K. Ogasahara

发表

Thermal stability of pyrrolidone carboxyl peptidases from the hyperthermophilic Archaeon, Pyrococcus furiosus.

K. Yutani, K. Ogasahara, N. N. Khechinashvili, 2001, European journal of biochemistry.

Dependence of conformational stability on hydrophobicity of the amino acid residue in a series of variant proteins substituted at a unique position of tryptophan synthase alpha subunit.

T Tsujita, K. Yutani, K. Ogasahara, 1987, Proceedings of the National Academy of Sciences of the United States of America.

Role of charged residues in stabilization of Pyrococcus horikoshii CutA1, which has a denaturation temperature of nearly 150 °C

N. Kunishima, Hitoshi Yamamoto, E. Katoh, 2012, The FEBS journal.

Contribution of hydrophobic residues to the stability of human lysozyme: calorimetric studies and X-ray structural analysis of the five isoleucine to valine mutants.

M. Oobatake, Y. Yamagata, E. Kanaya, 1996, Journal of molecular biology.

Large conformational changes in the Escherichia coli tryptophan synthase β2 subunit upon pyridoxal 5′‐phosphate binding

T. Tsukihara, K. Yutani, K. Ogasahara, 2010, The FEBS journal.

Assignment of tyrosine resonances in the 1H‐NMR spectrum of tryptophan synthase α‐subunit

K. Yutani, K. Ogasahara, H. Akutsu, 1990 .

Role of Tyr Residues in the Contact Region of Anti-lysozyme Monoclonal Antibody HyHEL10 for Antigen Binding (*)

K Watanabe, K. Tsumoto, K. Watanabe, 1995, The Journal of Biological Chemistry.

Origin of the mutual activation of the alpha and beta 2 subunits in the alpha 2 beta 2 complex of tryptophan synthase. Effect of alanine or glycine substitutions at proline residues in the alpha subunit.

K. Hiraga, K. Yutani, K. Ogasahara, 1992, The Journal of biological chemistry.

X-ray crystalline structures of pyrrolidone carboxyl peptidase from a hyperthermophile, Pyrococcus furiosus, and its cys-free mutant.

M. Ota, T. Mizushima, K. Yutani, 2001, Journal of biochemistry.

Characterization of soluble artificial proteins with random sequences

T. Yomo, I. Urabe, K. Yutani, 1998, FEBS letters.

High-resolution crystals of methionine aminopeptidase from Pyrococcus furiosus obtained by water-mediated transformation.

H. Oki, C. P. Libeu, T. Tsukihara, 1998, Journal of structural biology.

Crystal structure of Ufc1, the Ufm1-conjugating enzyme.

T. Mizushima, T. Yamane, Keiji Tanaka, 2007, Biochemical and biophysical research communications.

Absence of the thermal transition in apo-alpha-lactalbumin in the molten globule state. A study by differential scanning microcalorimetry.

K. Kuwajima, K. Yutani, K. Ogasahara, 1992, Journal of molecular biology.

Folding mechanism of mutant human lysozyme C77/95A with increased secretion efficiency in yeast.

K. Yutani, K. Ogasahara, M. Kikuchi, 1992, The Journal of biological chemistry.

Effect of amino acid substitutions on conformational stability of a protein.

K. Yutani, K. Ogasahara, Y. Sugino, 1985, Advances in biophysics.

Thermodynamic analysis of unusually thermostable CutA1 protein from human brain and its protease susceptibility.

N. Kunishima, Hitoshi Yamamoto, E. Katoh, 2015, Journal of biochemistry.

Studies on Thermophilic α-Amylase from Bacillus stearothermophilus II. Thermal Stability of Thermophilic α-Amylase

K. Ogasahara, T. Isemura, A. Imanishi, 1970 .

Properties and subunit composition of the pig heart 2-oxoglutarate dehydrogenase.

K. Ogasahara, N. Tanaka, M. Hamada, 1974, The Journal of biological chemistry.

Mammalian α-Keto Acid Dehydrogenase Complexes VIII. PROPERTIES AND SUBUNIT COMPOSITION OF THE PIG HEART LIPOATE SUCCINYLTRANSFERASE

K. Ogasahara, N. Tanaka, M. Hamada, 1974 .

The process of amyloid-like fibril formation by methionine aminopeptidase from a hyperthermophile, Pyrococcus furiosus.

K. Namba, Y. Yamagata, K. Yutani, 2000, Biochemistry.

[Circular dichroism].

K. Yutani, K. Ogasahara, 2004, Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme.

Conformational changes in the tryptophan synthase from a hyperthermophile upon α2β2 complex formation : Crystal structure of the complex

T. Tsukihara, M. Ishida, Y. Yamagata, 2005 .

Properties and subunit structure of pig heart pyruvate dehydrogenase.

K. Ogasahara, M. Hamada, T. Kanzaki, 1976, Journal of biochemistry.

Purification properties and subunit composition of pig heart lipoate acetyltransferase.

K. Ogasahara, N. Tanaka, M. Hamada, 1975, Journal of biochemistry.

Comparison of CD spectra in the aromatic region on a series on variant proteins substituted at a unique position of tryptophan synthase α‐subunit

K. Yutani, K. Ogasahara, S. Sawada, 1989, Proteins.

Comparison of Denaturation by Guanidine Hydrochloride of the Wild Type Tryptophan Synthase α-Subunit of Escherichia coli and Two Mutant Proteins (Glu 49—Met or Gln)

K. Ogasahara, Y. Sugino, Minoru Suzuki, 1979 .

Effect of a single amino acid substitution on stability of conformation of a protein

K. Yutani, K. Ogasahara, Y. Sugino, 1977, Nature.

Effect of the order of antibody variable regions on the expression of the single-chain HyHEL10 Fv fragment in E. coli and the thermodynamic analysis of its antigen-binding properties.

K. Tsumoto, K. Yutani, K. Ogasahara, 1994, Biochemical and biophysical research communications.

The intracellular region of ClC-3 chloride channel is in a partially folded state and a monomer.

A. Nakagawa, K. Ogasahara, S. Li, 2006, Journal of biochemistry.

Effects of amino acid substitution on the physicochemical properties of artificial proteins with random sequences.

T. Yomo, N. Tokuriki, I. Urabe, 2001, Journal of bioscience and bioengineering.

The unusually slow unfolding rate causes the high stability of pyrrolidone carboxyl peptidase from a hyperthermophile, Pyrococcus furiosus: equilibrium and kinetic studies of guanidine hydrochloride-induced unfolding and refolding.

K. Yutani, K. Ogasahara, M. Nakamura, 1998, Biochemistry.

Strategy for cold adaptation of the tryptophan synthase α subunit from the psychrophile Shewanella frigidimarina K14-2: crystal structure and physicochemical properties.

N. Urano, M. Ishida, Daisuke Mitsuya, 2014, Journal of Biochemistry (Tokyo).

Remarkable improvement in the heat stability of CutA1 from Escherichia coli by rational protein design.

M. Ota, N. Kunishima, B. Bagautdinov, 2010, Journal of biochemistry.

Completely buried, non-ion-paired glutamic acid contributes favorably to the conformational stability of pyrrolidone carboxyl peptidases from hyperthermophiles.

Y. Yamagata, K. Yutani, K. Ogasahara, 2006, Biochemistry.

Stabilization due to dimer formation of phosphoribosyl anthranilate isomerase from Thermus thermophilus HB8: X-ray Analysis and DSC experiments.

N. Kunishima, S. Yokoyama, K. Yutani, 2005, Journal of biochemistry.

The crystal structure of the tryptophan synthase beta subunit from the hyperthermophile Pyrococcus furiosus. Investigation of stabilization factors.

M. Ota, M. Ishida, M. Ikeguchi, 2004, European journal of biochemistry.

The unusually slow relaxation kinetics of the folding-unfolding of pyrrolidone carboxyl peptidase from a hyperthermophile, Pyrococcus furiosus.

K. Yutani, K. Ogasahara, J. Kaushik, 2002, Journal of molecular biology.

Stimulated Interaction between α and β Subunits of Tryptophan Synthase from Hyperthermophile Enhances Its Thermal Stability*

M. Ishida, K. Yutani, K. Ogasahara, 2003, The Journal of Biological Chemistry.

Thermal Conversion from Low- to High-activity Forms of Catalase I from Bacillus stearothermophilus *

T. Yomo, I. Urabe, K. Yutani, 1997, The Journal of Biological Chemistry.

Assignment of tyrosine resonances in the 1H-NMR spectrum of tryptophan synthase alpha-subunit. Monitoring conformational changes due to substitutions at position 49.

K. Yutani, K. Ogasahara, H. Akutsu, 1990, European journal of biochemistry.

Structural Evidence for Entropic Contribution of Salt Bridge Formation to a Protein Antigen-Antibody Interaction

K. Tsumoto, K. Yutani, K. Ogasahara, 2001, The Journal of Biological Chemistry.

Entropic Stabilization of the Tryptophan Synthase α-Subunit from a Hyperthermophile, Pyrococcus furiosus

Haruki Nakamura, M. Ishida, A. Nakagawa, 2001, The Journal of Biological Chemistry.

Further examination of the intermediate state in the denaturation of the tryptophan synthase alpha subunit. Evidence that the equilibrium denaturation intermediate is a molten globule.

K. Yutani, K. Ogasahara, E. Matsushita, 1993, Journal of molecular biology.

Effect of single amino acid substitutions at the same position on stability of a two-domain protein.

K. Yutani, K. Ogasahara, Y. Sugino, 1982, Journal of molecular biology.

Stabilization mechanism of the tryptophan synthase alpha-subunit from Thermus thermophilus HB8: X-ray crystallographic analysis and calorimetry.

M. Ota, N. Kunishima, K. Yutani, 2005, Journal of biochemistry.

Unfolding-refolding kinetics of the tryptophan synthase alpha subunit by CD and fluorescence measurements.

K. Yutani, K. Ogasahara, 1994, Journal of molecular biology.

Thermodynamics of protein denaturation at temperatures over 100 °C: CutA1 mutant proteins substituted with hydrophobic and charged residues

N. Kunishima, Y. Joti, K. Yutani, 2015, Scientific Reports.

Scanning calorimetric study of tryptophan synthase α-subunits from Escherichia coli, Salmonella typhimurium, and an interspecies hybrid

K. Yutani, K. Ogasahara, E. W. Miles, 1990 .

Thermal denaturation of tryptophan synthase alpha-subunit. Comparison of the values of thermodynamic parameters of unfolding obtained from van't Hoff analysis of CD measurement with those from calorimetry.

K. Yutani, K. Ogasahara, Y. Sugino, 2009, International journal of peptide and protein research.

Comparison of thermostable alpha-amylases from B. stearothermophilus grown at different temperatures.

K. Yutani, K. Ogasahara, I. Sasaki, 1973, Journal of biochemistry.

The structure, stability, and folding process of amyloidogenic mutant human lysozyme.

Kazufumi Takano, K. Takano, K. Yutani, 1996 .

Calorimetric Observation of a GroEL-Protein Binding Reaction with Little Contribution of Hydrophobic Interaction*

H. Taguchi, Masasuke Yoshida, K. Yutani, 1997, The Journal of Biological Chemistry.

Structure of Physarum polycephalum cytochrome b5 reductase at 1.56 A resolution.

T. Tsukihara, K. Ogasahara, Y. Minami, 2007, Acta crystallographica. Section F, Structural biology and crystallization communications.

Interaction of hydrophobic probes with the apoenzyme of pig heart lipoamide dehydrogenase.

K. Ogasahara, M. Hamada, K. Koike, 1976, Journal of Biochemistry (Tokyo).

Crystal structure of methionine aminopeptidase from hyperthermophile, Pyrococcus furiosus.

H. Oki, T. Tsukihara, T. Tahirov, 1998, Journal of molecular biology.

Tryptophan synthase alpha subunit glutamic acid 49 is essential for activity. Studies with 19 mutants at position 49.

K. Yutani, K. Ogasahara, T. Tsujita, 1987, The Journal of biological chemistry.

Crystal Structural and Functional Analysis of the Putative Dipeptidase from Pyrococcus horikoshii OT3

N. Kunishima, S. Yokoyama, K. Yutani, 2009, Journal of biophysics.

Role of Salt Bridge Formation in Antigen-Antibody Interaction

K. Tsumoto, K. Yutani, K. Ogasahara, 1996, The Journal of Biological Chemistry.

Contribution to antibody-antigen interaction of structurally perturbed antigenic residues upon antibody binding.

K Watanabe, K. Tsumoto, K. Watanabe, 1994, The Journal of biological chemistry.

Equilibrium and kinetic analyses of unfolding and refolding for the conserved proline mutants of tryptophan synthase alpha subunit.

K. Yutani, K. Ogasahara, 1997, Biochemistry.

Effect of guanidine hydrochloride on the holo- and apo-enzymes of pig heart lipoamide dehydrogenase.

K. Ogasahara, M. Hamada, K. Koike, 1976, Journal of biochemistry.

Folding pathway of Escherichia coli ribonuclease HI: a circular dichroism, fluorescence, and NMR study.

M. Oobatake, S. Kanaya, K. Yutani, 1995, Biochemistry.

Thermodynamic basis for the stabilities of three CutA1s from Pyrococcus horikoshii,Thermus thermophilus, and Oryza sativa, with unusually high denaturation temperatures.

S. Yokoyama, Hitoshi Yamamoto, E. Katoh, 2008, Biochemistry.

Hyper‐thermostability of CutA1 protein, with a denaturation temperature of nearly 150 °C

S. Yokoyama, E. Katoh, B. Bagautdinov, 2006 .

Electrostatic stabilization in methionine aminopeptidase from hyperthermophile Pyrococcus furiosus.

K. Yutani, K. Ogasahara, S. Tsunasawa, 1998, Biochemistry.

Experimental verification of the 'stability profile of mutant protein' (SPMP) data using mutant human lysozymes.

K Nishikawa, K. Nishikawa, M. Ota, 1999, Protein engineering.

Comparison of denaturation of tryptophan synthase alpha-subunits from Escherichia coli, Salmonella typhimurium, and an interspecies hybrid.

K. Yutani, K. Ogasahara, E. W. Miles, 1984, Archives of biochemistry and biophysics.

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 domains.

K. Yutani, K. Ogasahara, E. W. Miles, 1982, Biochemistry.

Hyper-thermostability of CutA1 protein, with a denaturation temperature of nearly 150 degrees C.

S. Yokoyama, E. Katoh, B. Bagautdinov, 2006, FEBS letters.

Different Immunoreactivity against Monoclonal Antibodies between Wild-type and Mutant Copper/Zinc Superoxide Dismutase Linked to Amyotrophic Lateral Sclerosis*

Keiichiro Suzuki, T. Ikegami, N. Taniguchi, 2005, Journal of Biological Chemistry.

Proton nuclear magnetic resonance studies on the wild-type and single amino acid substituted tryptophan synthase alpha-subunits.

Y. Kyōgoku, K. Yutani, K. Ogasahara, 1987, Biochemistry.

Novel selection method for engineered antibodies using the mechanism of Fv fragment stabilization in the presence of antigen.

K. Tsumoto, Teruyuki Nagamune, K. Yutani, 1997, Protein engineering.

Transition State of Heat Denaturation of Methionine Aminopeptidase from a Hyperthermophile

K. Yutani, K. Ogasahara, S. Potekhin, 2000 .

Role of conserved proline residues in stabilizing tryptophan synthase α subunit: Analysis by mutants with alanine or glycine

K. Yutani, K. Ogasahara, Yoshiko Sugisaki, 1991, Proteins.

Effect of amino acid residues on conformational stability in eight mutant proteins variously substituted at a unique position of the tryptophan synthase alpha-subunit.

K. Aoki, K. Yutani, K. Ogasahara, 1984, The Journal of biological chemistry.

Amino-terminally formylated tryptophan synthase alpha-subunit produced by the trp operon cloned in a plasmid vector.

K. Yutani, K. Ogasahara, Y. Sugino, 1980, Journal of Biochemistry (Tokyo).

Effect of single amino acid substitutions on the protease susceptibility of tryptophan synthase a subunit

K. Yutani, K. Ogasahara, Y. Sugino, 1985 .

pH dependence of stability of the wild-type tryptophan synthase α-subunit and two mutant proteins (Glu49 → Met or Gln)

K. Yutani, K. Ogasahara, Y. Sugino, 1980 .

Conformational changes in the α-subunit coupled to binding of the β2-Subunit of tryptophan synthase from Escherichia coli: Crystal structure of the tryptophan synthase α-subunit alone

T. Tsukihara, K. Yutani, K. Ogasahara, 2005 .

Unusually slow denaturation and refolding processes of pyrrolidone carboxyl peptidase from a hyperthermophile are highly cooperative: real-time NMR studies.

K. Yutani, K. Ogasahara, Satoshi Iimura, 2004, Biochemistry.

pH dependence of stability of the wild-type tryptophan synthase alpha-subunit and two mutant proteins (Glu49 replaced by Met or Gln).

K. Yutani, K. Ogasahara, Y. Sugino, 1980, Journal of molecular biology.

Comparison of denaturation by guanidine hydrochloride of the wild type tryptophan synthase alpha-subunit of Escherichia coli and two mutant protein (Glu 49 replaced by Met or Gln).

K. Yutani, K. Ogasahara, Y. Sugino, 1979, Journal of biochemistry.

Accumulation of Amino-terminally Formylated Tryptophan Synthase in Amplifying Conditions

M. Taketani, K. Yutani, K. Ogasahara, 1983 .

Structure of lysozyme. XII. Effect of pH on the stability of lysozyme.

K. Ogasahara, K. Hamaguchi, 1967, Journal of biochemistry.