Hayashi-Iwasaki Y - Search Results

1

Crystallization and preliminary X-ray diffraction studies of the prototypal homologue of mitoNEET (Tth-NEET0026) from the extreme thermophile Thermus thermophilus HB8.

Kounosu A, Iwasaki T, Baba S, Hayashi-Iwasaki Y, Oshima T, Kumasaka T. Kounosu A, et al. Among authors: hayashi iwasaki y. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Dec 1;64(Pt 12):1146-8. doi: 10.1107/S1744309108035975. Epub 2008 Nov 28. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008. PMID: 19052371 Free PMC article.

2

Electrostatic interaction between two domains of isocitrate dehydrogenase from Thermus thermophilus is important for the catalytic function and protein stability.

Yaoi T, Hayashi-Iwasaki Y, Oshima T. Yaoi T, et al. Among authors: hayashi iwasaki y. FEBS Lett. 1996 Dec 2;398(2-3):228-30. doi: 10.1016/s0014-5793(96)01243-4. FEBS Lett. 1996. PMID: 8977112 Free article.

3

Studies on interdomain interaction of 3-isopropylmalate dehydrogenase from an extreme thermophile, Thermus thermophilus, by constructing chimeric enzymes.

Numata K, Hayashiiwasaki Y, Yutani K, Oshima T. Numata K, et al. Extremophiles. 1999 Nov;3(4):259-62. doi: 10.1007/s007920050125. Extremophiles. 1999. PMID: 10591016

4

Purification and characterization of recombinant 3-isopropylmalate dehydrogenases from Thermus thermophilus and other microorganisms.

Hayashi-Iwasaki Y, Oshima T. Hayashi-Iwasaki Y, et al. Methods Enzymol. 2000;324:301-22. doi: 10.1016/s0076-6879(00)24240-7. Methods Enzymol. 2000. PMID: 10989439 No abstract available.

5

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. Numata K, et al. Among authors: hayashi iwasaki y. Biochim Biophys Acta. 2001 Feb 9;1545(1-2):174-83. doi: 10.1016/s0167-4838(00)00275-2. Biochim Biophys Acta. 2001. PMID: 11342043

6

A stable intermediate in the thermal unfolding process of a chimeric 3-isopropylmalate dehydrogenase between a thermophilic and a mesophilic enzymes.

Hayashi-Iwasaki Y, Numata K, Yamagishi A, Yutani K, Sakurai M, Tanaka N, Oshima T. Hayashi-Iwasaki Y, et al. Protein Sci. 1996 Mar;5(3):511-6. doi: 10.1002/pro.5560050313. Protein Sci. 1996. PMID: 8868488 Free PMC article.

7

Spectroscopic investigation of selective cluster conversion of archaeal zinc-containing ferredoxin from Sulfolobus sp. strain 7.

Iwasaki T, Watanabe E, Ohmori D, Imai T, Urushiyama A, Akiyama M, Hayashi-Iwasaki Y, Cosper NJ, Scott RA. Iwasaki T, et al. Among authors: hayashi iwasaki y. J Biol Chem. 2000 Aug 18;275(33):25391-401. doi: 10.1074/jbc.M909243199. J Biol Chem. 2000. PMID: 10827091 Free article.

8

The initial step of the thermal unfolding of 3-isopropylmalate dehydrogenase detected by the temperature-jump Laue method.

Hori T, Moriyama H, Kawaguchi J, Hayashi-Iwasaki Y, Oshima T, Tanaka N. Hori T, et al. Among authors: hayashi iwasaki y. Protein Eng. 2000 Aug;13(8):527-33. doi: 10.1093/protein/13.8.527. Protein Eng. 2000. PMID: 10964981

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