GUANIDINE HYDROCHLORIDE INDUCED UNFOLDING OF THE ALPHA SUBUNIT OF TRYPTOPHAN SYNTHASE AND OF THE TWO ALPHA PROTEOLYTIC FRAGMENTS: EVIDENCE FOR STEPWISE UNFOLDING OF THE TWO ALPHA DOMAINSMILES EW; YUTANI K; OGASAHARA K et al.1982; BIOCHEMISTRY (EAST.); ISSN 0006-2960; USA; DA. 1982; VOL. 21; NO 11; PP. 2586-2592; BIBL. 25 REF.Article

THE SECONDARY STRUCTURE OF ALPHA _S-CASEINONO T; YUTANI K; ODAGIRI S et al.1974; AGRIC. BIOL. CHEM.; JAP.; DA. 1974; VOL. 38; NO 9; PP. 1603-1608; BIBL. 23REF.Article

CONFORMATION OF ALPHA _S-CASEIN IN VARIOUS CONCENTRATIONSONO T; YUTANI K; ODAGIRI S et al.1974; AGRIC. BIOL. CHEM.; JAP.; DA. 1974; VOL. 38; NO 9; PP. 1609-1616; BIBL. 23REF.Article

Correlation of surface properties with conformational stabilities of wild-type and six mutant tryptophan synthase α-subunits substituted at the same positionKATO, A; YUTANI, K.Protein engineering (Print). 1988, Vol 2, Num 2, pp 153-156, issn 0269-2139Article

EFFECT OF SIMPLE AMINO ACID SUBSTITUTIONS AT THE SAME POSITION ON STABILITY OF A TWO-DOMAIN PROTEINYUTANI K; OGASAHARA K; KIMURA A et al.1982; J. MOL. BIOL.; ISSN 0022-2836; GBR; DA. 1982; VOL. 160; NO 2; PP. 387-390; BIBL. 15 REF.Article

EFFECT OF A SINGLE AMINO ACID SUBSTITUTION ON THE NEAR-ULTRAVIOLET CD SPECTRA OF TRYPTOPHAN SYNTHASE ALPHA -SUBUNITYUTANI K; OGASAHARA K; SUZUKI M et al.1980; J. BIOCHEM.; JPN; DA. 1980; VOL. 87; NO 1; PP. 117-121; BIBL. 16 REF.Article

EFFECT OF A SINGLE AMINO ACID SUBSTITUTION ON STABILITY OF CONFORMATION OF A PROTEIN.YUTANI K; OGASAHARA K; SUGINO Y et al.1977; NATURE; G.B.; DA. 1977; VOL. 267; NO 5608; PP. 274-275; BIBL. 18 REF.Article

STATE OF TYR49 IN A MUTANT TRYPTOPHAN SYNTHASE ALPHA -SUBUNIT SUBSTITUTED AT POSITION 49OGASAHARA K; YUTANI K; SUZUKI M et al.1980; J. BIOCHEM. (TOKYO); ISSN 0021-924X; JPN; DA. 1980; VOL. 88; NO 6; PP. 1733-1738; BIBL. 17 REF.Article

Evaluation of lung cancer by ^99mTc-tetrofosmin SPECT: Comparison with [¹⁸f]FDG-PETTATSUMI, M; YUTANI, K; NISHIMURA, T et al.Journal of computer assisted tomography. 2000, Vol 24, Num 4, pp 574-580, issn 0363-8715Article

Effect of patients' being prone during FDG PET for the diagnosis of breast cancerYUTANI, K; TATSUMI, M; UEHARA, T et al.American journal of roentgenology (1976). 1999, Vol 173, Num 5, pp 1337-1339, issn 0361-803XArticle

Technetium-99m HL91 uptake as a tumour hypoxia marker : relationship to tumour blood flowTATSUMI, M; YUTANI, K; KUSUOKA, H et al.European journal of nuclear medicine. 1999, Vol 26, Num 2, pp 91-94, issn 0340-6997Article

Characteristics of magnetic bearings biased with permanent magnets in the statorFUKATA, S; YUTANI, K; KOUYA, Y et al.JSME international journal. Series C, Mechanical systems, machine elements and manufacturing. 1998, Vol 41, Num 2, pp 206-213, issn 1344-7653Article

Absence of the thermal transition in apo-α-lactalbumin in the molten globule state : a study by differential scanning microcalorimetryYUTANI, K; OGASAHARA, K; KUWAJIMA, K et al.Journal of molecular biology. 1992, Vol 228, Num 2, pp 347-350, issn 0022-2836Article

Assignment of tyrosine resonances in the ¹H-NMR spectrum of tryptophan synthase α-subunit : monitoring conformational changes due to substitutions at position 49SAWADA, S; AKUTSU, H; OGASAHARA, K et al.European journal of biochemistry (Print). 1990, Vol 189, Num 3, pp 667-673, issn 0014-2956, 7 p.Article

Effects of proline mutations on the unfolding and refolding of human lysozyme : the slow refolding kinetic phase does not result from proline cis-trans isomerizationHERNING, T; YUTANI, K; TANIYAMA, Y et al.Biochemistry (Easton). 1991, Vol 30, Num 41, pp 9882-9891, issn 0006-2960Article

Further examination of the intermediate state in the denaturation of the tryptophan synthase α subunit : evidence that the equilibrium denaturation intermediate is a molten globuleOGASAHARA, K; MATSUSHITA, E; YUTANI, K et al.Journal of molecular biology. 1993, Vol 234, Num 4, pp 1197-1206, issn 0022-2836Article

Entropic stabilization of a mutant human lysozyme induced by calcium bindingKUROKI, R; KAWAKITA, S; NAKAMURA, H et al.Proceedings of the National Academy of Sciences of the United States of America. 1992, Vol 89, Num 15, pp 6803-6807, issn 0027-8424Article

Thermodynamic changes in the binding of Ca²⁺ to a mutant human lysozyme (D86/92) : enthalpy-entropy compensation observed upon Ca²⁺ binding to proteinsKUROKI, R; NITTA, K; YUTANI, K et al.The Journal of biological chemistry (Print). 1992, Vol 267, Num 34, pp 24297-24301, issn 0021-9258Article

Evidence that glutamic acid 49 of tryptophan synthase α subunit is a catalytic residue: inactive mutant proteins substituted at position 49 bind ligands and transmit ligand-dependent effects to the β subunitWILSON MILES, E; MCPHIE, P; YUTANI, K et al.The Journal of biological chemistry (Print). 1988, Vol 263, Num 18, pp 8611-8614, issn 0021-9258Article

Comparison of dual-head Coincidence gamma camera FDG imaging with FDG PET in detection of breast cancer and axillary lymph node metastasisYUTANI, K; TATSUMI, M; SHIBA, E et al.The Journal of nuclear medicine (1978). 1999, Vol 40, Num 6, pp 1003-1010, issn 0161-5505Article

Scanning calorimetric study of tryptophan synthase α-subunits from Escherichia coli, Salmonella typhimurium, and an interspecies hybridSUGISAKI, Y; OGASAHARA, K; MILES, E. W et al.Thermochimica acta. 1990, Vol 163, pp 117-122, issn 0040-6031, 6 p.Conference Paper

Role of tyrosine-80 in the stability of kanamycin nucleotidyltransferase analyzed by site-directed mutagenesisMATSUMURA, M; YAHANDA, S; YASUMURA, S et al.European journal of biochemistry (Print). 1988, Vol 171, Num 3, pp 715-720, issn 0014-2956Article

Proton nuclear magnetic resonance studies on the wild-type and single amino acid substituted tryptophan synthase α-subunitsYUTANI, K; AKUTSU, H; OGASAHARA, K et al.Biochemistry (Easton). 1987, Vol 26, Num 18, pp 5666-5671, issn 0006-2960Article

Assessment of reperfused myocardium using a new ischaemia-avid imaging agent, technetium-99m HL91 : comparison with myocardial glucose uptakeFUKUCHI, K; KUSUOKA, H; YUTANI, K et al.European journal of nuclear medicine. 1998, Vol 25, Num 4, pp 361-366, issn 0340-6997Article

Studies on interdomain interaction of 3-isopropylmalate dehydrogenase from an extreme thermophile, Thermus thermophilus, by constructing chimeric enzymesNUMATA, K; HAYASHI-IWASAKI, Y; YUTANI, K et al.Extremophiles (Tokyo. Print). 1999, Vol 3, Num 4, pp 259-262, issn 1431-0651Article