Crystallization and preliminary X-ray diffraction studies of the prototypal homologue of mitoNEET (Tth-NEET0026) from the extreme thermophile Thermus thermophilus HB8
Kounosu, Asako, Iwasaki, Toshio, Baba, Seiki, Hayashi-Iwasaki, Yoko, Oshima, Tairo, Kumasaka, Takashi
Published in Acta crystallographica. Section F, Structural biology and crystallization communications (01.12.2008)
Published in Acta crystallographica. Section F, Structural biology and crystallization communications (01.12.2008)
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Spectroscopic Investigation of Selective Cluster Conversion of Archaeal Zinc-containing Ferredoxin fromSulfolobus sp. Strain 7
Iwasaki, Toshio, Watanabe, Eiji, Ohmori, Daijiro, Imai, Takeo, Urushiyama, Akio, Akiyama, Minoru, Hayashi-Iwasaki, Yoko, Cosper, Nathaniel J., Scott, Robert A.
Published in The Journal of biological chemistry (18.08.2000)
Published in The Journal of biological chemistry (18.08.2000)
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A stable intermediate in the thermal unfolding process of a chimeric 3‐isopropylmalate dehydrogenase between a thermophilic and a mesophilic enzymes
Hayashi‐Iwasaki, Yoko, Numata, Koichi, Yamagishi, Akihiko, Yutani, Katsuhide, Sakurai, Masahiro, Tanaka, Nobuo, Oshima, Tairo
Published in Protein science (01.03.1996)
Published in Protein science (01.03.1996)
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2P069 Thermodynamic evaluation of the highly stabilized cold shock protein homologue by introducing a disulfide bond(Proteins-stability, folding, and other physicochemical properties,Oral Presentations)
Hasegawa, Aoi, Iizuka, Kazunari, Hayashi-Iwasaki, Yoko, Kidokoro, Shun-ichi
Published in Seibutsu Butsuri (20.11.2007)
Published in Seibutsu Butsuri (20.11.2007)
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Studies on interdomain interaction of 3-isopropylmalate dehydrogenase from an extreme thermophile, Thermus thermophilus, by constructing chimeric enzymes
NUMATA, K, HAYASHI-IWASAKI, Y, YUTANI, K, OSHIMA, T
Published in Extremophiles : life under extreme conditions (01.11.1999)
Published in Extremophiles : life under extreme conditions (01.11.1999)
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Thermostabilization of a chimeric enzyme by residue substitutions: four amino acid residues in loop regions are responsible for the thermostability of Thermus thermophilus isopropylmalate dehydrogenase
Numata, K, Hayashi-Iwasaki, Y, Kawaguchi, J, Sakurai, M, Moriyama, H, Tanaka, N, Oshima, T
Published in Biochimica et biophysica acta (09.02.2001)
Published in Biochimica et biophysica acta (09.02.2001)
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