Hayashi H - Search Results

1

Activation of protein phosphatase 2A by cAMP-dependent protein kinase-catalyzed phosphorylation of the 74-kDa B'' (delta) regulatory subunit in vitro and identification of the phosphorylation sites.

Usui H, Inoue R, Tanabe O, Nishito Y, Shimizu M, Hayashi H, Kagamiyama H, Takeda M. Usui H, et al. Among authors: hayashi h. FEBS Lett. 1998 Jul 3;430(3):312-6. doi: 10.1016/s0014-5793(98)00684-x. FEBS Lett. 1998. PMID: 9688562 Free article.

2

Further studies on aspartate aminotransferase of thermophilic methanogens by analysis of general properties, bound cofactors, and subunit structures.

Tanaka T, Yamamoto S, Taniguchi M, Hayashi H, Kuramitsu S, Kagamiyama H, Oi S. Tanaka T, et al. Among authors: hayashi h. J Biochem. 1992 Dec;112(6):811-5. doi: 10.1093/oxfordjournals.jbchem.a123981. J Biochem. 1992. PMID: 1295891 Free article.

3

Evaluation of the holoenzyme content of aromatic L-amino acid decarboxylase in brain and liver tissues.

Kawasaki Y, Hayashi H, Hatakeyama K, Kagamiyama H. Kawasaki Y, et al. Among authors: hayashi h. Biochem Biophys Res Commun. 1992 Aug 14;186(3):1242-8. doi: 10.1016/s0006-291x(05)81539-6. Biochem Biophys Res Commun. 1992. PMID: 1510658

4

Phosphorylation in vitro of the 85 kDa subunit of phosphatidylinositol 3-kinase and its possible activation by insulin receptor tyrosine kinase.

Hayashi H, Miyake N, Kanai F, Shibasaki F, Takenawa T, Ebina Y. Hayashi H, et al. Biochem J. 1991 Dec 15;280 ( Pt 3)(Pt 3):769-75. doi: 10.1042/bj2800769. Biochem J. 1991. PMID: 1722393 Free PMC article.

5

Replacement of an interdomain residue Val39 of Escherichia coli aspartate aminotransferase affects the catalytic competence without altering the substrate specificity of the enzyme.

Hayashi H, Kuramitsu S, Kagamiyama H. Hayashi H, et al. J Biochem. 1991 May;109(5):699-704. doi: 10.1093/oxfordjournals.jbchem.a123443. J Biochem. 1991. PMID: 1917893 Free article.

6

Effects of replacement of tryptophan-140 by phenylalanine or glycine on the function of Escherichia coli aspartate aminotransferase.

Hayashi H, Inoue Y, Kuramitsu S, Morino Y, Kagamiyama H. Hayashi H, et al. Biochem Biophys Res Commun. 1990 Mar 16;167(2):407-12. doi: 10.1016/0006-291x(90)92037-z. Biochem Biophys Res Commun. 1990. PMID: 2182010

7

Purification and characterization of rho-crystallin from Japanese common bullfrog lens.

Fujii Y, Watanabe K, Hayashi H, Urade Y, Kuramitsu S, Kagamiyama H, Hayaishi O. Fujii Y, et al. Among authors: hayashi h. J Biol Chem. 1990 Jun 15;265(17):9914-23. J Biol Chem. 1990. PMID: 2190986 Free article.

8

Pre-steady-state kinetics of Escherichia coli aspartate aminotransferase catalyzed reactions and thermodynamic aspects of its substrate specificity.

Kuramitsu S, Hiromi K, Hayashi H, Morino Y, Kagamiyama H. Kuramitsu S, et al. Among authors: hayashi h. Biochemistry. 1990 Jun 12;29(23):5469-76. doi: 10.1021/bi00475a010. Biochemistry. 1990. PMID: 2201406

9

Cloning, nucleotide sequence and gene expression of bovine lung prostaglandin F synthetase.

Watanabe K, Fujii Y, Nakayama K, Ohkubo H, Kuramitsu S, Hayashi H, Kagamiyama H, Nakanishi S, Hayaishi O. Watanabe K, et al. Among authors: hayashi h. Adv Prostaglandin Thromboxane Leukot Res. 1989;19:462-5. Adv Prostaglandin Thromboxane Leukot Res. 1989. PMID: 2526518 No abstract available.

10

[Arg292----Val] or [Arg292----Leu] mutation enhances the reactivity of Escherichia coli aspartate aminotransferase with aromatic amino acids.

Hayashi H, Kuramitsu S, Inoue Y, Morino Y, Kagamiyama H. Hayashi H, et al. Biochem Biophys Res Commun. 1989 Feb 28;159(1):337-42. doi: 10.1016/0006-291x(89)92443-1. Biochem Biophys Res Commun. 1989. PMID: 2564274

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