Hamada M - Search Results

1

Studies on yeast nucleoside triphosphate-nucleoside diphosphate transphosphorylase (nucleoside diphosphokinase). IV. Steady-state kinetic properties with thymidine nucleotides (including 3'-azido-3'-deoxythymidine analogues).

Kuby SA, Fleming G, Alber T, Richardson D, Takenaka H, Hamada M. Kuby SA, et al. Among authors: hamada m. Enzyme. 1991;45(1-2):1-13. doi: 10.1159/000468859. Enzyme. 1991. PMID: 1666874

2

Studies on adenosine triphosphate transphosphorylases. XVIII. Synthesis and preparation of peptides and peptide fragments of rabbit muscle ATP-AMP transphosphorylase (adenylate kinase) and their nucleotide-binding properties.

Kuby SA, Hamada M, Johnson MS, Russell GA, Manship M, Palmieri RH, Fleming G, Bredt DS, Mildvan AS. Kuby SA, et al. Among authors: hamada m. J Protein Chem. 1989 Aug;8(4):549-62. doi: 10.1007/BF01026438. J Protein Chem. 1989. PMID: 2553049

3

Multiforms of mammalian adenylate kinase and its monoclonal antibody against AK1.

Kurokawa Y, Takenaka H, Sumida M, Oka K, Hamada M, Kuby SA. Kurokawa Y, et al. Among authors: hamada m. Enzyme. 1990;43(2):57-71. doi: 10.1159/000468708. Enzyme. 1990. PMID: 2261892

4

Studies of adenosine triphosphate transphosphorylases. XIV. Equilibrium binding properties of the crystalline rabbit and calf muscle ATP--AMP transphosphorylase (adenylate kinase) and derived peptide fragments.

Hamada M, Palmieri RH, Russell GA, Kuby SA. Hamada M, et al. Arch Biochem Biophys. 1979 Jun;195(1):155-77. doi: 10.1016/0003-9861(79)90338-2. Arch Biochem Biophys. 1979. PMID: 224811 No abstract available.

5

Studies on NADPH-cytochrome c reductase I: Isolation and several properties of the crystalline enzyme from ale yeast.

Tryon E, Cress MC, Hamada M, Kuby SA. Tryon E, et al. Among authors: hamada m. Arch Biochem Biophys. 1979 Oct 1;197(1):104-18. doi: 10.1016/0003-9861(79)90225-x. Arch Biochem Biophys. 1979. PMID: 120699 No abstract available.

6

[Adenylate kinase--structure and functions].

Hamada M, Takenaka H, Sumida M. Hamada M, et al. Tanpakushitsu Kakusan Koso. 1988 Aug;33(10):1708-27. Tanpakushitsu Kakusan Koso. 1988. PMID: 2854898 Review. Japanese. No abstract available.

7

Steady-state kinetics of Thr35 and Thr39 mutants in human adenylate kinase by site-directed mutagenesis.

Ayabe T, Takenaka H, Onitsuka T, Shibata K, Takenaka O, Uesugi S, Hamada M. Ayabe T, et al. Among authors: hamada m. Enzyme Protein. 1996;49(5-6):305-12. doi: 10.1159/000468640. Enzyme Protein. 1996. PMID: 9252788

8

Studies on adenosine triphosphate transphosphorylases. XIII. Kinetic properties of the crystalline rabbit muscle ATP-AMP transphorphorylase (adenylate kinase) and a comparison with the crystalline calf muscle and liver adenylate kinases.

Hamada M, Kuby SA. Hamada M, et al. Arch Biochem Biophys. 1978 Oct;190(2):772-9. doi: 10.1016/0003-9861(78)90338-7. Arch Biochem Biophys. 1978. PMID: 214039 No abstract available.

9

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: hamada m. Biochemistry. 1990 Feb 6;29(5):1107-11. doi: 10.1021/bi00457a002. Biochemistry. 1990. PMID: 2157484

J., Nishikawa, S., Tanaka, T., Uesugi, S., Takenaka, H., Hamada, M., & Kuby, S. A. (1989) Protein Eng. 2, 379-386] to replace these arginine residues with alanyl residues and yield the mutants R44A hAK1, R132A hAK1, R138A hAK1, and R149A hAK1. ...

J., Nishikawa, S., Tanaka, T., Uesugi, S., Takenaka, H., Hamada, M., & Kuby, S. A. (1989) Protein Eng. 2, 379-386] to repl …

10

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: hamada m. Protein Eng. 1989 Jan;2(5):379-86. doi: 10.1093/protein/2.5.379. Protein Eng. 1989. PMID: 2538811

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