Nara Women's University Hiroshi Ueno

Hiroshi Ueno
Professor, B.E., Kyoto University M.A., Brandeis University Ph.D., Iowa State University
Previous positions: Assistant Professor, Rockefeller University Summer Investigator, Woods Hole Marine Biological Laboratory Associate Professor, Osaka Medical College Associate Professor, Kyoto University School of Agriculture Professor, Nara Women's University Professor, Ryukoku Univresity School of Agriculture Rockefeller Foundation Fellow New York Heart Association Investigator

	Ueno Lab Web Page
hueno@cc.nara-wu.ac.jp Phone&Fax：+81 742-20-3493

Research interests
Majority of proteins, including enzymes, are relocated within the cells to their final destinations after the protein synthesis being completed. During this process, many events, such as protein folding, post-translational modification, protein sorting or transportation, are in evident. Our research is to challenge to those unsolved mysteries with the help of techniques in protein chemistry, genetic engineering, and biophysics.

Publications (selected)
Microanalysis of GABA: An application for evaluating GABA production in yeast strains and the effect of spice extracts on glutamate decarboxylase activity. J. Biol. Macromol., 1,45-48 (2001).
Structural and functional changes in bovine pancreatic ribonuclease A by the replacement of Phe120 with other hydrophobic residues. J. Biochem., 129, 917-922 (2001).
Interaction mode of H397A mutant carboxypeptidase Y with protein substrates analyzed by the surface plasmon resonance. Bull. Chem. Soc. Japan, 73, 2587-2590 (2000).
Expression of functional pancreatic ribonuclease A in yeast: Comparative expression system between Saccharomyces cerevisiae and Pichia pastoris. Biosci. Biotechnol. Biosci., in press (2000).
Enzymatic and structural aspects on glutamate decarboxylase.　 J. Mol. Catalysis B: Enzymatic, 10, 67-79 (2000).
Effect of mutagenic replacement of carboxyl terminal amino acid, Val124, on properties and regeneration of bovine pancreatic ribonuclease A.　 J. Biochem., 127, 877-881 (2000).
Carboxypeptidase Y: Structural basis for protein sorting and catalytic triad.　 J. Biochem., 126, 1-6 (1999).
Contribution of the carbohydrate moiety to conformational stability of the carboxypeptidase Y: High pressure.　Eur. J. Biochem., 262, 475-483 (1999).
Expression of human histidine decarboxylase in Saccharomyces cerevisiae.　J. Biochem. Mol. Biol. Biophys., 2, 141-146 (1998).
Proton-relay system of carboxypeptidase Y as a sole catalytic site: Studies on mutagenic replacement of His397.　J. Biochem., 124, 446-450 (1998).
Role of Phe120 on the activity and structure of bovine pancreatic ribonuclease A.　J. Biochem., 124, 410-416 (1998).
Bovine spleen cathepsin A: Characterization and comparison with protective protein.　J. Biochem., 120, 701-706 (1998).
A novel heterologous gene expression system in Saccharomyces cerevisiae using the isocitrate lyase promoter from Candida tropicalis. Appl. Microbiol. Biotechnol., 44, 759-765 (1996).
A large compressibility change of proteins induced by a single amino acid substitution. Protein Science, 5, 542-545 (1996).
Identification of the catalytic histidine residue participating in the charge-relay system of carboxypeptidase Y. Protein Science, 4, 2433-2435 (1995).
Random chemical modification of the oxygen-linked chloride-binding sites of hemoglobin. Those in the central dyad axis may influence the transition between deoxy- and oxy-hemoglobin. J. Protein Chem., 12, 561-570 (1993).
Kinetic and stereochemical comparison of wild-type and active-site K145Q mutant enzyme of bacterial D-amino acid transaminase. J. Biol. Chem., 268, 6932-6938 (1993).
Effects of Methyl acetyl phosphate, a covalent anti-sickling agent, on the density profiles of sickle erythrocytes. J. Lab. Clin. Med., 120, 152-158 (1992).
The functional, oxygen-linked chloride binding sites of hemoglobin are contiguous within a channel in the central cavity. J. Protein Chem., 11, 177-185 (1992).
Substitution of glutamine for lysine at the pyridoxal phosphate binding site of bacterial D-amino acid transaminase: Effects of exogenous amines on the slow formation of intermediates. J. Biol. Chem., 265, 22306-22312 (1990).
Effects of D-serine on bacterial D-amino acid transaminase: Formation of a new spectral band and inactivation of the enzyme. Biochemistry, 28, 8798-8803 (1989).
Stereochemistry of reactions catalyzed by bacterial D-amino acid transaminase. J. Biol. Chem., 264, 17784-17789 (1989).
Methyl acetyl phosphate as a covalent probe for anion binding sites in human and bovine hemoglobins. J. Biol. Chem., 264, 12344-12351 (1989).
Sequence-dependent reactivity of model peptides with glyceraldehyde. Carbohydr. Res., 189, 49-63 (1989).
Inactivation of human immunodeficiency virus in vitro by gossypol. Contraception, 39, 579-587 (1989).
Some factors that influence the non-enzymic glycation of peptides and polypeptides by glyceraldehyde. J. Protein Chem., 8, 299-315 (1989).
Activity and spectroscopic properties of bacterial D-amino acid transaminase after multiple site-directed mutagenesis of a single tryptophan residue. Biochemistry, 28, 510-516 (1989).
Site-directed mutagenesis of the cysteinyl residues and the active site serine residue of bacterial D-amino acid transaminase. Biochemistry, 28, 505-509 (1989).
Properties of carboxymethylated, cross-linked hemoglobin A. Biochemistry, 26, 5755-5761 (1987).
Inhibition of the gelation of extracellular and intracellular hemoglobin S by selective acetylation with methyl acetyl phosphate. Biochemistry, 26, 3125-3129 (1987).
Pyrrolopyridine derivatives from pyridoxal 5'-sulfate. Biochemistry, 21, 5212-5219 (1982).
Chemistry of the inactivation of cytosolic aspartate aminotransferase by serine-O-sulfate. Biochemistry, 21, 4387-4393 (1982).
A novel reaction of the coenzyme of glutamate decarboxylase with L-serine-O-sulfate. Biochemistry, 21, 4377-4386 (1982).

Updated on 2005/01/12

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