T. Yoshimoto

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.

Crystallization and preliminary X-ray characterization of prolyl tripeptidyl aminopeptidase from Porphyromonas gingivalis.

T. Yoshimoto, Takashi Ito, Yue Xu, 2005, Acta crystallographica. Section F, Structural biology and crystallization communications.

Sequencing and high expression of aminopeptidase P gene from Escherichia coli HB101.

T. Yoshimoto, K. Osatomi, T. Honda, 1989, Journal of biochemistry.

Protease II from Escherichia coli: sequencing and expression of the enzyme gene and characterization of the expressed enzyme.

T. Yoshimoto, A. Kanatani, D. Tsuru, 1991, Journal of biochemistry.

A cysteine residue near the propionate side chain of heme is the radical site in ascorbate peroxidase

K. Oda, K. Kanaori, T. Yoshimoto, 2008, The FEBS journal.

Degradation of beta-casomorphin-5 by proline-specific-endopeptidase (PSE) and post-proline- cleaving-enzyme (PPCE). Comparative studies of the beta-casomorphin-5 cleavage by dipeptidyl-peptidase IV.

T. Yoshimoto, G. Fischer, K. Neubert, 1982, Die Pharmazie.

Creatine amidinohydrolase of Pseudomonas putida: crystallization and some properties.

T. Yoshimoto, D. Tsuru, I. Oka, 1976, Archives of biochemistry and biophysics.

Inhibitors of Plasmodium falciparum methionine aminopeptidase 1b possess antimalarial activity

Jun O. Liu, C. Chong, D. Sullivan, 2006, Proceedings of the National Academy of Sciences.

Crystal structures of the binary and ternary complexes of 7 alpha-hydroxysteroid dehydrogenase from Escherichia coli.

T. Nonaka, T. Yoshimoto, T. Tanabe, 1996, Biochemistry.

Crystal structure of serine dehydrogenase from Escherichia coli: important role of the C-terminal region for closed-complex formation.

T. Yoshimoto, Y. Nakajima, Kiyoshi Ito, 2011, Journal of biochemistry.

Post-proline dipeptidyl aminopeptidase (dipeptidyl aminopeptidase IV) from lamb kidney. Purification and some enzymatic properties.

T. Yoshimoto, R. Walter, 1977, Biochimica et biophysica acta.

Postproline cleaving enzyme: identification as serine protease using active site specific inhibitors.

T. Yoshimoto, R. Walter, R. Orlowski, 1977, Biochemistry.

Purification and properties of a novel glycine amino peptidase from Actinomucor elegans and its potential application

T. Yoshimoto, X. Ma, X. Zhou, 2004, Journal of applied microbiology.

Creatinine Decomposing Enzymes in Pseudomonas putida

T. Yoshimoto, D. Tsuru, I. Oka, 1976 .

Sarcosine Dehydrogenase from Pseudomonas putida: Purification and Some Properties

T. Yoshimoto, D. Tsuru, I. Oka, 1979 .

Creatinine amidohydrolase (creatininase) from Pseudomonas putida. Purification and some properties.

T. Yoshimoto, M. Ando, D. Tsuru, 1979, Journal of biochemistry.

Prolyl oligopeptidase is a glyceraldehyde-3-phosphate dehydrogenase-binding protein that regulates genotoxic stress-induced cell death.

T. Yoshimoto, M. Sakaguchi, M. Takaoka, 2013, The international journal of biochemistry & cell biology.

Continuous assays for meprin alpha and beta using prolyl tripeptidyl aminopeptidase (PtP) from Porphyromonas gingivalis.

T. Yoshimoto, S. Schilling, M. Wermann, 2018, Analytical biochemistry.

Crystal structure of formaldehyde dehydrogenase

T. Yoshimoto, N. Tanaka, Kazuo T. Nakamura, 2002 .

Crystal structure of prolyl aminopeptidase from Serratia marcescens.

T. Yoshimoto, N. Tanaka, T. Kabashima, 1999, Journal of biochemistry.

Prolyl aminopeptidase is not a sulfhydryl enzyme: identification of the active serine residue by site-directed mutagenesis.

T. Yoshimoto, K. Ito, A. Kitazono, 1994, Journal of biochemistry.

Cloning and high-level expression of the glutathione-independent formaldehyde dehydrogenase gene from Pseudomonas putida

M. Takahashi, T. Yoshimoto, K. Ito, 1994, Journal of bacteriology.

Substitution of Glu122 by glutamine revealed the function of the second water molecule as a proton donor in the binuclear metal enzyme creatininase.

T. Yoshimoto, K. Yamashita, H. Oyama, 2010, Journal of molecular biology.

Structure of aminopeptidase N from Escherichia coli complexed with the transition‐state analogue aminophosphinic inhibitor PL250

B. Roques, T. Yoshimoto, Y. Nakajima, 2009, Acta crystallographica. Section D, Biological crystallography.

Proline-specific dipeptidyl aminopeptidase from Flavobacterium meningosepticum.

T. Yoshimoto, D. Tsuru, 1982, Journal of biochemistry.

Studies on bacterial proteases. Some enzymatic and physiochemical properties of the alkaline protease from Bacillus natto.

T. Yoshimoto, D. Tsuru, J. Fukumoto, 2009, International journal of protein research.

Studies on bacterial proteases. Chemical modification of tyrosyl residues of neutral subtilopeptidase amylosacchariticus.

T. Yoshimoto, T. Yoshida, D. Tsuru, 2009, International journal of protein research.

Cloning, sequencing, and high expression of the proline iminopeptidase gene from Bacillus coagulans

T. Yoshimoto, D. Tsuru, A. Kitazono, 1992, Journal of bacteriology.

Protease II from Moraxella lacunata: cloning, sequencing, and expression of the enzyme gene, and crystallization of the expressed enzyme.

T. Yoshimoto, K. Ito, S. Inoue, 1995, Journal of biochemistry.

Processing of pro-colipase and trypsinogen by pancreatic dipeptidyl peptidase IV.

A. Feller, T. Yoshimoto, C. Erlanson‐Albertsson, 1986, Biomedica biochimica acta.

Crystallization and preliminary X-ray characterization of D-3-hydroxybutyrate dehydrogenase from Pseudomonas fragi.

T. Yoshimoto, Yue Xu, Y. Nakajima, 2005, Acta crystallographica. Section F, Structural biology and crystallization communications.

Preliminary crystallographic studies of the creatinine amidohydrolase from Pseudomonas putida.

T. Yoshimoto, K. Yamashita, N. Tanaka, 2002, Acta crystallographica. Section D, Biological crystallography.

An Arabidopsis FAD pyrophosphohydrolase, AtNUDX23, is involved in flavin homeostasis.

M. Tamoi, S. Shigeoka, T. Yoshimoto, 2012, Plant & cell physiology.

Cloning of L-amino acid deaminase gene from Proteus vulgaris.

T. Yoshimoto, K. Ito, E. Takahashi, 1999, Bioscience, biotechnology, and biochemistry.

Substrate specificity of aminopeptidase P from Escherichia coli: comparison with membrane-bound forms from rat and bovine lung.

W. Simmons, T. Yoshimoto, A. T. Orawski, 1994, Archives of biochemistry and biophysics.

Prolyl oligopeptidase participates in cell cycle progression in a human neuroblastoma cell line.

T. Yoshimoto, E. Matsumura, M. Sakaguchi, 2011, Biochemical and biophysical research communications.

CPT-11 converting enzyme from rat serum: purification and some properties.

T. Yoshimoto, T. Yokokura, D. Tsuru, 1991, Journal of pharmacobio-dynamics.

Lyophyllum cinerascens aminopeptidase: purification and enzymatic properties.

T. Yoshimoto, D. Tsuru, A. K. Abdus Sattar, 1989, Archives of biochemistry and biophysics.

Studies on prolyl endopeptidase from carrot (Daucus carota): purification and enzymatic properties

T. Yoshimoto, D. Tsuru, A. Sattar, 1987 .

Pyroglutamyl-peptidase from Bacillus amyloliquefaciens: An improved purification method and some properties of the enzyme

T. Yoshimoto, K. Fujiwara, D. Tsuru, 1984 .

Proline specific endo- and exopeptidases

W. Simmons, T. Yoshimoto, R. Walter, 1980, Molecular and Cellular Biochemistry.

Aminopeptidase N (proteobacteria alanyl aminopeptidase) from Escherichia coli: Crystal structure and conformational change of the methionine 260 residue involved in substrate recognition

T. Yoshimoto, Takashi Ito, Y. Onohara, 2006 .

Oligopeptidase B: protease II from Escherichia coli.

T. Yoshimoto, D. Tsuru, 1994, Methods in enzymology.

Prolyl endopeptidase from Aeromonas hydrophila: cloning, sequencing, and expression of the enzyme gene, and characterization of the expressed enzyme.

T. Yoshimoto, A. Kanatani, D. Tsuru, 1993, Journal of biochemistry.

Prolyl endopeptidase from Flavobacterium meningosepticum: cloning and sequencing of the enzyme gene.

T. Yoshimoto, A. Kanatani, D. Tsuru, 1991, Journal of biochemistry.

Protamine: a unique and potent inhibitor of oligopeptidase B

T. Yoshimoto, A. Tsuji, K. Yuasa, 2006, Journal of peptide science : an official publication of the European Peptide Society.

Postproline cleaving enzyme: kinetic studies of size and stereospecificity of its active site.

T. Yoshimoto, R. Walter, 1978, Biochemistry.

Prolyl endopeptidase inhibitors derived from actinomycetes.

T. Yoshimoto, M. Yoshihama, K. Kimura, 1997, Bioscience, biotechnology, and biochemistry.

Post-proline cleaving enzyme. Synthesis of a new fluorogenic substrate and distribution of the endopeptidase in rat tissues and body fluids of man.

T. Yoshimoto, M. Koida, R. Walter, 1979, Biochimica et biophysica acta.

Glycerol transport and phosphoenolpyruvate-dependent enzyme I- and HPr-catalysed phosphorylation of glycerol kinase in Thermus flavus.

J. Deutscher, T. Yoshimoto, S. Poncet, 1999, Microbiology.

Purification and characterization of thermostable glycerol kinase from Thermus flavus

T. Yoshimoto, Kiyoshi Ito, T. Kabashima, 1997 .

Novel Aminopeptidase Specific for Glycine from Actinomucor elegans

T. Yoshimoto, Kiyoshi Ito, Hua-Shan Huang, 2003, Bioscience, biotechnology, and biochemistry.

Extracellular tyrosinase from Streptomyces sp. KY-453: purification and some enzymatic properties.

T. Yoshimoto, K. Yamamoto, D. Tsuru, 1985, Journal of biochemistry.

STUDIES ON BACTERIAL PROTEASES

T. Yoshimoto, D. Tsuru, J. Fukumoto, 2009 .

Nucleotide sequence of the neutral protease gene from Bacillus subtilis var. amylosacchariticus

T. Yoshimoto, H. Higashi, Sheng Xu, 1990 .

Formaldehyde dehydrogenase from Pseudomonas putida. Purification and some properties.

T. Yoshimoto, M. Ando, S. Shibata, 1979, Journal of biochemistry.

Pyroglutamyl peptidase from chicken liver: purification and some properties.

T. Yoshimoto, K. Fujiwara, K. Sakabe, 1982, Journal of pharmacobio-dynamics.

Crystal structure of formaldehyde dehydrogenase from Pseudomonas putida: the structural origin of the tightly bound cofactor in nicotinoprotein dehydrogenases.

T. Yoshimoto, N. Tanaka, Kazuo T. Nakamura, 2002, Journal of molecular biology.

Post-proline cleaving enzyme and post-proline dipeptidyl aminopeptidase. Comparison of two peptidases with high specificity for proline residues.

T. Yoshimoto, R. Walter, R. Orlowski, 1978, The Journal of biological chemistry.

Cloning and sequencing of the 7 alpha-hydroxysteroid dehydrogenase gene from Escherichia coli HB101 and characterization of the expressed enzyme

T. Yoshimoto, H. Higashi, H. Oyama, 1991, Journal of bacteriology.

Two continuous spectrophotometric assays for methionine aminopeptidase.

T. Yoshimoto, D. Pei, Y. Zhou, 2000, Analytical biochemistry.

Post-proline cleaving enzyme from lamb brain.

W. Simmons, T. Yoshimoto, T. Kita, 1981, Journal of biochemistry.

Colocalization of prolyl endopeptidase and amyloid β-peptide in brains of senescence-accelerated mouse

Akira Kato, T. Yoshimoto, S. Ishiura, 1994, Neuroscience Letters.

Comparison of inhibitory effects of prolinal-containing peptide derivatives on prolyl endopeptidases from bovine brain and Flavobacterium.

T. Yoshimoto, D. Tsuru, K. Kawahara, 1985, Journal of biochemistry.

Isolation and characterization of the prolyl aminopeptidase gene (pap) from Aeromonas sobria: comparison with the Bacillus coagulans enzyme.

T. Yoshimoto, D. Tsuru, A. Kitazono, 1994, Journal of Biochemistry (Tokyo).

[Proline iminopeptidase].

T. Yoshimoto, D. Tsuru, 1984, Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme.

An Aminopeptidase N from Escherichia coli HB101: Purification and Demonstration that the Enzyme Possesses Arylamidase and Peptidase Activitiest(Biological Chemistry)

T. Yoshimoto, D. Tsuru, N. Murayama, 1988 .

An arylamidase from Flavobacterium meningosepticum.

T. Yoshimoto, D. Tsuru, 1981 .

Acetyl-CoA carboxylase from Escherichia coli: gene organization and nucleotide sequence of the biotin carboxylase subunit.

H. Kondo, T. Yoshimoto, T. Tanabe, 1991, Proceedings of the National Academy of Sciences of the United States of America.

[15] Oligopeptidase B: Protease II from Escherichia coli

T. Yoshimoto, D. Tsuru, 1994 .

Characterization of the Promoter Region of Biosynthetic Enzyme Genes Involved in Berberine Biosynthesis in Coptis japonica

Yasuyuki Yamada, F. Sato, T. Yoshimoto, 2016, Front. Plant Sci..

Isoquinoline alkaloid biosynthesis is regulated by a unique bHLH-type transcription factor in Coptis japonica.

Yasuyuki Yamada, F. Sato, T. Yoshimoto, 2011, Plant & cell physiology.

transcription factor in Coptis japonica

Yasuyuki Yamada, F. Sato, T. Yoshimoto, 2011 .

Prolyl aminopeptidase is also present in Enterobacteriaceae: cloning and sequencing of the Hafnia alvei enzyme-gene and characterization of the expressed enzyme.

T. Yoshimoto, K. Ito, T. Kabashima, 1996, Journal of biochemistry.

Proline iminopeptidase from Bacillus coagulans: purification and enzymatic properties.

T. Yoshimoto, D. Tsuru, 1985, Journal of biochemistry.

Proline iminopeptidase from Bacillus megaterium: purification and characterization.

T. Yoshimoto, D. Tsuru, T. Saeki, 1983, Journal of biochemistry.

Unusual Extra Space at the Active Site and High Activity for Acetylated Hydroxyproline of Prolyl Aminopeptidase from Serratia marcescens

M. Sakata, T. Yoshimoto, Yue Xu, 2006, Journal of bacteriology.

Substrate recognition mechanism of prolyl aminopeptidase from Serratia marcescens.

T. Yoshimoto, K. Ito, T. Kabashima, 2000, Journal of biochemistry.

Prolyl aminopeptidase from Serratia marcescens: cloning of the enzyme gene and crystallization of the expressed enzyme.

T. Yoshimoto, K. Ito, T. Kabashima, 1997, Journal of biochemistry.

Dipeptidyl Aminopeptidase IV from Stenotrophomonas maltophilia Exhibits Activity against a Substrate Containing a 4-Hydroxyproline Residue

T. Yoshimoto, E. Takahashi, Heng Zheng, 2008, Journal of bacteriology.

[Biochemistry and structural biology of microbial enzymes and their medical applications].

T. Yoshimoto, 2007, Yakugaku zasshi : Journal of the Pharmaceutical Society of Japan.

Novel inhibitor for prolyl aminopeptidase from Serratia marcescens and studies on the mechanism of substrate recognition of the enzyme using the inhibitor.

Susumi Hatakeyama, Kiyoshi Ito, T. Yoshimoto, 2003, Archives of biochemistry and biophysics.

Structure activity relationship of inhibitors specific for prolyl endopeptidase.

T. Yoshimoto, D. Tsuru, N. Yamamoto, 1991, Agricultural and biological chemistry.

Thiazolidine derivatives as potent inhibitors specific for prolyl endopeptidase.

T. Yoshimoto, D. Tsuru, S. Furukawa, 1988, Journal of biochemistry.

Specific inhibitors for prolyl endopeptidase and their anti-amnesic effect.

T. Yoshimoto, D. Tsuru, H. Kaneto, 1987, Journal of pharmacobio-dynamics.

Post-proline cleaving enzyme (prolyl endopeptidase) from bovine brain.

T. Yoshimoto, T. Kita, D. Tsuru, 1983, Journal of biochemistry.

Purification and characterization of an extracellular prolyl endopeptidase from Agaricus bisporus.

T. Yoshimoto, D. Tsuru, A. Sattar, 1990, Journal of biochemistry.

An inhibitor for post-proline cleaving enzyme; distribution and partial purification from porcine pancreas.

T. Yoshimoto, D. Tsuru, N. Takatsuka, 1982, Journal of pharmacobio-dynamics.

Prolyl oligopeptidase inhibition-induced growth arrest of human gastric cancer cells.

T. Yoshimoto, M. Sakaguchi, M. Takaoka, 2014, Biochemical and biophysical research communications.

Cloning and Sequencing of the Thermus aquaticus Glycerol Facilitator Gene

T. Yoshimoto, Kiyoshi Ito, Hua-Shan Huang, 2002, DNA sequence : the journal of DNA sequencing and mapping.

Crystal Structure of Aminopeptidase N (Proteobacteria Alanyl Aminopeptidase) from Escherichia coli and Conformational Change of Methionine 260 Involved in Substrate Recognition*

T. Yoshimoto, Takashi Ito, Y. Onohara, 2006, Journal of Biological Chemistry.

Crystallization and preliminary X-ray characterization of aminopeptidase N from Escherichia coli

T. Yoshimoto, Takashi Ito, Yue Xu, 2006, Acta crystallographica. Section F, Structural biology and crystallization communications.

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.

Secretion of Escherichia coli Aminopeptidase P in Bacillus subtilis Using the Prepro-Structure Coding Region of Subtilisin Amylosacchariticus

T. Yoshimoto, H. Oyama, D. Tsuru, 1989 .

putida . dehydrogenase gene from Pseudomonas glutathione-independent formaldehyde Cloning and high-level expression of the

M. Takahashi, T. Yoshimoto, K. Ito, 2022 .

The crystal structure of pyroglutamyl peptidase I from Bacillus amyloliquefaciens reveals a new structure for a cysteine protease.

J. Clardy, T. Yoshimoto, K. Ito, 1999, Structure.

Factors influencing analysis of prolyl endopeptidase in human blood and cerebrospinal fluid: increase in assay sensitivity

T. Yoshimoto, A. Grubb, B. Ryberg, 2003, Scandinavian journal of clinical and laboratory investigation.

Purification of several bacteriolytic enzymes by affinity chromatography on lysozyme-lysate of Micrococcus lysodeikticus cell wall coupled with sepharose.

T. Yoshimoto, D. Tsuru, K. Kado, 1975, Journal of biochemistry.

Substrate specificity of aminopeptidase M: evidence that the commercial preparation is contaminated by dipeptidyl aminopeptidase IV and prolidase.

T. Yoshimoto, D. Tsuru, 1983, Journal of biochemistry.

Closed complex of the D-3-hydroxybutyrate dehydrogenase induced by an enantiomeric competitive inhibitor.

T. Yoshimoto, Y. Nakajima, Kiyoshi Ito, 2009, Journal of biochemistry.

D-3-hydroxybutyrate dehydrogenase from Pseudomonas fragi: molecular cloning of the enzyme gene and crystal structure of the enzyme.

T. Yoshimoto, Y. Nakajima, Kiyoshi Ito, 2006, Journal of molecular biology.

Purification and comparison of two types of beta -galactosidases from Aspergillus oryzae.

T. Yoshimoto, D. Tsuru, S. Ogushi, 1980 .

Purification and characterization of proline iminopeptidase from Lyophyllum cinerascens

T. Yoshimoto, D. Tsuru, A. Sattar, 1989 .

Crystal structure of glutathione-independent formaldehyde dehydrogenase.

T. Yoshimoto, N. Tanaka, Kazuo T. Nakamura, 2003, Chemico-biological interactions.

Cloning of a novel prolidase gene from Aureobacterium esteraromaticum.

T. Yoshimoto, K. Ito, T. Kabashima, 1999, Biochimica et biophysica acta.

Prolyl endopeptidase from Sphingomonas capsulata: isolation and characterization of the enzyme and nucleotide sequence of the gene.

T. Yoshimoto, K. Ito, T. Kabashima, 1998, Archives of biochemistry and biophysics.

Dipeptidyl peptidase IV from Xanthomonas maltophilia: sequencing and expression of the enzyme gene and characterization of the expressed enzyme.

T. Yoshimoto, K. Ito, T. Kabashima, 1996, Journal of biochemistry.

Crystal structures of creatininase reveal the substrate binding site and provide an insight into the catalytic mechanism.

T. Yoshimoto, Yue Xu, M. Haratake, 2004, Journal of molecular biology.

Degradation of streptomyces metalloprotease inhibitor (SMPI) by neutral protease from Bacillus subtilis var. amylosacchariticus.

T. Yoshimoto, K. Ito, Y. Fujita, 1992, Bioscience, biotechnology, and biochemistry.

Purification and characterization of a prolyl endopeptidase from Pseudomonas sp. KU-22

T. Yoshimoto, S. Murao, H. Oyama, 1997 .

Studies on prolyl endopeptidase from shakashimeji (Lyophyllum cinerascens): purification and enzymatic properties.

T. Yoshimoto, D. Tsuru, A. Sattar, 1988, Journal of biochemistry.

Nucleotide sequence of the gene encoding pepstatin-insensitive acid protease B, scytalidopepsin B, of Scytalidium lignicolum.

T. Yoshimoto, S. Murao, K. Oda, 1996, Bioscience, biotechnology, and biochemistry.

Proline-specific endopeptidase from Flavobacterium. Purification and properties.

T. Yoshimoto, R. Walter, D. Tsuru, 1980, The Journal of biological chemistry.

Directed evolution to improve the thermostability of prolyl endopeptidase.

T. Yoshimoto, H. Togame, T. Kokubo, 2000, Journal of biochemistry.

Cloning and expression of subtilisin amylosacchariticus gene.

T. Yoshimoto, H. Oyama, T. Honda, 1988, Journal of biochemistry.

Inactivation of Rhizopus chinensis acid protease by specific pepsin inhibitors.

T. Yoshimoto, K. Fujiwara, D. Tsuru, 2009, International journal of peptide and protein research.

Proline Specific Endopeptidase from Flavobacterium

T. Yoshimoto, D. Tsuru, 1978 .

Cloning and expression of aminopeptidase P gene from Escherichia coli HB101 and characterization of expressed enzyme.

T. Yoshimoto, T. Honda, D. Tsuru, 1988, Journal of biochemistry.

Studies on Proline Specific Peptidases and Their Inhibitors

T. Yoshimoto, 1984 .

Prolidase from Xanthomonas maltophilia: purification and characterization of the enzyme.

T. Yoshimoto, K. Ito, J. Kataoka, 1995, Bioscience, biotechnology, and biochemistry.

Prolidase from bovine intestine: purification and characterization.

T. Yoshimoto, E. Kawano, D. Tsuru, 1983, Journal of biochemistry.

Glutathione-independent formaldehyde dehydrogenase from Pseudomons putida: survey of functional groups with special regard for cysteine residues.

S. Ishikawa, T. Yoshimoto, K. Ito, 1997, Bioscience, biotechnology, and biochemistry.

Dipeptidyl aminopeptidase IV from porcine pancreas.

T. Yoshimoto, T. Kita, D. Tsuru, 1982, Journal of biochemistry.

Arachidonic acid-induced chemiluminescence of human polymorphonuclear leukocytes.

T. Yoshimoto, E. Tsubura, S. Yoshimoto, 1982, Biochemical and biophysical research communications.

Enhancement of the thermal stability of pyroglutamyl peptidase I by introduction of an intersubunit disulfide bond.

T. Yoshimoto, K. Ito, T. Kabashima, 2001, Biochimica et biophysica acta.

Novel inhibitor for prolyl tripeptidyl aminopeptidase from Porphyromonas gingivalis and details of substrate-recognition mechanism.

T. Hoffmann, T. Yoshimoto, Yue Xu, 2008, Journal of molecular biology.

Cloning, sequencing, and expression of the dipeptidyl peptidase IV gene from Flavobacterium meningosepticum in Escherichia coli.

T. Yoshimoto, K. Ito, T. Yoshida, 1995, Archives of biochemistry and biophysics.

Cloning, sequencing, high expression, and crystallization of the thermophile Thermus aquaticus glycerol kinase.

T. Yoshimoto, K. Ito, C. Yin, 1998, Bioscience, biotechnology, and biochemistry.

Crystal structure and mechanism of tripeptidyl activity of prolyl tripeptidyl aminopeptidase from Porphyromonas gingivalis.

T. Yoshimoto, Takashi Ito, Yue Xu, 2006, Journal of molecular biology.

Cloning and expression of the cDNA encoding prolyl oligopeptidase (prolyl endopeptidase) from bovine brain.

T. Yoshimoto, K. Ito, T. Kabashima, 1997, Biological & pharmaceutical bulletin.

Prolyl aminopeptidase gene from Flavobacterium meningosepticum: cloning, purification of the expressed enzyme, and analysis of its sequence.

T. Yoshimoto, K. Ito, T. Kabashima, 1996, Archives of biochemistry and biophysics.

Roles of the Ser146, Tyr159, and Lys163 residues in the catalytic action of 7alpha-hydroxysteroid dehydrogenase from Escherichia coli.

T. Nonaka, T. Yoshimoto, K. Ito, 1998, Journal of biochemistry.

Inactivation of Scytalidium Lignicolum Acid Protease b with 1, 2-epoxy-3-(4’ -azido-2’ -nitrophenoxy)Propane

T. Yoshimoto, S. Murao, K. Oda, 1989 .

Inhibition of Scytalidium lignicolum Acid Protease B by 1-Diazo-3-phenyl-2-propanone

T. Yoshimoto, N. Nakagawa, D. Tsuru, 1989 .

Isolation and amino acid sequence of a peptide containing an epoxide-reactive residue from the thermolysin-digest of Scytalidium lignicolum acid protease B.

T. Yoshimoto, S. Iwanaga, S. Murao, 1986, Journal of biochemistry.

A NOVEL ENZYME IN RAT BRAIN CONVERTING β‐ENDORPHIN INTO METHIONINE ENKEPHALIN: AFFINITY CHROMATOGRAPHY AND SPECIFICITY

T. Yoshimoto, M. Koida, S. Sakakibara, 1979, Journal of neurochemistry.

Proline-specific Endopeptidase from Flavobacterium meningosepticum: Physicochemical Properties

T. Yoshimoto, M. Ando, K. Ohta, 1982 .

Preliminary crystallographic study of Thermus aquaticus glycerol kinase.

T. Yoshimoto, Kiyoshi Ito, Hua-Shan Huang, 2001, Acta crystallographica. Section D, Biological crystallography.

Thermostable glycerol kinase from Thermus flavus: cloning, sequencing, and expression of the enzyme gene.

T. Yoshimoto, K. Ito, C. Yin, 1998, Biochimica et biophysica acta.

Pyroglutamyl peptidase gene from Bacillus amyloliquefaciens: cloning, sequencing, expression, and crystallization of the expressed enzyme.

T. Yoshimoto, K. Ito, D. Tsuru, 1993, Journal of biochemistry.