Nishikawa S - Search Results

1

Expression of a synthetic gene for human cap binding protein (human IF-4E) in Escherichia coli and fluorescence studies on interaction with mRNA cap structure analogues.

Ueda H, Maruyama H, Doi M, Inoue M, Ishida T, Morioka H, Tanaka T, Nishikawa S, Uesugi S. Ueda H, et al. Among authors: nishikawa s. J Biochem. 1991 Jun;109(6):882-9. doi: 10.1093/oxfordjournals.jbchem.a123475. J Biochem. 1991. PMID: 1939010 Free article.

2

Combination of Trp and Glu residues for recognition of mRNA cap structure. Analysis of m7G base recognition site of human cap binding protein (IF-4E) by site-directed mutagenesis.

Ueda H, Iyo H, Doi M, Inoue M, Ishida T, Morioka H, Tanaka T, Nishikawa S, Uesugi S. Ueda H, et al. Among authors: nishikawa s. FEBS Lett. 1991 Mar 25;280(2):207-10. doi: 10.1016/0014-5793(91)80294-d. FEBS Lett. 1991. PMID: 1672854 Free article.

3

Secretion of recombinant ribonuclease T1 into the periplasmic space of Escherichia coli with the aid of the signal peptide of alkaline phosphatase.

Fujimura T, Tanaka T, Ohara K, Morioka H, Uesugi S, Ikehara M, Nishikawa S. Fujimura T, et al. Among authors: nishikawa s. FEBS Lett. 1990 Jun 4;265(1-2):71-4. doi: 10.1016/0014-5793(90)80886-n. FEBS Lett. 1990. PMID: 2114313 Free article.

4

Synthetic genes for human muscle-type adenylate kinase in Escherichia coli.

Kim HJ, Nishikawa S, Tanaka T, Uesugi S, Takenaka H, Hamada M, Kuby SA. Kim HJ, et al. Among authors: nishikawa s. Protein Eng. 1989 Jan;2(5):379-86. doi: 10.1093/protein/2.5.379. Protein Eng. 1989. PMID: 2538811

5

Increase in nucleolytic activity of ribonuclease T1 by substitution of tryptophan 45 for tyrosine 45.

Nishikawa S, Morioka H, Kimura T, Ueda Y, Tanaka T, Uesugi S, Hakoshima T, Tomita K, Ohtsuka E, Ikehara M. Nishikawa S, et al. Eur J Biochem. 1988 Apr 15;173(2):389-94. doi: 10.1111/j.1432-1033.1988.tb14011.x. Eur J Biochem. 1988. PMID: 3129293 Free article.

6

Conformation of 2'GMP bound to a mutant ribonuclease T1 (Y45W) determined by X-ray diffraction and NMR methods.

Itoh T, Tomita K, Hakoshima T, Hiroaki H, Uesugi S, Nishikawa S, Amisaki T, Morioka H, Ohtsuka E, Ikehara M. Itoh T, et al. Among authors: nishikawa s. J Biochem. 1991 Nov;110(5):677-80. doi: 10.1093/oxfordjournals.jbchem.a123639. J Biochem. 1991. PMID: 1664424 Free article.

7

In vitro mutagenesis studies at the arginine residues of adenylate kinase. A revised binding site for AMP in the X-ray-deduced model.

Kim HJ, Nishikawa S, Tokutomi Y, Takenaka H, Hamada M, Kuby SA, Uesugi S. Kim HJ, et al. Among authors: nishikawa s. Biochemistry. 1990 Feb 6;29(5):1107-11. doi: 10.1021/bi00457a002. Biochemistry. 1990. PMID: 2157484

With use of the site-directed mutagenesis method, point mutations were made in the artificial gene for hAK1 [Kim, H. J., Nishikawa, S., Tanaka, T., Uesugi, S., Takenaka, H., Hamada, M., & Kuby, S. ...

With use of the site-directed mutagenesis method, point mutations were made in the artificial gene for hAK1 [Kim, H. J., Nishikawa, …

8

A thermoresistant mutant of ribonuclease T1 having three disulfide bonds.

Nishikawa S, Adiwinata J, Morioka H, Fujimura T, Tanaka T, Uesugi S, Hakoshima T, Tomita K, Nakagawa S, Ikehara M. Nishikawa S, et al. Protein Eng. 1990 Apr;3(5):443-8. doi: 10.1093/protein/3.5.443. Protein Eng. 1990. PMID: 2349214

9

Structure and activity of artificial mutant variants of human growth hormone.

Nishikawa S, Nishida Y, Uemura H, Yamada Y, Tanaka T, Uesugi S, Morikawa M, Uchida E, Hayakawa T, Ikehara M. Nishikawa S, et al. Protein Eng. 1989 Oct;3(1):49-53. doi: 10.1093/protein/3.1.49. Protein Eng. 1989. PMID: 2682610

10

Two histidine residues are essential for ribonuclease T1 activity as is the case for ribonuclease A.

Nishikawa S, Morioka H, Kim HJ, Fuchimura K, Tanaka T, Uesugi S, Hakoshima T, Tomita K, Ohtsuka E, Ikehara M. Nishikawa S, et al. Biochemistry. 1987 Dec 29;26(26):8620-4. doi: 10.1021/bi00400a019. Biochemistry. 1987. PMID: 3126807

However, we have recently demonstrated that Glu-58 is an important but not an essential residue for catalytic activity, using the methods of genetic engineering to change Glu-58 to Gln-58 etc [Nishikawa, S., Morioka, H., Fuchimura, K., Tanaka, T., Uesugi, S., …

However, we have recently demonstrated that Glu-58 is an important but not an essential residue for catalytic activity, using the methods of …

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