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1. Full Text Structure‐guided mutagenesis for the improvement of substrate specificity of Bacillus megaterium glucose 1‐dehydrogenase IV
by Nishioka, Taiki and Yasutake, Yoshiaki and Nishiya, Yoshiaki and Tamura, Tomohiro
The FEBS Journal, ISSN 1742-464X, 09/2012, Volume 279, Issue 17, pp. 3264 - 3275
Bacillus megaterium IAM 1030 (Bacillus sp. JCM 20016) possesses four d‐glucose 1‐dehydrogenase isozymes (BmGlcDH‐I, ‐II, ‐III and ‐IV) that belong to the... 
crystal structure | site‐directed mutagenesis | Bacillus megaterium | glucose 1‐dehydrogenase | short‐chain dehydrogenase/reductase | substrate specificity | site-directed mutagenesis | glucose 1-dehydrogenase | Bacillus megaterium | short-chain dehydrogenase/reductase | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | DROSOPHILA ALCOHOL-DEHYDROGENASE | ENZYMATIC-PROPERTIES | SHORT-CHAIN DEHYDROGENASES/REDUCTASES | reductase | ANGSTROM RESOLUTION | DISSOCIATION | PURIFICATION | C-TERMINAL TAIL | short-chain dehydrogenase | Glucose 1-Dehydrogenase - genetics | Glucose 1-Dehydrogenase - chemistry | Mutagenesis, Site-Directed | Glucose 1-Dehydrogenase - metabolism | Bacillus megaterium - enzymology | Glucose - metabolism | Models, Molecular | Substrate Specificity | Glucose metabolism | Dextrose | Glucose | Index Medicus
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2. Full Text Over-expression, characterization, and modification of highly active alkaline phosphatase from a Shewanella genus bacterium
by Aiba, Hiroshi and Nishiya, Yoshiaki and Ojima, Yoshihiro and Azuma, Masayuki
Bioscience, Biotechnology, and Biochemistry, ISSN 0916-8451, 10/2017, Volume 81, Issue 10, pp. 1994 - 2001
We isolated a Shewanella sp. T3-3 bacterium that yielded highly active alkaline phosphatase (APase). We then cloned the APase gene from Shewanella sp. T3-3... 
alkaline phosphatases | Shewanella | APase | ELISA | Alkaline phosphatases | ANTIBODIES | BIOCHEMISTRY & MOLECULAR BIOLOGY | FOOD SCIENCE & TECHNOLOGY | DNA-POLYMERASE | ENZYME | PSYCHROPHILE | CLONING | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | CHEMISTRY, APPLIED | PCR | Recombinant Proteins - metabolism | Gene Expression | Alkaline Phosphatase - genetics | Escherichia coli - genetics | Shewanella - genetics | Alkaline Phosphatase - metabolism | Shewanella - enzymology | Substrate Specificity | Recombinant Proteins - genetics | Kinetics
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3. Full Text Structure-guided mutagenesis for the improvement of substrate specificity ofBacillus megateriumglucose 1-dehydrogenase IV
: Bacillus megateriumglucose 1-dehydrogenase IV
by Nishioka, Taiki and Yasutake, Yoshiaki and Nishiya, Yoshiaki and Tamura, Tomohiro
FEBS Journal, ISSN 1742-464X, 09/2012, Volume 279, Issue 17, pp. 3264 - 3275
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4. Structure-guided mutagenesis for the improvement of substrate specificity of Bacillusmegaterium glucose 1-dehydrogenase IV
by Taiki Nishioka and Yoshiaki Yasutake and Yoshiaki Nishiya and Tomohiro Tamura
The FEBS Journal, ISSN 1742-464X, 09/2012, Volume 279, Issue 17, p. 3264
  Bacillusmegaterium IAM 1030 (Bacillus sp. JCM 20016) possesses four d-glucose 1-dehydrogenase isozymes (BmGlcDH-I, -II, -III and -IV) that belong to the... 
Enzymes | Mutagenesis | Bacteria | Biochemistry | Glucose | Crystal structure
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5. Full Text New enzymatic assays based on the combination of signal accumulation type of ion sensitive field effect transistor (SA-ISFET) with horseradish peroxidase
by Tomari, Naohiro and Sasamoto, Kohei and Sakai, Hanami and Tani, Toshio and Yamamoto, Yoshihiro and Nishiya, Yoshiaki
Analytical Biochemistry, ISSN 0003-2697, 11/2019, Volume 584, p. 113353
Peroxidase is widely used for the detection of secondary reactions during measurements of various enzymatic reactions, such as that of oxidase activity, or as... 
ISFET | Immunoassay | Escherichia coli (E. coli) | Horseradish peroxidase | H2O2 | ABTS | Sensor
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6. Full Text Nitinol stent implantation for femoropopliteal disease in patients on hemodialysis: results of the 3-year retrospective multicenter APOLLON study
by Fujihara, Masahiko and Fujihara, Masahiko and Higashimori, Akihiro and Higashimori, Akihiro and Kato, Yoshihiro and Kato, Yoshihiro and Taniguchi, Hiromasa and Taniguchi, Hiromasa and Iwasaki, Yusuke and Iwasaki, Yusuke and Amano, Tomonori and Amano, Tomonori and Sumiyoshi, Akinori and Sumiyoshi, Akinori and Nishiya, Daisuke and Nishiya, Daisuke and Yokoi, Yoshiaki and Yokoi, Yoshiaki
Heart and Vessels, ISSN 0910-8327, 9/2016, Volume 31, Issue 9, pp. 1476 - 1483
The clinical outcomes of nitinol stents for femoropopliteal arterial (FP) disease in patients on hemodialysis were assessed. Endovascular therapy (EVT) is... 
Biomedical Engineering | Femoropopliteal artery disease | Endovascular therapy | Medicine & Public Health | Cardiac Surgery | Hemodialysis | Vascular Surgery | Cardiology | Nitinol stent | CARDIAC & CARDIOVASCULAR SYSTEMS | PERCUTANEOUS TRANSLUMINAL ANGIOPLASTY | PACLITAXEL-ELUTING STENTS | PREVALENCE | LESIONS | SUPERFICIAL FEMORAL-ARTERY | BALLOON ANGIOPLASTY | CALCIFICATION | PERIPHERAL VASCULAR DISEASE | PERIPHERAL ARTERIAL-DISEASE | Recurrence | Constriction, Pathologic | Humans | Middle Aged | Male | Renal Insufficiency, Chronic - complications | Peripheral Arterial Disease - complications | Prosthesis Design | Endovascular Procedures - instrumentation | Renal Insufficiency, Chronic - therapy | Time Factors | Popliteal Artery - physiopathology | Amputation | Aged, 80 and over | Female | Renal Insufficiency, Chronic - diagnosis | Retrospective Studies | Ultrasonography, Doppler, Duplex | Stents | Limb Salvage | Endovascular Procedures - adverse effects | Femoral Artery - physiopathology | Japan | Risk Factors | Alloys | Kaplan-Meier Estimate | Treatment Outcome | Popliteal Artery - diagnostic imaging | Peripheral Arterial Disease - therapy | Peripheral Arterial Disease - physiopathology | Femoral Artery - diagnostic imaging | Renal Dialysis - adverse effects | Peripheral Arterial Disease - diagnostic imaging | Aged | Vascular Patency | Nickel alloys | Analysis | Stent (Surgery) | Studies | Therapy
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7. Full Text Simple and reliable urea assay based on a signal accumulation type of ion-sensitive field-effect transistor
by Tomari, Naohiro and Kawasaki, Asako and Yamamoto, Yoshihiro and Nishiya, Yoshiaki
Journal of Bioscience and Bioengineering, ISSN 1389-1723, 02/2015, Volume 119, Issue 2, pp. 247 - 250
A simple urea assay was developed using a signal accumulation type of ion-sensitive field-effect transistor (SA-ISFET). Decreases in proton concentration... 
Proton | Urease | Signal accumulation | Ion-sensitive field-effect transistor | Urea assay | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | FOOD SCIENCE & TECHNOLOGY | NITROGEN | Hydrolysis | Protons | Reproducibility of Results | Biocatalysis | Biosensing Techniques - instrumentation | Biosensing Techniques - methods | Ions | Urease - metabolism | Urea - analysis | Hydrogen-Ion Concentration | Transistors, Electronic | Urea | Field-effect transistors
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8. Full Text The reaction mechanism of sarcosine oxidase elucidated using FMO and QM/MM methodsElectronic supplementary information (ESI) available: Computational details of QM/MM model and theoretical level (Cl− treatment and basis set dependency for energy and atomic charges), all the results for models 2 and 3 (molecular structures, energy profiles, pair interaction energies, UV-vis spectra, and relative energies along the reaction coordinates), RESP charges used for the MD calculations and the xyz coordinates for all the states (all the atoms in the QM region in models 1, 2 and 3). See DOI: 10.1039/c6cp08172j
by Abe, Yukihiro and Shoji, Mitsuo and Nishiya, Yoshiaki and Aiba, Hiroshi and Kishimoto, Takahide and Kitaura, Kazuo
ISSN 1463-9076, 4/2017, Volume 19, Issue 15, pp. 9811 - 9822
Monomeric sarcosine oxidase (MSOX) is a flavoprotein that oxidizes sarcosine to the corresponding imine product and is widely used in clinical diagnostics to... 
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9. Full Text Characterization of d-succinylase from Cupriavidus sp. P4-10-C and its application in d-amino acid synthesis
by Sumida, Yosuke and Iwai, Sachio and Nishiya, Yoshiaki and Kumagai, Shinya and Yamada, Toshihide and Azuma, Masayuki
Journal of Bioscience and Bioengineering, ISSN 1389-1723, 03/2018, Volume 125, Issue 3, pp. 282 - 286
-Amino acids are important building blocks for various compounds, such as pharmaceuticals and agrochemicals. A more cost-effective enzymatic method for -amino... 
d-Succinylase | Dynamic kinetic resolution | d-Amino acids production | N-Succinyl amino acid racemase | Biotransformation | N-Succinyl amino acids | D-Succinylase | D-Amino acids production | Cupriavidus - genetics | Metabolic Engineering - methods | Temperature | Phenylalanine - metabolism | Tryptophan - metabolism | Amino Acids - biosynthesis | Amino Acids - metabolism | Valine - metabolism | Amino Acid Isomerases - isolation & purification | Amino Acid Isomerases - metabolism | Succinic Acid - metabolism | Amino Acid Isomerases - genetics | Cloning, Molecular | Kinetics | Cupriavidus - enzymology | Tryptophan | Enzymes | Amino acids | Synthesis | Biological products | Phenylalanine
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10. Full Text Structural Insights into Unique Substrate Selectivity of Thermoplasma acidophilum d-Aldohexose Dehydrogenase
by Yasutake, Yoshiaki and Nishiya, Yoshiaki and Tamura, Noriko and Tamura, Tomohiro
Journal of Molecular Biology, ISSN 0022-2836, 04/2007, Volume 367, Issue 4, pp. 1034 - 1046
The d-aldohexose dehydrogenase from the thermoacidophilic archaea Thermoplasma acidophilum (AldT) belongs to the short-chain dehydrogenase/reductase (SDR)... 
short-chain dehydrogenase/reductase (SDR) | d-aldohexose dehydrogenase | Thermoplasma acidophilum | d-mannose | d-glucose dehydrogenase | Amino Acid Sequence | Models, Molecular | Molecular Sequence Data | Substrate Specificity | Sequence Homology, Amino Acid | Coenzymes - metabolism | Mannose - metabolism | Thermoplasma - enzymology | Glucose - chemistry | Protein Structure, Quaternary | Bacillus megaterium - enzymology | Glucose - metabolism | Protein Binding | Protein Subunits - chemistry | Catalysis | Binding Sites | Carbohydrate Dehydrogenases - chemistry | Carbohydrate Dehydrogenases - metabolism | Mannose - chemistry | Protein Structure, Tertiary - physiology
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11. Full Text Insertion sequence-excision enhancer removes transposable elements from bacterial genomes and induces various genomic deletions
by Sekine, Yasuhiko and Akiba, Masato and Hayashi, Tetsuya and Kusumoto, Masahiro and Ooka, Tadasuke and Iwata, Taketoshi and Nishiya, Yoshiaki and Saito, Takashi and Ogura, Yoshitoshi
Nature Communications, ISSN 2041-1723, 01/2011, Volume 2, Issue 1, p. 152
Insertion sequences (ISs) are the simplest transposable elements and are widely distributed in bacteria. It has long been thought that IS excision rarely... 
MUTANTS | ENTEROHEMORRHAGIC ESCHERICHIA-COLI | PROTEIN | REPLICATION | GENE | O157-H7 | ELEGANS | MULTIDISCIPLINARY SCIENCES | DIVERSITY | IDENTIFICATION | TRANSPOSITION
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12. Full Text The reaction mechanism of sarcosine oxidase elucidated using FMO and QM/MM methods
by Abe, Yukihiro and Shoji, Mitsuo and Nishiya, Yoshiaki and Aiba, Hiroshi and Kishimoto, Takahide and Kitaura, Kazuo
Physical Chemistry Chemical Physics, ISSN 1463-9076, 2017, Volume 19, Issue 15, pp. 9811 - 9822
Monomeric sarcosine oxidase (MSOX) is a flavoprotein that oxidizes sarcosine to the corresponding imine product and is widely used in clinical diagnostics to... 
MONOAMINE-OXIDASE | SITE | ELECTRON-TRANSFER | HYDROGEN-ATOM TRANSFER | CATALYZED OXIDATION | PHYSICS, ATOMIC, MOLECULAR & CHEMICAL | CHEMISTRY, PHYSICAL | BENZYLAMINE | PROTON | DENSITY-FUNCTIONAL THEORY | CHARGE-TRANSFER | AMINE-OXIDATION | Electron Transport | Biocatalysis | Oxidation-Reduction | Molecular Conformation | Models, Molecular | Sarcosine - metabolism | Sarcosine Oxidase - chemistry | Thermodynamics | Quantum Theory | Hydrogen Bonding | Sarcosine - chemistry | Flavins - chemistry | Kinetics | Sarcosine Oxidase - metabolism | Flavins - metabolism
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13. Full Text Identification and Characterization ofD-Succinylase, and a Proposed Enzymatic Method forD-Amino Acid Synthesis
by Sumida, Yosuke and Iwai, Sachio and Nishiya, Yoshiaki and Kumagai, Shinya and Yamada, Toshihide and Azuma, Masayuki
Advanced Synthesis & Catalysis, ISSN 1615-4150, 06/2016, Volume 358, Issue 13, pp. 2041 - 2046
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14. Full Text Hyperstabilization of Tetrameric Bacillus sp. TB-90 Urate Oxidase by Introducing Disulfide Bonds through Structural Plasticity
by Hibi, Takao and Kume, Asami and Kawamura, Akie and Itoh, Takafumi and Fukada, Harumi and Nishiya, Yoshiaki
Biochemistry, ISSN 0006-2960, 02/2016, Volume 55, Issue 4, pp. 724 - 732
Bacillus sp. TB-90 urate oxidase (BTUO) is one of the most thermostable homotetrameric enzymes. We previously reported [Hibi, T., et al. (2014) Biochemistry... 
THERMOSTABILITY | CRYSTAL-STRUCTURE | STABILIZATION | STABILITY | BIOCHEMISTRY & MOLECULAR BIOLOGY | SEQUENCE | Protein Multimerization | Bacterial Proteins - chemistry | Bacterial Proteins - genetics | Enzyme Stability | Crystallography, X-Ray | Bacillus - genetics | Mutation, Missense | Urate Oxidase - genetics | Bacillus - enzymology | Disulfides - chemistry | Urate Oxidase - chemistry | Protein Structure, Quaternary | Amino Acid Substitution | Oxidases | Usage | Chemical bonds | Bacillus (Bacteria) | Calorimetry | Research | Chemical properties | Index Medicus
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15. Full Text C‐terminal tail derived from the neighboring subunit is critical for the activity of Thermoplasma acidophilumD‐aldohexose dehydrogenase
by Nishioka, Taiki and Yasutake, Yoshiaki and Nishiya, Yoshiaki and Tamura, Noriko and Tamura, Tomohiro
Proteins: Structure, Function, and Bioinformatics, ISSN 0887-3585, 03/2009, Volume 74, Issue 4, pp. 801 - 807
The D‐aldohexose dehydrogenase from the thermoacidophilic archaeon Thermoplasma acidophilum (AldT) is a homotetrameric enzyme that catalyzes the oxidation of... 
D‐glucose dehydrogenase | D‐mannose | Thermoplasma acidophilum | C‐terminal tail | short‐chain dehydrogenase/reductase (SDR) | D‐aldohexose dehydrogenase (AldT)
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16. Full Text C-terminal tail derived from the neighboring subunit is critical for the activity ofThermoplasma acidophilumD-aldohexose dehydrogenase
by Nishioka, Taiki and Yasutake, Yoshiaki and Nishiya, Yoshiaki and Tamura, Noriko and Tamura, Tomohiro
Proteins: Structure, Function, and Bioinformatics, ISSN 0887-3585, 03/2009, Volume 74, Issue 4, pp. 801 - 807
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17. Full Text Doripenem Versus Meropenem As the First-Line Mono-Therapy in High-Risk Febrile Neutropenic Patients with Acute Leukemia: A Randomized, Controlled Trial
by Oyake, Tatsuo and Sugawara, Norifumi and Miyajima, Shinri and Kiyohara, Kazuki and Nishiya, Maki and Shimoyama, Tadashi and Takemasa-Fujisawa, Yuka and Sasaki, Ryosei and Izumita, Wataru and Tsukushi, Yasuhiko and Otsu, Akihiro and Mine, Takahiro and Sugawara, Takeshi and Suzuki, Yuzo and Okano, Yoshiaki and Hanamura, Ichiro and Kowata, Shugo and Ito, Shigeki
Blood, ISSN 0006-4971, 11/2019, Volume 134, Issue Supplement_1, pp. 4865 - 4865
BACKGROUND: Febrile neutropenia (FN) is often observed in patients with hematological malignancies (HEM), especially in those with acute leukemia (AL).... 
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18. Full Text Correction to Intersubunit Salt Bridges with a Sulfate Anion Control Subunit Dissociation and Thermal Stabilization of Bacillus sp. TB-90 Urate Oxidase
by Hibi, Takao and Hayashi, Yuta and Fukada, Harumi and Itoh, Takafumi and Nago, Tomohiro and Nishiya, Yoshiaki
Biochemistry, ISSN 0006-2960, 08/2014, Volume 53, Issue 33, pp. 5471 - 5471
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19. Full Text Identification and Characterization of D‐Succinylase, and a Proposed Enzymatic Method for D‐Amino Acid Synthesis
by Sumida, Yosuke and Iwai, Sachio and Nishiya, Yoshiaki and Kumagai, Shinya and Yamada, Toshihide and Azuma, Masayuki
Advanced Synthesis & Catalysis, ISSN 1615-4150, 06/2016, Volume 358, Issue 13, pp. 2041 - 2046
Chiral amino acids are important intermediates for the pharmaceutical industry. We have developed a novel one‐pot enzymatic method for D‐amino acid synthesis... 
N‐succinylamino acid racemase | biotransformation | N‐succinylamino acids | D‐succinylase | dynamic kinetic resolution | D‐amino acids | N-succinylamino acids | PENICILLIN ACYLASE | CHEMISTRY, ORGANIC | N-succinylamino acid racemase | AMIDOHYDROLASE | RACEMASE | ENOLASE SUPERFAMILY | D-succinylase | D-amino acids | EVOLUTION | CHEMISTRY, APPLIED | Screening | Microorganisms | Synthesis | Genes | Escherichia coli | Amino acids | Conversion | Recombinant
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20. Full Text Characterization of a thermostable glucose dehydrogenase with strict substrate specificity from a hyperthermophilic archaeonThermoproteussp. GDH-1
by Aiba, Hiroshi and Nishiya, Yoshiaki and Azuma, Masayuki and Yokooji, Yuusuke and Atomi, Haruyuki and Imanaka, Tadayuki
Bioscience, Biotechnology, and Biochemistry, ISSN 0916-8451, 07/2015, Volume 79, Issue 7, pp. 1094 - 1102
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