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au.\*:("YUTANI K")

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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

PH DEPENDENCE OF STABILITY OF THE WILD-TYPE TRYPTOPHAN SYNTHASE ALPHA -SUBUNIT AND TWO MUTANT PROTEINS (GLU 49->MET OR GLN)YUTANI K; OGASAHARA K; SUGINO Y et al.1980; J. MOL. BIOL.; ISSN 0022-2836; GBR; DA. 1980; VOL. 144; NO 4; PP. 455-465; BIBL. 13 REF.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

Unfolding-refolding kinetics of the tryptophan synthase α subunit by CD and fluorescence measurementsOGASAHARA, K; YUTANI, K.Journal of molecular biology. 1994, Vol 236, Num 4, pp 1227-1240, issn 0022-2836Article

CALORIMETRIC STUDY OF TRYPTOPHAN SYNTHASE ALPHA -SUBUNIT AND TWO MUTANT PROTEINSYUTANI K; KHECHINASHVILI NN; LAPSHINA EA et al.1982; INT. J. PEPT. PROTEIN RES.; ISSN 0367-8377; DNK; DA. 1982; VOL. 20; NO 4; PP. 331-336; BIBL. 19 REF.Article

AMINO-TERMINALLY FORMYLATED TRYPTOPHAN SYNTHASE ALPHA -SUBUNIT PRODUCED BY THE TRP OPERON CLONED IN A PLASMID VECTORSUGINO Y; TSUNASAWA S; YUTANI K et al.1980; J. BIOCHEM.; JPN; DA. 1980; VOL. 87; NO 1; PP. 351-354; BIBL. 15 REF.Article

ROLE OF CALCIUM IONS IN THE THERMOSTABILITY OF THERMOLYSIN AND BACILLUS SUBTILIS VAR. AMYLOSACCHARITICUS NEUTRAL PROTEASE.TAJIMA M; URABE I; YUTANI K et al.1976; EUROP. J. BIOCHEM.; GERM.; DA. 1976; VOL. 64; PP. 243-247; BIBL. 15 REF.Article

COMPARISON OF DENATURATION BY GUANIDINE HYDROCHLORIDE OF THE WILD TYPE TRYPTOPHAN SYNTHASE ALPHA -SUBUNIT OF ESCHERICHIA COLI AND TWO MUTANT PROTEINS (GLU 49->MET OR GLN)YUTANI K; OGASAHARA K; SUZUKI M et al.1979; J. BIOCHEM.; JPN; DA. 1979; VOL. 85; NO 4; PP. 915-921; BIBL. 25 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

NMR EVIDENCE FOR THE STEPWISE UNFOLDING OF THE TWO DOMAINS OF TRYPTOPHAN SYNTHASE ALPHA -SUBUNITIWAHASHI H; YUTANI K; OGASAHARA K et al.1983; BIOCHIMICA ET BIOPHYSICA ACTA; ISSN 0006-3002; NLD; DA. 1983; VOL. 744; NO 2; PP. 189-192; BIBL. 10 REF.Article

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

Folding mechanism of mutant human lysozyme C77/95A with increased secretion efficiency in yeastTANIYAMA, Y; OGASAHARA, K; YUTANI, K et al.The Journal of biological chemistry (Print). 1992, Vol 267, Num 7, pp 4619-4624, issn 0021-9258Article

Role of conserved proline residues in stabilizing tryptophan synthase α subunit: analysis by mutant with alanine or glycineYUTANI, K; HAYASHI, S; SUGISAKI, Y et al.Proteins. 1991, Vol 9, Num 2, pp 90-98, issn 0887-3585, 9 p.Article

Comparison of CD spectra in the aromatic region on a series of variant proteins substituted at a unique position of tryptophan synthase α-subunitOGASAHARA, K; SAWADA, S; YUTANI, K et al.Proteins. 1989, Vol 5, Num 3, pp 211-217, issn 0887-3585, 7 p.Article

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