Y., Yoshida, M.*
On the maximum size of proteins to stay and fold in the cavity of GroEL underneath GroES.
J. Biol. Chem. 274, 21251-21256 (1999) free PDF

23. Pack, C-G., Nishimura, G., Tamura, M., Aoki, K., Taguchi, H., Yoshida, M., Kinjo, M.*
Analysis of interaction between chaperonin GroEL and its substrate using fluorescence correlation spectroscopy.
Cytometry, 36, 247-253 (1999)

1998
22. Teshima, T., Kohda, J., Kondo, A.*, Taguchi, H., Yohda, M., Endo, I., Fukuda, H.
Protein refolding system using holo-chaperonin from thermophilic bacterium Thermus thermophilus.
J. Ferment. Bioeng., 85, 564-570 (1998)

21. Taguchi, H. and Yoshida, M.*
Chaperonin from thermophile Thermus thermophilus.
Methods Enzymol. 290, (1998) 169-180

1997
20. Yoshida T., Yohda M.*, Iida T., Maruyama T., Taguchi H., Yazaki K., Ohta T., Odaka M., Endo I., and Kagawa Y.*
Structural and Functional Characterization of Homo-oligomeric Complexes of alfa and beta Chaperonin Subunits from the Hyperthermophilic Archaeum, Thermococcus strain KS-1.
J. Mol. Biol., 273, 635-645 (1997).

19. Aoki, K., Taguchi, H., Shindo, Y., Yoshida, M.*, Ogasahara, K., Yutani, K., Tanaka, N.
Calorimetric Observation of a GroEL-Protein Binding Reaction with Little Contribution of Hydrophobic Interaction.
J. Biol. Chem. 272, 32158-32162 (1997) free PDF

18. Nakamura, N., Taguchi, H., Ishii, N., Yoshida, M., Suzuki, M., Endo, I., Miura, K., Yohda, M.*
Purification and molecular cloning of the group II chaperonin from the acidothermophilic archaeon, Sulfolobus sp. strain 7.
Biochem. Biophys. Res. Commun. 236, 727-732 (1997)

17. Taguchi, H., Amada, K., Murai, N., Yamakoshi, M., Yoshida, M.*
ATP-, K+-dependent Heptamer Exchange Reaction Produces Hybrids between GroEL and Chaperonin from Thermus thermophilus.
J. Biol. Chem. 272, 18155-18160 (1997) free PDF

16. Makino, Y., Amada, K., Taguchi, H., Yoshida, M.*
Chaperonin-mediated folding of Green Fluorescent Protein.
J. Biol. Chem. 272, 12468-12474 (1997) free PDF

1995
15. Amada, K., Yohda, M., Odaka, M., Endo, I., Ishii, N., Taguchi, H., and Yoshida, M.*
Molecular cloning, expression, and characterizatiion of chaperonin-60 and chaperonin-10 from a thermophilic bacterium, Thermus thermophilus HB8.
J. Biochem. 118, 347-354 (1995) .

14. Murai, N., Taguchi, H. and Yoshida, M.*
Kinetic analysis of interaction between GroEL and reduced alfa-lactalbumin; Effect of GroES and nucleotides.
J. Biol. Chem. 270, 19957-19963 (1995) free PDF

13. Ishii, N., Taguchi, H., Sasabe, H., and Yoshida, M.*
Equatorial split of holo-chaperonin from Thermus thermophilus by ATP and K+.
FEBS Lett. 362, 121-125 (1995)

12. Taguchi, H. and Yoshida, M.*
Chaperonin releases the substrate protein in a form with tendency to aggregate and ability to rebind to chaperonin.
FEBS Lett. 359, 195-198 (1995)

1994
11. Motohashi, K., Taguchi, H., Ishii, N., and Yoshida, M.*
Isolation of the stable hexameric DnaK-DnaJ complex from Thermus thermophilus.
J. Biol. Chem. 269, 27074-27079 (1994) free PDF

10. Ishii, N., Taguchi, H., Sasabe, H., and Yoshida, M.*
Folding intermediate binds to the bottom of bullet-shaped holo-chaperonin and is readily accessible to antibody.
J. Mol. Biol. 236, 691-696 (1994)

9. Taguchi, H., Makino, Y., and Yoshida, M.*
Monomeric chaperonin-60 and its 50kD fragment possess the ability to interact with non-native proteins, to suppress aggregation, and to promote protein folding.
J. Biol. Chem. 269, 8529-8534 (1994) free PDF


1993
8. Makino, Y., Taguchi, H. and Yoshida, M.*
Truncated GroEL monomer has the ability to promote folding of rhodanese without GroES and ATP.
FEBS Lett. 336, 363-367 (1993)

7. Yoshida, M.*, Ishii, N., Muneyuki, E. and Taguchi, H.
A chaperonin from a thermophilic bacterium, Thermus thermophilus.
Phil. Trans. R. Soc. Lond. B 339, 305-312 (1993)

6. Taguchi, H. and Yoshida, M.*
Chaperonin from Thermus thermophilus can protect several enzymes from irreversible heat denaturation by capturing denaturation intermediate.
J. Biol. Chem. 268, 5371-5375 (1993) free PDF


1992
5. Sumi, M., Taguchi, H., Yokoyama, K., Ishii, N. and Yoshida, M.*
Identification and characterization of a chaperonin from Paracoccus denitrificans.
Life Sci. Adv. 11, 179-182 (1992)

4. Ishii, N., Taguchi, H., Sumi, M. and Yoshida, M.*
Structure of holo-chaperonin studied with electron microscopy: Oligomeric cpn10 on top of two layers of cpn60 rings with two stripes each.
FEBS Lett. 299, 169-174 (1992)

1991
3. Ishii, N., Taguchi, H., Yoshida, M., Yoshimura, H., and Nagayama, K.*
Image analysis by electron microscopy of two-dimensional crystals developed on a mercury surface of chaperonin from Thermus thermophilus.
J. Biochem. 110, 905-908 (1991)

2. Taguchi, H., Konishi, J., Ishii, N., and Yoshida, M.*
A chaperonin from a thermophilic bacterium, Thermus thermophilus, that controls refoldings of several thermophilic enzymes.
J. Biol. Chem. 266, 22411-22418 (1991) free PDF

1990
1. Kobayashi, Y.*, Shimazaki, T., Taguchi, H., and Sato, F.*
Highly stereocontrolled total synthesis of Leukotriene B4, 20-hydroxyleukotriene B4, Leukotriene B3, and their analogues.
J. Org. Chem. 55, 5324-5335 (1990)
------- Books --------

1. Taguchi, H. and Yoshida, M.GroEL and GroES of Thermus thermophilus. in "Guidebook to Molecular Chaperones and Protein-folding catalysts" edited by M. -J. Gething, Sambrook and Tooze Publication at Oxford University Press 187-188 (1997).

2. Yamakoshi, M., Taguchi, H., Ishii, N., Yoshida, M.,A Chaperonin from a Thermophilic Bacterium, Thermus thermophilus.in "Molecular Chaperones in the life cycle of proteins", edited by A. L. Fink and Y. Goto), Marcel Dekker, 301-330 (1997)