A. Koike-Takeshita

发表

Crystal structure of the native chaperonin complex from Thermus thermophilus revealed unexpected asymmetry at the cis-cavity.

Hideki Taguchi, So Iwata, Masasuke Yoshida, 2004, Structure.

Mechanism of product chain length determination for heptaprenyl diphosphate synthase from Bacillus stearothermophilus.

T. Koyama, T. Nishino, K. Hirooka, 2000, European journal of biochemistry.

Gene cloning and overexpression of a geranylgeranyl diphosphate synthase of an extremely thermophilic bacterium, Thermus thermophilus.

K. Yokoyama, T. Nishino, C. Ohto, 1999, Bioscience, biotechnology, and biochemistry.

Cryo-EM structure of the native GroEL-GroES complex from thermus thermophilus encapsulating substrate inside the cavity.

H. Taguchi, K. Yokoyama, K. Mitsuoka, 2009, Structure.

Molecular Cloning and Nucleotide Sequences of the Genes for Two Essential Proteins Constituting a Novel Enzyme System for Heptaprenyl Diphosphate Synthesis (*)

T. Koyama, A. Koike-Takeshita, S. Obata, 1995, The Journal of Biological Chemistry.

Butirosin-biosynthetic gene cluster from Bacillus circulans.

T. Eguchi, K. Kakinuma, A. Koike-Takeshita, 2000, The Journal of antibiotics.

Identification of a Novel Gene Cluster Participating in Menaquinone (Vitamin K2) Biosynthesis

T. Koyama, A. Koike-Takeshita, K. Ogura, 1997, The Journal of Biological Chemistry.

Significance of the 20-kDa Subunit of Heterodimeric 2-Deoxy-scyllo-inosose Synthase for the Biosynthesis of Butirosin Antibiotics in Bacillus circulans

E. Nango, K. Kakinuma, A. Koike-Takeshita, 2002, Bioscience, biotechnology, and biochemistry.

Identification of significant residues in the substrate binding site of Bacillus stearothermophilus farnesyl diphosphate synthase.

T. Koyama, T. Nishino, A. Koike-Takeshita, 1996, Biochemistry.

Yeast prion protein New1 can break Sup35 amyloid fibrils into fragments in an ATP‐dependent manner

H. Taguchi, Masasuke Yoshida, A. Koike-Takeshita, 2011, Genes to cells : devoted to molecular & cellular mechanisms.

Asp-52 in Combination with Asp-398 Plays a Critical Role in ATP Hydrolysis of Chaperonin GroEL*

H. Taguchi, K. Mitsuoka, A. Koike-Takeshita, 2014, The Journal of Biological Chemistry.

Revisiting the GroEL-GroES Reaction Cycle via the Symmetric Intermediate Implied by Novel Aspects of the GroEL(D398A) Mutant*♦

H. Taguchi, Masasuke Yoshida, A. Koike-Takeshita, 2008, Journal of Biological Chemistry.

BeFx Stops the Chaperonin Cycle of GroEL-GroES and Generates a Complex with Double Folding Chambers*

H. Taguchi, Masasuke Yoshida, A. Koike-Takeshita, 2004, Journal of Biological Chemistry.

Leu309 Plays a Critical Role in the Encapsulation of Substrate Protein into the Internal Cavity of GroEL*

H. Taguchi, Masasuke Yoshida, K. Yokoyama, 2006, Journal of Biological Chemistry.

In vivo client proteins of the chaperonin GroEL-GroES provide insight into the role of chaperones in protein evolution

H. Taguchi, A. Koike-Takeshita, 2023, Frontiers in Molecular Biosciences.

Crystallization of the chaperonin GroEL-GroES complex from Thermus thermophilus HB8.

H. Taguchi, Masasuke Yoshida, S. Iwata, 2003, Acta crystallographica. Section D, Biological crystallography.

Crystal structure of a symmetric football-shaped GroEL:GroES2-ATP14 complex determined at 3.8Å reveals rearrangement between two GroEL rings.

H. Taguchi, T. Shimamura, T. Arakawa, 2014, Journal of molecular biology.

Structure of the Chaperonin-Substrate Complex

H. Taguchi, K. Mitsuoka, A. Koike-Takeshita, 2009 .

Monitoring Amyloid Sup35NM Growth with Label‐Free Electrical Detection Using a Field‐Effect Transistor Biosensor

T. Osaka, T. Nakanishi, A. Koike-Takeshita, 2014 .