Mihara H - Search Results

1

cDNA cloning, purification, and characterization of mouse liver selenocysteine lyase. Candidate for selenium delivery protein in selenoprotein synthesis.

Mihara H, Kurihara T, Watanabe T, Yoshimura T, Esaki N. Mihara H, et al. J Biol Chem. 2000 Mar 3;275(9):6195-200. doi: 10.1074/jbc.275.9.6195. J Biol Chem. 2000. PMID: 10692412 Free article.

2

Selenocysteine lyase from mouse liver.

Mihara H, Esaki N. Mihara H, et al. Methods Enzymol. 2002;347:198-203. doi: 10.1016/s0076-6879(02)47018-8. Methods Enzymol. 2002. PMID: 11898407 No abstract available.

3

Structure of external aldimine of Escherichia coli CsdB, an IscS/NifS homolog: implications for its specificity toward selenocysteine.

Mihara H, Fujii T, Kato S, Kurihara T, Hata Y, Esaki N. Mihara H, et al. J Biochem. 2002 May;131(5):679-85. doi: 10.1093/oxfordjournals.jbchem.a003151. J Biochem. 2002. PMID: 11983074 Free article.

4

Assembly of iron-sulfur clusters mediated by cysteine desulfurases, IscS, CsdB and CSD, from Escherichia coli.

Kurihara T, Mihara H, Kato S, Yoshimura T, Esaki N. Kurihara T, et al. Among authors: mihara h. Biochim Biophys Acta. 2003 Apr 11;1647(1-2):303-9. doi: 10.1016/s1570-9639(03)00078-5. Biochim Biophys Acta. 2003. PMID: 12686149

5

The putative malate/lactate dehydrogenase from Pseudomonas putida is an NADPH-dependent delta1-piperideine-2-carboxylate/delta1-pyrroline-2-carboxylate reductase involved in the catabolism of D-lysine and D-proline.

Muramatsu H, Mihara H, Kakutani R, Yasuda M, Ueda M, Kurihara T, Esaki N. Muramatsu H, et al. Among authors: mihara h. J Biol Chem. 2005 Feb 18;280(7):5329-35. doi: 10.1074/jbc.M411918200. Epub 2004 Nov 23. J Biol Chem. 2005. PMID: 15561717 Free article.

6

Identification of proteins interacting with selenocysteine lyase.

Tobe R, Mihara H, Kurihara T, Esaki N. Tobe R, et al. Among authors: mihara h. Biosci Biotechnol Biochem. 2009 May;73(5):1230-2. doi: 10.1271/bbb.90065. Epub 2009 May 7. Biosci Biotechnol Biochem. 2009. PMID: 19420685 Free article.

7

IscS functions as a primary sulfur-donating enzyme by interacting specifically with MoeB and MoaD in the biosynthesis of molybdopterin in Escherichia coli.

Zhang W, Urban A, Mihara H, Leimkühler S, Kurihara T, Esaki N. Zhang W, et al. Among authors: mihara h. J Biol Chem. 2010 Jan 22;285(4):2302-8. doi: 10.1074/jbc.M109.082172. Epub 2009 Nov 29. J Biol Chem. 2010. PMID: 19946146 Free PMC article.

8

Reaction mechanism and molecular basis for selenium/sulfur discrimination of selenocysteine lyase.

Omi R, Kurokawa S, Mihara H, Hayashi H, Goto M, Miyahara I, Kurihara T, Hirotsu K, Esaki N. Omi R, et al. Among authors: mihara h. J Biol Chem. 2010 Apr 16;285(16):12133-9. doi: 10.1074/jbc.M109.084475. Epub 2010 Feb 17. J Biol Chem. 2010. PMID: 20164179 Free PMC article.

9

Mammalian selenocysteine lyase is involved in selenoprotein biosynthesis.

Kurokawa S, Takehashi M, Tanaka H, Mihara H, Kurihara T, Tanaka S, Hill K, Burk R, Esaki N. Kurokawa S, et al. Among authors: mihara h. J Nutr Sci Vitaminol (Tokyo). 2011;57(4):298-305. doi: 10.3177/jnsv.57.298. J Nutr Sci Vitaminol (Tokyo). 2011. PMID: 22041913 Free article.

10

Cysteine sulfinate desulfinase, a NIFS-like protein of Escherichia coli with selenocysteine lyase and cysteine desulfurase activities. Gene cloning, purification, and characterization of a novel pyridoxal enzyme.

Mihara H, Kurihara T, Yoshimura T, Soda K, Esaki N. Mihara H, et al. J Biol Chem. 1997 Sep 5;272(36):22417-24. doi: 10.1074/jbc.272.36.22417. J Biol Chem. 1997. PMID: 9278392 Free article.

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