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1. Rivaroxaban Monotherapy in Patients With Atrial Fibrillation After Coronary Stenting

Author

Tetsuya Matoba, Satoshi Yasuda, Koichi Kaikita, Masaharu Akao, Junya Ako, Masato Nakamura, Katsumi Miyauchi, Nobuhisa Hagiwara, Kazuo Kimura, Atsushi Hirayama, Kunihiko Matsui, Hisao Ogawa, Yukihiro Koretsune, Takafumi Hiro, Tetsuya Sumiyoshi, Kazumi Kimura, Yoichiro Hashimoto, Teruyuki Hirano, Hiroyuki Daida, Yasushi Okada, Tsutomu Yamazaki, A. Nakamura, E. Tamiya, T. Yamamoto, S. Suetake, T. Noguchi, S. Nakamura, A. Matsumura, J. Kojima, S. Suwa, H. Yamaguchi, K. Kaikita, T. Yasu, A. Nakajima, T. Yamada, H. Arai, Y. Hata, T. Sakanashi, H. Tateishi, T. Nakayama, Y. Nozaki, M. Akao, Y. Okumura, M. Tokue, N. Kuroki, Y. Maruyama, T. Matoba, N. Hagiwara, H. Suzuki, Y. Nishida, M. Ajioka, K. Yumoto, S. Shimizu, T. Aoyama, H. Shimomura, T. Takeda, K. Oshiro, N. Sugishita, Y. Shibata, T. Otonari, H. Kihara, H. Ogawa, A. Ohno, M. Hazama, M. Shimizu, K. Tsukahara, S. Haruta, T. Wakeyama, T. Haruna, M. Ito, K. Fujii, N. Atsuchi, M. Sata, K. Kimura, N. Hasebe, Y. Kobayasi, K. Ohsato, K. Hironaga, Y. Naganuma, K. Anzaki, K. Oiwa, S. Okazaki, Y. Nakagawa, K. Tokuhiro, K. Tanaka, T. Momose, Y. Fukushima, R. Kametani, K. Kawamitsu, Y. Saito, S. Akashi, K. Kumagai, K. Eshima, T. Tobaru, T. Seo, K. Okuhara, K. Kozuma, Y. Ikari, T. Takahashi, I. Michishita, H. Fujikura, S. Momomura, Y. Yamamoto, K. Otomo, T. Matsubara, H. Tashiro, T. Inoue, M. Ishihara, I. Shiojima, E. Tachibana, J. Ako, K. Sumii, N. Yamamoto, N. Ohmura, T. Nakamura, Y. Morita, N. Takahashi, K. Watanabe, H. Fujinaga, M. Maruyama, T. Oka, T. Shirayama, T. Amano, K. Fukui, K. Ando, S. Oshima, S. Kagiyama, H. Teragawa, M. Yuge, S. Ono, T. Koga, K. Fujiu, M. Kuwabara, Y. Ohya, Y. Yumoto, N. Kuji, M. Ikemura, K. Kario, K. Chatani, K. Sato, H. Miyagi, M. Murakami, K. Saito, M. Hoshiga, S. Sato, N. Kubo, Y. Sakamoto, K. Ashida, H. Sakamoto, S. Murasaki, H. Uehara, T. Akasaka, Y. Ooba, S. Nakahara, Y. Hanaoka, T. Nishimiya, R. Tsunoda, Y. Onuma, S. Higuchi, A. Tani, A. Wada, M. Kato, H. Obata, Y. Higuchi, T. Endo, R. Katou, T. Matsunaga, T. Matsuoka, H. Noguchi, M. Usui, T. Hayashi, Y. Otsuji, T. Osaki, H. Zaizen, H. Yoshihara, K. Kadota, T. Hirose, T. Miyazawa, A. Mori, M. Takano, W. Shimizu, M. Wake, S. Oriso, M. Yoshiyama, S. Kakinoki, T. Nishioka, T. Ozaki, K. Nomoto, K. Seki, K. Kawai, Y. Ozaki, S. Miura, M. Kawasaki, R. Funada, K. Dote, T. Nagano, S. Okamoto, T. Kubo, Y. Murozono, T. Owada, T. Doke, T. Matsumura, M. Horiuchi, A. Takaishi, M. Yamamoto, H. Nakashima, M. Munemasa, Y. Sakata, N. Inoue, T. Ota, Y. Hamano, N. Abe, T. Tsubokura, M. Goto, I. Kubota, M. Yano, K. Umetani, T. Date, H. Morimoto, T. Noda, S. Goto, K. Hibi, A. Nakano, S. Hiramitsu, Y. Kihara, M. Sugi, N. Shiba, D. Izumi, T. Sato, S. Tayama, T. Matsui, A. Suzuki, K. Ajiki, M. Oishi, M. Kiryu, T. Ko, H. Ando, S. Miyazaki, T. Kinugawa, H. Otake, H. Kitaoka, Y. Hirata, S. Honda, M. Manita, Y. Ishii, H. Oka, Y. Nanba, M. Nishino, T. Sakamoto, T. Saito, H. Sakai, M. Ichikawa, S. Namiuchi, K. Inoue, N. Komiyama, Y. Akashi, Y. Nakamura, T. Komaru, T. Hosokawa, T. Chikamori, H. Tanaka, O. Arasaki, K. Aonuma, Y. Wakasa, T. Yoshizawa, T. Sugano, N. Yokota, A. Kakutani, T. Suzuki, Y. Abe, T. Kataoka, H. Okayama, H. Yokoi, K. Chin, K. Hasegawa, H. Tomita, H. Honzyo, H. Kawai, K. Yamamoto, Y. Morino, S. Tsujiyama, S. Hamasaki, Y. Niijima, Y. Mizuno, A. Maki, K. Tanabe, T. Murohara, S. Naomi, M. Arikawa, T. Kato, N. Matsumoto, T. Minamino, H. Sairenji, N. Miyamoto, H. Ito, Y. Matsuura, S. Hata, Y. Nakatsu, T. Onodera, M. Yoshimura, H. Amano, E. Tokutake, M. Kasao, M. Moriguchi, M. Tsuji, H. Yamamoto, Y. Yanbe, T. Iwasawa, M. Suzuki, and H. Mori

Subjects
Rivaroxaban, medicine.medical_specialty, business.industry, Unstable angina, medicine.medical_treatment, Percutaneous coronary intervention, Atrial fibrillation, medicine.disease, Thrombosis, Coronary artery disease, Internal medicine, medicine, Cardiology, cardiovascular diseases, Myocardial infarction, Cardiology and Cardiovascular Medicine, business, Stroke, medicine.drug
Abstract

Objectives The aim of this AFIRE (Atrial Fibrillation and Ischemic Events With Rivaroxaban in Patients With Stable Coronary Artery Disease) trial subgroup analysis was to examine rivaroxaban monotherapy benefits and their relation to the time between stenting and enrollment among patients after coronary stenting. Background Of 2,215 patients with atrial fibrillation and stable coronary artery disease in the AFIRE trial, rivaroxaban monotherapy was noninferior to rivaroxaban plus antiplatelet therapy (combination therapy) in terms of efficacy and superior for safety endpoints. However, thrombotic risk after antiplatelet therapy cessation remained a concern among 1,444 patients who had undergone coronary stenting >1 year before enrollment. Methods The benefits of rivaroxaban monotherapy in coronary stenting subgroups were assessed for efficacy (a composite of stroke, systemic embolism, myocardial infarction, unstable angina requiring revascularization, or death of any cause), safety (major bleeding defined according to International Society on Thrombosis and Haemostasis criteria), ischemic endpoints, net adverse clinical event, and time between stenting and enrollment. Results Efficacy and safety endpoints for monotherapy were superior to combination therapy, with HRs of 0.70 for efficacy (95% CI: 0.50-0.98; P = 0.036) and 0.55 for safety (95% CI: 0.33-0.92; P = 0.019). For ischemic endpoints, the HR was 0.82 (95% CI: 0.58-1.15; P = 0.240). The HR became smaller with longer time between stenting and enrollment (efficacy, P for interaction = 0.158; safety, P = 0.097). Conclusions In patients with atrial fibrillation after coronary stenting, the benefits of rivaroxaban monotherapy for efficacy and safety endpoints were consistent with those in the whole AFIRE trial population. The benefits became apparent with longer time between stenting and enrollment. (Atrial Fibrillation and Ischemic Events With Rivaroxaban in Patients With Stable Coronary Artery Disease Study [AFIRE]; UMIN000016612 , NCT02642419 )

Published
2021
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3. Heat Transfer and Pressure Drop Inside Duct with Different Surface Profiles

Author

V. M. Sonde, P. T. Date, T. R. Badule, and P. P. Shirpurkar

Subjects
Pressure drop, symbols.namesake, Transverse plane, Materials science, Heat flux, Heat transfer, Broken ribs, medicine, symbols, Reynolds number, Duct (flow), Mechanics, medicine.disease
Abstract

In this experimental study, the heat transfer rate with respect to the pressure drop in rectangular duct is studied. The ribs with various profiles are used as an inserts and heat transfer rate was determined. The rectangular duct of cross-section 700 × 100 mm made up of mild steel was used. The experiments were carried for the Reynolds number in the range 5000–22,000. Five cases were analyzed in this study. Case 1 includes the rectangular duct with 300 mm as effective test section without ribs. In Case 2, flat ribs were used at angle of 900 with respect to the direction of the flow. V-shaped broken ribs inclined at an angle of 30°, 45°, and 60° with respect to the direction of flow are used as inserts in case 3, 4, and 5, respectively. The readings were noted at constant heat flux of test section. Initially, air was supplied with velocity of 0.6 m/s and then it was gradually increased to 2.4 m/s. In this case, less pressure drop is observed experimentally, as compared to transverse broken V-shaped ribs.

Published
2020
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5. Enhancement of photoluminescence at 1.54μm from Er in strained Si and SiGe

Author

S. Yoneyama, Taisuke Hasegawa, K. Okuno, K. Inoue, T. Date, Yoshifumi Yamashita, Yoichi Kamiura, and Takeshi Ishiyama

Subjects
Photoluminescence, Materials science, Silicon, Pl spectra, Doping, Analytical chemistry, chemistry.chemical_element, Condensed Matter Physics, Electronic, Optical and Magnetic Materials, Erbium, chemistry, Impurity, Electrical and Electronic Engineering, Luminescence, Molecular beam epitaxy
Abstract

We studied on the photoluminescence (PL) properties of Er in tensile-strained Si on a SiGe layer (Si:Er:O/SiGe) and compressively strained SiGe on a Si layer (SiGe:Er:O/Si) grown by molecular beam epitaxy (MBE). Er-related luminescence was observed around 1.54 μm in both tensile- and compressively strained samples. The PL intensities of strained Si:Er:O/SiGe and SiGe:Er:O/Si samples were much stronger than those of unstrained Si:Er:O/Si samples. Moreover, intensive luminescence was observed in strained samples with low Er concentrations far below 10 18 cm −3 . The PL spectra of Si:Er:O/SiGe samples were broader than those of unstrained Si:Er:O/Si samples. On the other hand, no significant differences in the width between SiGe:Er:O/Si and unstrained samples were observed. These differences in the PL intensity between strained and unstrained samples strongly suggest that the optical activation of Er in Si and SiGe can be enhanced by the presence of strain.

Published
2006
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6. Enhancing effect of tensile strain on photoluminescence of Er in Si on a SiGe layer

Author

K. Okuno, K. Inoue, Yoshifumi Yamashita, Takeshi Ishiyama, M. Yoshida, Yoichi Kamiura, T. Hasegawa, and T. Date

Subjects
Photoluminescence, Materials science, Silicon, Doping, Analytical chemistry, chemistry.chemical_element, Condensed Matter Physics, Electronic, Optical and Magnetic Materials, Erbium, chemistry, Electrical and Electronic Engineering, Thin film, Luminescence, Layer (electronics), Molecular beam epitaxy
Abstract

We studied on the effect of the strain on photoluminescence (PL) properties of Er-doped Si on a SiGe layer (Si:Er:O/SiGe) and Er-doped SiGe on a Si layer (SiGe:Er:O/Si) grown by molecular beam epitaxy. Er-related luminescence was observed around 1.54 μm in all the samples. The PL spectra of the Si:Er:O/SiGe samples are much broader and stronger than those of the Si:Er:O/Si samples prepared as reference. Moreover, the intensive luminescence was observed in the Si:Er:O/SiGe sample that had much lower Er concentration of about 2.5×10 16 cm −3 . On the other hand, the significant differences in the PL spectra between the SiGe:Er:O/Si and Si:Er:O/Si samples were not observed. These indicate that the tensile strained Si enhances the optical activation of Er.

Published
2003
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7. A facile conversion of ethoxydihydropyrans to 4-cyanoethylisoxazoles

Author

Masashige Yamauchi, S. Akiyama, Tokuhiro Watanabe, T. Date, and K. Okamura

Subjects
chemistry.chemical_compound, Chemistry, Organic Chemistry, Ethyl vinyl ether, Substituent, Hydroxylamine Hydrochloride, Medicinal chemistry, Acyl group
Abstract

The reaction of ethoxydihydropyrans 2, which were prepared from 2-methylene-1,3-dicarbonyl compounds 1 with ethyl vinyl ether, and hydroxylamine hydrochloride gave 4-cyanoethylisoxazoles 3 whose substituents at the 3 and 5 positions were transformed from substituent at the 2 position and the acyl group of 2 regioselectively.

Published
1996
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8. Phthalocyanines ultrathin alternating layer film on silicon, prepared by molecular beam deposition

Author

S. Tomita, M. Nishimura, T. Date, Naoto Nagai, Akira Ishitani, T. Nonaka, and Y. Murata

Subjects
Silicon, Chemistry, Metals and Alloys, Analytical chemistry, Infrared spectroscopy, chemistry.chemical_element, Surfaces and Interfaces, Surfaces, Coatings and Films, Electronic, Optical and Magnetic Materials, Secondary ion mass spectrometry, symbols.namesake, Fourier transform, Transmission electron microscopy, Materials Chemistry, symbols, Molecule, Group 2 organometallic chemistry, Molecular beam epitaxy
Abstract

Copper-phthalocyanine (CuPc) and magnesium-phthalocyanine (MgPc) were alternatively deposited on silicon substrates by organic molecular beam deposition. The thickness of each layer was varied in the range 3.0–10.0 nm. The layered structure of the film was confirmed by secondary ion mass spectrometry depth profiling and cross-sectional observations with a transmission electron microscope. The molecular orientation within a film was estimated by Fourier transform IR spectroscopy. The measurements suggested that the planar molecules of CuPc and MgPc were inclined at an angle of 22° with respect to the substrate surface.

Published
1994
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9. Mutation of histidine 373 to leucine in cytochrome P450c17 causes 17 alpha-hydroxylase deficiency

Author

M Kobayashi, Hideyuki Ogawa, M Fujioka, S Monno, T Date, and W L Miller

Subjects
Cytochrome, biology, Heme binding, Point mutation, Mutagenesis, Mutant, Cell Biology, Biochemistry, Molecular biology, chemistry.chemical_compound, chemistry, Mutant protein, Complementary DNA, biology.protein, Molecular Biology, Heme
Abstract

We identified a new homozygous missense mutation His373-->Leu in the CYP17 gene of two sisters with 17 alpha-hydroxylase deficiency with an elevated plasma aldosterone concentration by sequencing their genomic DNAs amplified by polymerase chain reaction. Using polymerase chain reaction-based site-directed mutagenesis, we prepared a DNA that encoded the Leu373 mutant protein. COS-1 cells transfected with the mutant DNA, despite having an RNA hybridizable to the P450c17 cDNA, did not show 17 alpha-hydroxylase and 17,20-lyase activities. Also, the cells were devoid of 11 beta-hydroxylase and aldosterone synthase activities. To examine the mechanism by which the single amino acid change His373-->Leu eliminates activity, we expressed N-terminally modified P450c17 proteins with and without the Leu373 mutation in Escherichia coli and performed spectral studies. Membrane preparations from E. coli cells expressing the wild-type form of the modified enzyme showed an absorption peak at 449 nm upon addition of carbon monoxide in the reduced state and produced characteristic substrate-induced difference spectra, whereas those from the cells expressing the mutant form did not show these spectral changes. The 17 alpha-hydroxylase and 17,20-lyase activities were observed only in E. coli cells expressing the wild-type enzyme. These results show that the His373-->Leu mutant does not incorporate the heme prosthetic group properly and suggest a critical role of His373 in heme binding.

Published
1993
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10. Expression of active human DNA ligase I in Escherichia coli cells that harbor a full-length DNA ligase I cDNA construct

Author

Shigeyuki Iijima, O Koiwai, H Minami, T Date, Hirobumi Teraoka, and Kinji Tsukada

Subjects
chemistry.chemical_classification, DNA ligase, biology, Okazaki fragments, Cell Biology, Molecular cloning, Biochemistry, Molecular biology, law.invention, chemistry, law, Recombinant DNA, biology.protein, Genomic library, DNA polymerase I, Ligase chain reaction, Molecular Biology, In vitro recombination
Abstract

A recombinant plasmid for expression of full-length human DNA ligase I (phLig-I) was constructed in a plasmid/phage chimeric vector, pTD-T7N, which was derived from pUC118 by oligonucleotide-directed mutagenesis. The insert contained a 2757-base pair coding sequence for a whole human DNA ligase I and an extra ACC codon adjacent to the ATG initiation codon. This ACC codon was required for achieving high levels of expression of full-length DNA ligase I in Escherichia coli strain BL21. The recombinant plasmid, which was designed to exploit the T7 late promoter and the ATG initiation codon for beta-galactosidase was transfected into E. coli BL21 cells that express T7 RNA polymerase. The recombinant clone produced relatively high levels of DNA ligase I with a molecular mass of 130 kDa, as estimated by SDS-polyacrylamide gel electrophoresis. The DNA ligase was purified to near-homogeneity by the two-step column chromatographic procedure from BLphLig-I cells that had been induced with isopropyl beta-D-thiogalactoside. The specific activity, chromatographic behavior, kinetic properties, molecular mass, and antigenicity of the recombinant human DNA ligase I were indistinguishable from those of purified mammalian DNA ligase I. Metabolically labeling experiments with 32P(i) indicate that the recombinant DNA ligase I was present as an enzyme-AMP reaction intermediate, but not as a phosphoprotein, in the E. coli cells.

Published
1993
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11. Stereoselective addition of 2-aminothiophenol to α-alkoxycinnamic acid derivatives—alternative synthesis of (±)-diltiazem

Author

Takeaki Naito, Okiko Miyata, K. Okamura, T. Date, Ichiya Ninomiya, and Tetsuro Shinada

Subjects
Nucleophilic addition, Bicyclic molecule, Chemistry, Organic Chemistry, 2-Aminothiophenol, Biochemistry, chemistry.chemical_compound, Drug Discovery, medicine, Lactam, Organic chemistry, Stereoselectivity, Diltiazem, medicine.drug
Abstract

A stereocontrolled synthesis of (±)-diltiazem by applying nucleophilic addition of 2-aminothiophenol to α-alkoxycinnamic acid derivatives is described.

Published
1993
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12. Current Development Status and Future Challenges of FeRAM

Author

T. Kanaya, Suzuki Tatsuya, Masato Moriwake, N. Kinouchi, Yoshinobu Ichida, Hidemi Takasu, J. Iida, K. Ashikaga, Z. Zhiyong, Yoshikazu Fujimori, Hiromitsu Kimura, M. Kojima, T. Date, T. Ozawa, H. Ito, D. Notsu, and T. Fuchikami

Subjects
Materials science, Ferroelectric RAM, Systems engineering, Nanotechnology, Current (fluid)
Published
2010
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18. ChemInform Abstract: Stereoselective Addition of 2-Aminothiophenol to α- Alkoxycinnamic Acid Derivatives - Alternative Synthesis of (.+-.)- Diltiazem

Author

T. Date, Tetsuro Shinada, Takeaki Naito, K. Okamura, Okiko Miyata, and Ichiya Ninomiya

Subjects
Nucleophilic addition, Chemistry, medicine, Stereoselectivity, General Medicine, Diltiazem, 2-Aminothiophenol, Medicinal chemistry, medicine.drug
Abstract

A stereocontrolled synthesis of (±)-diltiazem by applying nucleophilic addition of 2-aminothiophenol to α-alkoxycinnamic acid derivatives is described.

Published
2010
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21. ChemInform Abstract: A Facile Conversion of Ethoxydihydropyrans to 4-Cyanoethylisoxazoles

Author

Tokuhiro Watanabe, K. Okamura, Masashige Yamauchi, S. Akiyama, and T. Date

Subjects
chemistry.chemical_compound, chemistry, Stereochemistry, Ethyl vinyl ether, Substituent, General Medicine, Hydroxylamine Hydrochloride, Medicinal chemistry, Acyl group
Abstract

The reaction of ethoxydihydropyrans 2, which were prepared from 2-methylene-1,3-dicarbonyl compounds 1 with ethyl vinyl ether, and hydroxylamine hydrochloride gave 4-cyanoethylisoxazoles 3 whose substituents at the 3 and 5 positions were transformed from substituent at the 2 position and the acyl group of 2 regioselectively.

Published
2010
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22. ChemInform Abstract: Enantioselective Catalytic Diels-Alder Reaction of Ethyl 2- Benzoylacrylate with Chiral Bis(oxazoline)- or Mono(oxazoline)- Magnesium Complex

Author

Hajime Hiramatsu, T. Date, Yuko Honda, and Masashige Yamauchi

Subjects
chemistry.chemical_classification, Ligand, Magnesium, fungi, Enantioselective synthesis, chemistry.chemical_element, General Medicine, Oxazoline, Medicinal chemistry, Catalysis, chemistry.chemical_compound, chemistry, Bridged compounds, Diels–Alder reaction
Abstract

The magnesium catalysed Diels–Alder reaction of 2-benzoylacrylate gave the endo-adduct enantioselectively with bis(oxazoline) 5 as a C 2 -symmetric ligand or mono(oxazoline) 4 as a non-C 2 -symmetric ligand.

Published
2010
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23. Molecular dissection of the beta subunit of F1-ATPase into peptide fragments

Author

Masasuke Yoshida, M Odaka, K Tozawa, and T Date

Subjects
chemistry.chemical_classification, biology, Protein subunit, Protein primary structure, Peptide, Cell Biology, Biochemistry, Molecular biology, Protein tertiary structure, chemistry, biology.protein, Beta (finance), Molecular Biology, Polyacrylamide gel electrophoresis, ATP synthase alpha/beta subunits, G alpha subunit
Abstract

Partial digestion of the native beta subunit of F1-ATPase from the thermophilic Bacillus strain PS3 by three different proteases produced a limited number of peptide fragments. In most cases, the peptides remained associated, and the gross structure of the beta subunit was not destroyed. Furthermore, most peptides were able to reassociate into the form of the beta subunit after denaturating urea treatment. Therefore, the cleaved sites are most likely located in water-exposed loop regions in the tertiary structure of the protein. Almost all peptides were analyzed, and 17 cleaved sites were determined. From the analysis of the distribution of cleaved sites and deletions or insertions in the multiple amino acid sequence alignment of proteins homologous to the beta subunit, locations of five loops and four candidate loops in the beta subunit are suggested. There are two large loops in the central region of the beta subunit sequence, and dicyclohexylcarbodiimide-reactive Glu190 is located in one of them. Tyr341, involved in putative catalytic ATP binding, is also found in one of the loops. Then, taking cleaved sites as a reference, two kinds of expression plasmids, each of which carried genes of two complementary peptide fragments, 1-193 and 198-473 or 1-284 and 285-473, were constructed and expressed in Escherichia coli. For each plasmid, two peptides were coexpressed, associated into a stable beta subunit form in E. coli cells, and purified without dissociation. When these beta subunits were denatured by urea and applied to polyacrylamide gel without denaturant, a protein band with the same mobility as that of the beta subunit appeared, indicating that reassociation of peptide fragments into the form of the beta subunit occurred upon removal of urea. These beta subunits retained the ability to reconstitute the alpha 3 beta 3 gamma complexes even though the efficiency of reconstitution and the recovered ATPase activities were decreased. These complexes were stable at high or low temperature, and ATPase activities were sensitive to inhibition by N3-.

Published
1992
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24. High Pressure Structures of Organic Low Dimensional Conductor DCNQI Compounds

Author

Kazumasa Oshima, S. Hayashi, T. Date, Y. Nogami, Kazushi Kanoda, and Ko-ichi Hiraki

Subjects
Condensed matter physics, Chemistry, General Chemistry, Crystal structure, Condensed Matter Physics, Mott transition, Conductor, Chemical physics, High pressure, X-ray crystallography, Condensed Matter::Strongly Correlated Electrons, General Materials Science, Metal–insulator transition, Charge density wave, Curse of dimensionality
Abstract

Using X-ray and DAC, room-temperature crystal structures under physical pressure (PP) were solved for DCNQI-Cu compounds which exhibit particular metal-insulator (M-I) transition owing to their electronic low dimensionality (CDW) and strong correlation (Mott). This M-I transition is known to be triggered with moderate (=small) PP or chemical substitution (chemical pressure:CP). Observed high pressure structures were compared with theoretical structure determinations. From the structural viewpoint, relation between PP and CP effects on the M-I transition was discussed.

Published
1998
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25. Structure and optical property of large size CaF 2 single crystals grown by the CZ method

Author

Eiichi Nishijima, Toshiro Mabuchi, Tsuguo Fukuda, T. Date, Teruhiko Nawata, Isao Masada, and Yoji Inui

Subjects
Materials science, business.industry, Physics::Optics, Crystal structure, law.invention, Crystal, Lens (optics), Optics, law, Homogeneity (physics), Photolithography, business, Single crystal, Lithography, Refractive index
Abstract

CaF 2 single crystals are required for the most suitable lens materials for the ArF laser lithography stepper because of its excellent transparency and laser durability in the DUV region. We have succeeded in growing the large size and high quality CaF 2 single crystals with both and orientation, and the diameter of 300mm by means of the Czochralski (CZ) method. The refractive index homogeneity is one of the most important optical properties required for the lithography lens material. Particularly, the residual homogeneity which is a high-order refractive index distribution after subtraction of Zernike 36 coefficient is very important. The vein-like striations were observed in the residual homogeneity pattern of the CaF 2 single crystals. The structure of CaF 2 single crystal correlating with the residual homogeneity is characterized by using the reflection X-ray topography. It is observed that the structure of CaF 2 single crystal composed with sub-grains parted by the small-angle tilt boundaries. The sub-grains are grown along the growth direction. It is understood that the large angle tilt type sub-boundaries among the domains composed of small sub-grains correspond to the vein-like striations. In the growth of CaF 2 single crystal, the sub-grain structure of seed is introduced into grown crystal. While the bending of crystal lattice plane from the neck toward the shoulder lead to the large angle tilt type sub-boundaries. Use of high crystalline seed and control of crystal lattice plane in the shoulder are effective in the growth of high crystalline CaF 2 single crystal getting good residual homogeneity.

Published
2006
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26. Biventricular involvement in cardiac sarcoidosis

Author

S Mochizuki, T Date, and Y Nakada

Subjects
medicine.medical_specialty, Systemic disease, Sarcoidosis, Heart Ventricles, Miscellanea, Ventricular tachycardia, Magnetic resonance angiography, Electrocardiography, Internal medicine, medicine, Humans, cardiovascular diseases, medicine.diagnostic_test, Bundle branch block, business.industry, Middle Aged, medicine.disease, medicine.anatomical_structure, Ventricle, Circulatory system, cardiovascular system, Cardiology, Female, Cardiology and Cardiovascular Medicine, business, Cardiomyopathies, Magnetic Resonance Angiography
Abstract

A 50 year old woman was admitted to our department to undergo an assessment of recurrent wide QRS tachycardia. An electrophysiologic study was performed. Ventricular tachycardia (VT) of three different morphologies, with left and right bundle branch block configurations, were induced with double extrastimuli from the right ventricle (left panel), thus suggesting that arrhythmogenic substrates existed in both the right and left ventricles. Endocardial mapping study showed that the site of earliest …

Published
2005

27. [Significance of interferon alpha therapy for advanced renal cell carcinoma. Fukushima Renal Cancer Study Group]

Author

M, Ogihara, K, Aikawa, T, Suzuki, T, Yanagida, N, Kushida, O, Yamaguchi, Y, Shiraiwa, K, Kumakawa, K, Koseki, S, Ichijo, T, Date, S, Kurosu, M, Takeuchi, J, Yokoyama, F, Murakami, K, Itoh, and M, Noguchi

Subjects
Male, Multivariate Analysis, Humans, Interferon-alpha, Female, Middle Aged, Prognosis, Carcinoma, Renal Cell, Survival Analysis, Kidney Neoplasms, Aged, Retrospective Studies
Abstract

We ranked prognostic factors to retrospectively evaluate the clinical significance of interferon alpha (IFN-alpha) therapy in patients with Robson stage IVB renal cell carcinoma. A total of 44 Robson stage IVB renal cancer patients were divided into 2 groups, one with more than 6 months administration of IFN-alpha (3-7 times a week: group A) and another without any IFN-alpha administration. The distribution of these 2 groups was not randomized. In addition to IFN-alpha therapy, survival was analyzed with respect to performance status (PS), mass reductive nephrectomy, concomitant use of other cytotoxic therapies, the number of metastatic organs, growth type, site of metastasis and the period of diagnosis, using a multivariate method with Cox proportional hazards regression. The multivariate analysis showed administration of IFN-alpha to be the most significant factor influencing a good prognosis. Improved survival was also significantly correlated with slow growing type and good PS. Among group A, a significant favorable prognosis was obtained in patients with the responses of no change (NC), partial response (PR) and complete remission (CR) 6 months after initiating administration of IFN-alpha, as well as with good PS and a slow growing type carcinoma. We conclude that IFN-alpha therapy might improve the prognosis of patients with Robson stage IVB renal cell carcinoma, especially, in cases when a greater than NC response is obtained after 6 months administration of IFN-alpha.

Published
2000

28. Mode analysis of a fatty acid molecule binding to the N-terminal 8-kDa domain of DNA polymerase beta. A 1:1 complex and binding surface

Author

Y, Mizushina, T, Ohkubo, T, Date, T, Yamaguchi, M, Saneyoshi, F, Sugawara, and K, Sakaguchi

Subjects
Binding Sites, Circular Dichroism, Fatty Acids, Escherichia coli, Animals, DNA Polymerase beta, Rats
Abstract

We reported previously that long-chain fatty acids are potent inhibitors of mammalian DNA polymerase beta. At present, based on information available from the NMR structure of the N-terminal 8-kDa domain, we examined the structural interaction with the 8-kDa domain using two species, C(18)-linoleic acid (LA) or C(24)-nervonic acid (NA). In the 8-kDa domain with LA or NA, the structure that forms the interaction interface included helix-1, helix-2, helix-4, the three turns (residues 1-13, 48-51, and 79-87) and residues adjacent to an Omega-type loop connecting helix-1 and helix-2 of the same face. No significant shifts were observed for any of the residues on the opposite side of the 8-kDa domain. The NA interaction interface on the amino acid residues of the 8-kDa domain fragment was mostly the same as that of LA, except that the shifted cross-peaks of Leu-11 and Thr-79 were significantly changed between LA and NA. The 8-kDa domain bound to LA or NA as a 1:1 complex with a dissociation constant (K(D)) of 1.02 or 2.64 mM, respectively.

Published
1999

29. Rat liver serine dehydratase. Bacterial expression and two folding domains as revealed by limited proteolysis

Author

H, Ogawa, F, Takusagawa, K, Wakaki, H, Kishi, M R, Eskandarian, M, Kobayashi, T, Date, N H, Huh, and H C, Pitot

Subjects
Male, L-Serine Dehydratase, Protein Denaturation, Protein Folding, DNA, Complementary, Hydrolysis, Serine Endopeptidases, Recombinant Proteins, Rats, Liver, Pyridoxal Phosphate, Escherichia coli, Animals, Trypsin, Cloning, Molecular, Rats, Wistar, Protein Binding
Abstract

A pCW vector harboring rat liver serine dehydratase cDNA was expressed in Escherichia coli. The expressed level was about 5-fold higher in E. coli BL21 than in JM109 cell extract; the former lacked two kinds of proteases. Immunoblot analysis revealed the occurrence of a derivative other than serine dehydratase in the JM109 cell extract. The recombinant enzyme was purified to homogeneity. Staphylococcus aureus V8 protease and trypsin cleaved the enzyme at Glu-206 and Lys-220, respectively, with a concomitant loss of enzyme activity. Spectrophotometrically, the nicked enzyme showed a approximately 50% reduced capacity for binding of the coenzyme pyridoxal phosphate and no spectral change of circular dichroism in the region at 300-480 nm, whereas circular dichroism spectra of both enzymes in the far-UV region were similar, suggesting that proteolysis impairs the coenzyme binding without an accompanying gross change of the secondary structure. Whereas the nicked enzyme behaved like the intact enzyme on Sephadex G-75 column chromatography, it was dissociated into two fragments on the column containing 6 M urea. Upon the removal of urea, both fragments spontaneously refolded. These results suggest that serine dehydratase consists of two folding domains connected by a region that is very susceptible to proteases.

Published
1999

30. [A case of thyroid sarcoidosis]

Author

T, Date, T, Kinoshita, M, Ishiki, M, Ejima, M, Taniguchi, M, Mochizuki, Y, Miyazawa, and A, Sakata

Subjects
Sarcoidosis, Prednisolone, Anti-Inflammatory Agents, Thyroid Gland, Thyroidectomy, Humans, Female, Middle Aged, Thyroid Diseases
Published
1995

31. NP-06: a novel anti-human immunodeficiency virus polypeptide produced by a Streptomyces species

Author

M Machida, Eiji Kojima, T Date, S Ishida, Masatoshi Tanaka, S Anderson, K Toyota, Kazuhiro Watanabe, Sudhichai Chokekijchai, and M Nomizu

Subjects
Pharmacology, Oligopeptide, biology, Molecular Sequence Data, Cystine, HIV, Biological activity, biology.organism_classification, Peripheral blood mononuclear cell, Streptomyces, Antiviral Agents, Peptides, Cyclic, Virus, In vitro, chemistry.chemical_compound, Infectious Diseases, chemistry, Biochemistry, Humans, Pharmacology (medical), Amino Acid Sequence, Peptide sequence, Research Article
Abstract

From an extract of a Streptomyces culture, we identified and purified a novel compound, NP-06, which is active against human immunodeficiency virus (HIV) in vitro. Analyses indicate that NP-06 is a hydrophobic 21-mer oligopeptide, N terminally cyclized through the side chain of Asp-9, containing two intramolecular cystine linkages with a molecular weight of 2,163.4. The 50% inhibitory concentrations were 2.8 and 1.3 microM when NP-06 was tested for in vitro anti-HIV-1 activity in ATH8 cells and phytohemagglutinin-activated peripheral blood mononuclear cells, respectively, NP-06 appears to block the early stage of HIV-1 infection, most likely at the stage of virus-cell fusion.

Published
1995

32. Synthesis and antiviral activities of 9-cyclopentylpurine derivatives

Author

E, Kojima, K, Ohta, S, Miyawaki, T, Date, M, Machida, and K, Murakami

Subjects
Structure-Activity Relationship, Avian Sarcoma Viruses, Adenine, Drug Evaluation, Preclinical, HIV-1, Animals, Stereoisomerism, Chick Embryo, Fibroblasts, In Vitro Techniques, Antiviral Agents
Abstract

The synthesis and anti-RSV (Rouse Sarcoma Virus) activity of HMCA, (+/-)-9-(2-hydroxymethyl-cyclopenthyl)-adenine, and its derivatives are described. It has been demonstrated that trans-HMCA has greater anti-RSV activity in tissue culture than cis-HMCA.

Published
1995

33. Poster Session 1

Author

A. Deshmukh, S. S. Sharma, F. G. Gobal, S. S. Singla, P. H. Hebbar, H. P. Paydak, M. Igarashi, H. Tada, Y. Sekiguchi, H. Yamasaki, K. Kuroki, T. Machino, K. Yoshida, K. Aonuma, J. Shavadia, H. Otieno, G. Yonga, A. Jinah, J. F. Qvist, P. H. Soerensen, U. Dixen, M. A. Ramirez-Marrero, B. Perez-Villardon, D. Gaitan-Roman, M. Jimenez-Navarro, J. L. Delgado-Prieto, E. De Teresa-Galvan, M. De Mora-Martin, P. B. Hebbar, W. X. Wei, S. Bardari, M. Zecchin, R. Salame', L. Vitali Serdoz, A. Di Lenarda, N. Guerrini, G. Barbati, G. Sinagra, K. Hanazawa, K. Kaitani, Y. Nakagawa, I. Lenaerts, R. Driesen, N. Hermida, H. Heidbuchel, S. Janssens, J. L. Balligand, K. R. Sipido, R. Willems, R. Sehra, D. Krummen, C. Briggs, S. Narayan, Y. Tanaka, K. Hirao, T. Nakamura, O. Inaba, A. Yagishita, K. Higuchi, H. Hachiya, M. Isobe, E. Kallergis, E. M. Kanoupakis, H. E. Mavrakis, C. A. Goudis, N. E. Maliaraki, P. E. Vardas, K. Kiuchi, C. Piorkowski, S. Kircher, T. Gaspar, N. Watanabe, A. Bollmann, G. Hindricks, K. Wauters, A. Grosse, S. Raffa, M. Brunelli, J. C. Geller, A. P. Maggioni, L. Gonzini, G. Gussoni, G. Vescovo, M. Gulizia, S. Pirelli, G. Mathieu, G. Di Pasquale, R. Salame, S. Magnani, T. Sakamoto, K. Kumagai, E. Fuke, S. Nishiuchi, T. Hayashi, Y. Miki, S. Naito, S. Oshima, I. E. Hof, E. Vonken, B. K. Velthuis, M. Meine, R. N. W. Hauer, K. P. Loh, J. O. Na, C. U. Choi, E. J. Kim, S. W. Rha, C. G. Park, H. S. Seo, D. J. Oh, H. E. Lim, D. Wichterle, V. Bulkova, M. Fiala, J. Chovancik, J. Simek, P. Peichl, R. Cihak, J. Kautzner, A. Glick, S. Viskin, B. Belhassen, A. Navarrete, F. Conte, A. Ishti, D. Sai, M. Moran, Z. Chitovova, H. Ahmed, K. Mares, J. Skoda, L. Sediva, J. Petru, V. Y. Reddy, P. Neuzil, M. Schmidt, U. Dorwarth, A. Leber, M. Wankerl, J. Krieg, F. Straube, S. Reif, E. Hoffmann, E. Mikhaylov, V. Tikhonenko, D. Lebedev, S. Y. Shin, H. S. Yong, J. I. Choi, S. H. Kim, S. Matsuo, T. Yamane, M. Hioki, K. Ito, R. Narui, T. Date, K. Sugimoto, M. Yoshimura, S. Rolf, P. Sommer, R. Batalov, S. Popov, I. Antonchenko, T. Suslova, S. Fichtner, U. Czudnochowsky, H. L. Estner, S. Ammar, T. Reents, C. Jilek, G. Hessling, I. Deisenhofer, E. Pokushalov, A. Romanov, G. Corbucci, S. Artemenko, D. Losik, V. Shabanov, A. Turov, D. Elesin, M. Abramov, P. Sanders, P. Jais, K. Roberts-Thomson, K. Fukumoto, S. Takatsuki, T. Kimura, N. Nishiyama, Y. Aizawa, T. Sato, S. Miyoshi, K. Fukuda, Y. Roux, J. Tenkorang, P. Carroz, J. Schlaepfer, P. Pascale, A. Forclaz, M. Fromer, E. Pruvot, L. Sknouril, R. Nevralova, M. Dorda, J. Januska, R. Santi, C. Geller, K. Nakamura, K. Kasseno, K. Taniguchi, A. Wutzler, M. Huemer, A. Parwani, L. H. Boldt, D. Blaschke, R. Dietz, W. Haverkamp, B. Coutu, R. Malanuk, M. Ait Said, A. Vicentini, S. Schade, K. Ando, A. Rousseauplasse, T. Deering, B. C. Picarra, A. R. Santos, P. Dionisio, P. Semedo, R. Matos, M. Leitao, A. Jacinto, M. Trinca, C. Wan, J. Glad, S. Szymkiewicz, M. Habibovic, H. Versteeg, A. J. M. Pelle, D. A. M. J. Theuns, L. Jordaens, S. S. Pedersen, S. Pakarinen, L. Toivonen, J. Taggeselle, A. Frey, A. Birkenhagen, S. Kohler, S. K. G. Maier, N. Lobitz, S. Paule, J. Becher, G. Mustafa, A. Ibrahim, G. King, B. Foley, B. Wilkoff, R. Freedman, D. Hayes, S. Kalbfleisch, S. Kutalek, R. Schaerf, I. A. Fazal, M. Tynan, C. J. Plummer, J. M. Mccomb, A. Oto, K. Aytemir, H. Yorgun, U. Canpolat, E. B. Kaya, L. Tokgozoglu, G. Kabakci, H. Ozkutlu, S. Greenberg, F. Hamati, R. Styperek, J. Alonso, D. Peress, O. Bolanos, R. Augostini, M. Pelini, S. Zhang, S. Stoycos, S. Witsaman, K. Mowrey, J. Bremer, A. Oza, G. Ciconte, P. Mazzone, G. Paglino, A. Marzi, P. Vergara, N. Sora, S. Gulletta, P. Della Bella, M. Nagashima, M. Goya, Y. Soga, K. Hiroshima, K. Andou, K. Hayashi, Y. An, M. Nobuyoshi, A. Kutarski, B. Malecka, R. Pietura, P. Osmancik, D. Herman, P. Stros, V. Kocka, P. Tousek, H. Linkova, M. Bortnik, E. Occhetta, G. Dell'era, A. Degiovanni, L. Plebani, P. N. Marino, M. V. Gorev, D. G. Alimov, P. Raju, S. Kully, S. Ugni, S. Furniss, G. Lloyd, N. R. Patel, M. W. Richards, C. E. Warren, M. H. Anderson, M. Hero, J. L. Rey, S. Ouali, S. Azzez, S. Kacem, S. Hammas, H. Ben Salem, E. Neffeti, F. Remedi, E. Boughzela, M. B. Kronborg, P. T. Mortensen, S. H. Poulsen, J. C. Nielsen, E. N. Simantirakis, J. E. Kontaraki, E. G. Arkolaki, S. I. Chrysostomakis, E. G. Nyktari, A. P. Patrianakos, R. C. Funck, C. Harink, H. H. Mueller, S. Koelsch, B. Maisch, V. Bolzani, P. Costandi, R. E. Shehada, N. Butala, B. Coppola, M. Taborsky, P. Heinc, M. Fedorco, V. Doupal, A. Di Cori, G. Zucchelli, E. Soldati, L. Segreti, R. De Lucia, S. Viani, L. Paperini, M. G. Bongiorni, K. J. Gutleben, W. Kranig, C. Barr, M. M. Morgenstern, M. Simon, Y. H. Dalal, M. Landolina, A. Pierantozzi, T. Agricola, M. Lunati, E. Pisano', G. Lonardi, G. Bardelli, G. Zucchi, B. Thibault, M. Dubuc, E. Karst, K. Ryu, P. Paiement, M. D. Carlson, T. Farazi, H. Alhous, L. Mont, J. M. Porres, J. Alzueta, X. Beiras, I. Fernandez-Lozano, A. Macias, R. Ruiz, J. Brugada, S. M. Viani, M. Seifert, T. Schau, V. Moeller, J. Meyhoefer, C. Butter, V. Ganiere, V. Niculescu, G. Domenichini, C. Stettler, P. Defaye, H. Burri, M. Stockburger, E. De Teresa, G. Lamas, M. Desaga, C. Koenig, E. Cobo, X. Navarro, U. Wiegand, M. Blich, S. Carasso, M. Suleiman, I. Marai, L. Gepstein, M. Boulos, M. Sasov, B. Liska, P. Margitfalvi, T. Malacky, M. Svetlosak, E. Goncalvesova, R. Hatala, Y. Takaya, T. Noda, Y. Yamada, H. Okamura, K. Satomi, W. Shimizu, N. Aihara, S. Kamakura, A. Proclemer, S. Boveda, H. Oswald, P. Scipione, A. Da Costa, W. Brzozowski, A. Tomaszewski, A. Wysokinski, E. Arbelo, D. Tamborero, B. Vidal, J. M. Tolosana, M. Sitges, M. Matas, G. L. Botto, C. D. Dicandia, M. Mantica, C. La Rosa, A. D' Onofrio, G. Molon, G. Raciti, R. Verlato, P. W. X. Foley, S. Chalil, K. Ratib, R. E. A. Smith, F. Printzen, A. Auricchio, F. Leyva, R. Abu Sham'a, J. Buber, D. Luria, R. Kuperstein, M. Feinberg, H. Granit, M. Eldar, M. Glikson, K. Vondrak, E. Nof, I. Lipchenca, R.- G. Vatasescu, C. Iorgulescu, C. Caldararu, A. Vasile, S. Bogdan, D. Constantinescu, M. Dorobantu, H. Sakaguchi, A. Miyazaki, T. Yamamoto, K. Fujimoto, S. Ono, H. Ohuchi, M. Martinelli, S. Martins, R. Molina, S. Siqueira, S. A. D. Nishioka, G. L. Peixoto, R. Alkmim-Teixeira, R. Costa, M. M. Meine, A. E. Tuinenburg, P. A. Doevendans, J. Denollet, K. Goscinska-Bis, I. Zupan, H. Van Der, F. Anselme, H. Hartog, M. Block, A. Borri, L. Padeletti, M. Toniolo, G. Zanotto, A. Rossi, E. Raytcheva, L. Tomasi, C. Vassanelli, I. Fernandez Lozano, C. Mitroi, J. Toquero Ramos, V. Castro Urda, V. Monivas Palomero, A. Corona Figueroa, L. Ruiz Bautista, L. Alonso Pulpon, A. S. Jadidi, F. Sacher, A. S. Shah, D. Scherr, N. Derval, M. Hocini, M. Haissaguerre, S. Castrejon Castrejon, C. Largo-Aramburu, J. Sachar, E. Gang, A. Estrada, D. Doiny, E. De Miguel, J. L. Merino, N. Trevisi, A. Ricco, F. Petracca, F. Baratto, A. Bisceglie, G. Maccabelli, A. El-Damaty, J. Sapp, J. Warren, P. Macinnis, M. Horacek, B. Dinov, R. Schoenbauer, F. Braunschweig, A. Arya, D. Andreu, A. Berruezo, J. T. Ortiz, E. Silva, T. M. De Caralt, J. Fernandez-Armenta, A. Perez-Silva, M. Ortega, J. L. Lopez-Sendon, F. Regoli, F. Faletra, G. Nucifora, E. Pasotti, T. Moccetti, C. Klersy, M. Casella, A. Dello Russo, M. Moltrasio, M. Zucchetti, G. Fassini, L. Di Biase, A. Natale, C. Tondo, N. Matsuhashi, H. J. Weig, G. Kerst, S. Weretk, P. Seizer, M. P. Gawaz, J. Schreieck, G. Sarquella-Brugada, F. Prada, C. M. Salling, C. Kolb, M. Pytkowski, A. Maciag, M. Farkowski, A. Jankowska, I. Kowalik, A. Kraska, H. Szwed, P. Maury, A. Duparc, P. Mondoly, A. Rollin, R. Pap, M. Kohari, G. Bencsik, A. Makai, L. Saghy, T. Forster, E. Ebrille, M. Scaglione, C. Raimondo, D. Caponi, P. Di Donna, A. Blandino, S. D. L. Delcre, F. Gaita, I. Roca Luque, L. D. S. Dos, N. R. G. Rivas, A. P. D. Pijuan, J. Perez, J. Casaldaliga, D. G. D. Garcia-Dorado, A. M. M. Moya, H. Sato, T. Yagi, T. Yambe, F. Streitner, C. Dietrich, E. Mahl, N. Schoene, C. Veltmann, M. Borggrefe, J. Kuschyk, P. P. Sadarmin, K. C. K. Wong, K. Rajappan, Y. Bashir, T. R. Betts, C. Leclercq, R. Martins, J. C. Daubert, P. Mabo, M. Koide, G. Hamano, T. Taniguchi, M. Yamato, N. Sasaki, K. Hirooka, Y. Ikeda, Y. Yasumura, W. Dichtl, T. Wolber, U. Paoli, S. Bruellmann, T. Berger, M. Stuehlinger, F. Duru, F. Hintringer, E. Kanoupakis, H. Mavrakis, E. Koutalas, I. Saloustros, C. Goudis, G. Chlouverakis, P. Vardas, J. M. Herre, M. Saeed, L. Saberi, S. Neuman, K. Yamaji, M. Iwabuchi, A. Baranchuk, F. Femenia, R. Miranda Hermosilla, J. C. Lopez Diez, J. L. Serra, M. Valentino, E. Retyk, N. Galizio, W. Kwasniewski, A. Filipecki, W. Orszulak, D. Urbanczyk-Swic, M. Trusz - Gluza, O. Piot, B. Degand, A. Donofrio, P. Scanu, A. Quesada, A. Kloppe, D. Mijic, H. Bogossian, M. Zarse, B. Lemke, J. Tyler, G. Comfort, T. F. Deering, A. E. Epstein, S. M. G. Greenberg, D. S. Goldman, J. Rhude, J. P. Majewski, J. Lelakowski, I. Tomala, C. M. Santos, R. S. Miranda, P. J. Sousa, D. M. Cavaco, P. P. Adragao, R. E. Knops, A. A. Wilde, M. Belhameche, J. S. Hermida, E. Dovellini, G. Frohlig, P. Siot, G. Z. Duray, C. W. Israel, J. Brachmann, K. H. Seidl, M. Foresti, F. Birkenhauer, S. H. Hohnloser, C. Ferreira, P. Mateus, H. Ribeiro, S. Carvalho, A. Ferreira, J. Moreira, W. Kadro, H. Rahim, M. Turkmani, M. Abu Lebdeh, A. Altabban, N. Cerrato, S. Rivera, F. Scazzuso, G. Albina, A. Klein, R. Laino, V. Sammartino, A. Giniger, T. Kvantaliani, M. Akhvlediani, M. Namdar, J. Steffel, S. Jetzer, F. Bayrak, G. B. Chierchia, R. Jenni, P. Brugada, Z. Bakos, M. M. Medvedev M, J. C. Jonas Carlsson, F. H. Fredrik Holmqvist, P. P. Pyotr Platonov, T. Nurbaev, M. Pirnazarov, A. Nikishin, P. Aagaard, A. Sahlen, L. Bergfeldt, E. Simeonidou, S. Kastellanos, C. Varounis, C. Michalakeas, C. Koniari, A. Nikolopoulou, M. Anastasiou-Nana, Y. Furukawa, T. Yamada, T. Morita, K. Tanaka, Y. Iwasaki, M. Kawasaki, Y. Kuramoto, M. Fukunami, C. Blanche, N. Tran, F. Rigamonti, M. Zimmermann, E. Okisheva, D. Tsaregorodtsev, V. Sulimov, D. Novikova, T. Popkova, E. Udachkina, Y. Korsakova, A. Volkov, A. Novikov, E. Alexandrova, E. Nasonov, P. Arsenos, K. Gatzoulis, G. Manis, P. Dilaveris, T. Gialernios, E. Kartsagoulis, S. Asimakopoulos, C. Stefanadis, M. Marocolo, O. Barbosa Neto, A. C. Carvalho, S. R. Marques Neto, G. R. Mota, P. R. B. Barbosa, A. Fernandez-Fernandez, S. Manzano Fernandez, F. J. Pastor-Perez, O. Barquero-Perez, R. Goya-Esteban, M. Salar, J. L. Rojo-Alvarez, A. Garcia-Alberola, M. Takigawa, M. Kawamura, T. Aiba, T. Sakaguchi, H. Itoh, M. Horie, T. Igarashi, J. Negishi, N. Toyota, O. Yamada, M. Papavasileiou, F. Cabrera Bueno, M. J. Molina Mora, J. Alzueta Rodriguez, A. Barrera Cordero, E. De Teresa Galvan, A. S. Revishvili, T. Dzhordzhikiya, O. Sopov, G. Simonyan, O. Lyadzhina, E. Fetisova, V. Kalinin, J. C. Balt, R. C. Steggerda, L. V. A. Boersma, M. C. E. F. Wijffels, E. F. D. Wever, J. M. Ten Berg, R. P. Ricci, L. Morichelli, A. D'onofrio, D. Vaccari, L. Calo', G. Buja, N. Rovai, A. Gargaro, J. Sperzel, G. Speca, L. Santini, J. Haarbo, K. Dubin, M. Carlson, A. Garcia Quintana, H. Mendoza-Lemes, L. Garcia Perez, S. Led Ramos, E. Caballero Dorta, M. Matinez De Espronceda, V. Piro Mastracchio, L. Serrano Arriezu, L. Sciarra, M. Marziali, E. Marras, M. Rebecchi, G. Allocca, E. Lioy, P. Delise, V. E. Santobuono, M. Iacoviello, F. Nacci, G. Luzzi, A. Puzzovivo, M. Memeo, F. Quadrini, S. Favale, M. E. Trucco, M. Arce, J. Palazzolo, W. Uribe, R. Maggi, T. Furukawa, F. Croci, A. Solano, M. Brignole, A. Lebreiro, A. Sousa, A. S. Correia, P. Lourenco, S. Oliveira, M. Paiva, J. Freitas, M. J. Maciel, N. Linker, G. Rieger, C. Garutti, N. Edvardsson, R. Salguero Bodes, M. De Riva Silva, A. Fontenla Cerezuela, M. Lopez Gil, E. Mejia Martinez, A. Jurado Roman, S. Garcia Alvarez, F. Arribas Ynsaurriaga, N. R. Petix, A. Del Rosso, V. Guarnaccia, A. Zipoli, F. Rabajoli, G. Foglia Manzillo, C. Tolardo, C. Checchinato, S. Chiaravallotti, M. Santarone, M. T. Spinnler, C. Podoleanu, A. Frigy, D. Dobreanu, C. Ginghina, and E. Carasca

Subjects
Lv function, medicine.medical_specialty, business.industry, Physiology (medical), Internal medicine, Cardiology, Medicine, Cardiology and Cardiovascular Medicine, business, Predictive value, Value (mathematics), Surgery
Abstract

was higher in the NRG (p 0.70 was the more accurate RT-MCE value to predict LV regional recovery with positive predictive value of 70% and negative predictive value of 56% (p

Published
2011
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34. Poster Session 4

Author

H. Tada, H. Yamasaki, Y. Sekiguchi, M. Igarashi, K. Kuroki, T. Machino, K. Yoshida, K. Aonuma, F. R. Heinzel, H. Forstner, P. Lercher, E. Bisping, B. Rotman, F. M. Fruhwald, B. M. Pieske, R. Dabrowski, I. Kowalik, A. Borowiec, E. Smolis-Bak, A. Trybuch, C. Sosnowski, H. Szwed, M. A. Baturova, A. Lindgren, Y. V. Shubik, B. Olsson, P. G. Platonov, K. C. Van Den Broek, J. Denollet, J. Widdershoven, N. Kupper, R. Allam, R. A. G. A. B. Allam, W. A. G. D. Y. Galal, H. A. Y. A. M. El-Damnhoury, A. Y. M. A. N. Mortada, J. Jimenez-Candil, A. Martin, J. Hernandez, F. Martin, M. Gallego, C. Martin-Luengo, J. G. Quintanilla, J. Moreno Planas, R. Molina-Morua, T. Archondo, M. J. Garcia-Torrent, N. Perez-Castellano, C. Macaya, J. Perez-Villacastin, J. Saiz, C. Tobon, J. F. Rodriguez, F. Hornero, J. M. Ferrero, K. Ito, T. Date, M. Kawai, M. Hioki, R. Narui, S. Matsuo, M. Yoshimura, T. Yamane, N. Tabatabaei, G. Lin, B. D. Powell, R. Smairat, J. F. Glockner, P. A. Brady, S. Fichtner, U. Czudnochowsky, H. Estner, T. Reents, C. Jilek, S. Ammar, G. Hessling, I. Deisenhofer, D. C. Shah, J. Kautzner, N. Saoudi, C. Herrera, P. Jais, G. Hindricks, P. Neuzil, K. H. Kuck, K. C. K. Wong, M. Jones, N. Qureshi, A. Muthumala, T. R. Betts, Y. Bashir, K. Rajappan, T. Vogtmann, M. Wagner, J. Schurig, P. Hein, B. Hamm, G. Baumann, A. Lembcke, B. Saad, C. Slater, L. A. Oliveira, R. Elias, A. Camiletti, D. Moura, P. Maldonado, L. E. Camanho, A. Bulava, J. Hanis, D. Sitek, A. Novotny, W. B. Chik, T. W. Lim, H. K. Choon, V. A. See, R. Mccall, L. Thomas, D. L. Ross, S. P. Thomas, J. Chen, A. De Bortoli, O. Rossvoll, P. I. Hoff, E. Solheim, L. Z. Sun, P. Schuster, O. J. Ohm, A. V. Ardashev, E. Zhelyakov, M. S. Rybachenko, A. V. Konev, Y. U. N. Belenkov, M. Gunawardene, K. R. J. Chun, B. Schulte-Hahn, V. Windhorst, M. Kulikoglu, B. Nowak, B. Schmidt, G. A. Albina, R. S. Rivera, F. Scazzuso, R. L. Laino, G. A. Giniger, E. Arbelo, N. Calvo, D. Tamborero, D. Andreu, R. Borras, A. Berruezo, J. Brugada, L. Mont, L. Stefan, M. Eisenberger, E. Celentano, P. Peytchev, O. Bodea, P. Geelen, T. De Potter, M. M. Oliveira, N. Silva, P. S. Cunha, J. Feliciano, A. Lousinha, A. Toste, S. Santos, R. C. Ferreira, H. Matsuda, T. Harada, K. Soejima, Y. Ishikawa, K. Mizukoshi, T. Sasaki, K. Mizuno, F. Miyake, P. P. Adragao, D. Cavaco, R. Miranda, M. Santos, F. Morgado, K. Reis Santos, R. Candeias, S. Marcelino, F. Zoppo, G. Grandolino, F. Zerbo, E. Bertaglia, S. M. Schlueter, O. Grebe, E. G. Vester, A. L. Miracle Blanco, A. Arenal Maiz, F. Atienza Fernandez, T. Datino Romaniega, E. Gonzalez Torrecilla, G. Eidelman, J. Hernandez Hernandez, F. Fernandez Aviles, K. Fukumoto, S. Takatsuki, T. Kimura, N. Nishiyama, Y. Aizawa, T. Sato, S. Miyoshi, K. Fukuda, B. Richter, M. Gwechenberger, A. Socas, G. Zorn, S. Albinni, M. Marx, J. Wojta, H. Goessinger, T. Deneke, O. Balta, M. Paesler, K. Buenz, H. Anders, M. Horlitz, A. Muegge, D.- I. Shin, K. Natsuyama, K. M. Yamaguchi, Y. N. Nishida, J. Kosiuk, K. Bode, A. Arya, C. Piorkowski, T. Gaspar, P. Sommer, A. Bollmann, D. Wichterle, P. Peichl, J. Simek, S. Havranek, V. Bulkova, R. Cihak, A. Jurado Roman, R. Salguero Bodes, M. Lopez Gil, A. Fontenla Cerezuela, M. De Riva Silva, F. Arribas Ynsaurriaga, A. I. Fernandez Herranz, S. De Dios Perez, A. S. Revishvili, M. Dishekov, Z. Tembotova, S. Barsamyan, D. Vaccari, C. Alvarenga, I. Jesus, J. Layher, A. Takahashi, N. Singh, P. Siot, J. P. Elkaim, I. Savelieva, L. Mcclelland, A. Lovegrove, S. Jones, J. Camm, A. F. Folino, R. Breda, P. Calzavara, J. Comisso, F. Borghetti, S. Iliceto, G. Buja, R. Mlynarski, A. Mlynarska, M. Sosnowski, J. Wilczek, P. Mabo, G. Carrault, P. Bordachar, A. Makdissi, L. Duchemin, C. Alonso, G. Neri, G. Masaro, S. Vittadello, A. Gardin, A. Barbetta, F. Di Gregorio, E. Sciaraffia, M. R. Ginks, J. S. Gustafsson, M. C. Hollmark, C. A. Rinaldi, C. Blomstrom Lundqvist, S. Brusich, D. Tomasic, B. Ferek-Petric, Z. Mavric, A. Kutarski, B. Malecka, A. Kolodzinska, M. Grabowski, E. V. Dovellini, L. Giurlani, G. Cerisano, N. Carrabba, R. Valenti, D. Antoniucci, G. Opolski, G. Tomassoni, J. Baker, R. Corbisiero, D. Martin, I. Niazi, R. Sheppard, J. Sperzel, K. Gutleben, J. Petru, L. Sediva, J. Skoda, P. Mazzone, G. Ciconte, P. Vergara, A. Marzi, G. Paglino, N. Sora, S. Gulletta, P. Della Bella, R. Pietura, M. Czajkowski, N. Cabanelas, V. P. Martins, M. Alves, F. X. Valente, L. Marta, A. Francisco, R. Silva, G. Ferreira Da Silva, Y. Huo, F. Holmqvist, J. Carlson, U. Wetzel, P. Platonov, E. Nof, R. Abu Shama, R. Kuperstein, M. S. Feinberg, M. Eldar, M. Glikson, D. Luria, P. Kubus, O. Materna, R. A. Gebauer, T. Matejka, R. Gebauer, T. Tlaskal, J. Janousek, A. Muessigbrodt, S. Richter, M. Stockburger, S. Boveda, P. Defaye, P. Stancak Branislav, G. Kaliska, M. Rolando, J. Moreno, M.- A. G. Ohlow, B. Lauer, B. Buchter, M. Schreiber, J. C. Geller, J. E. Val-Mejias, S. Ouali, S. Azzez, S. Kacem, H. Ben Salem, S. Hammas, E. Neffeti, F. Remedi, E. Boughzela, H. Miyazaki, S. Miyanaga, K. Shibayama, M. Tokuda, T. Kudo, B. Coppola, R. E. N. Shehada, P. Costandi, J. Healey, S. H. Hohnloser, M. R. Gold, A. Capucci, I. C. Van Gelder, M. Carlson, C. P. Lau, S. J. Connolly, M. D. Bogaard, G. E. Leenders, B. Maskara, A. E. Tuinenburg, P. Loh, R. N. Hauer, P. A. Doevendans, M. Meine, B. Thibault, M. Dubuc, E. Karst, K. Ryu, P. Paiement, T. Farazi, V. Puetz, C. Berndt, J. Buchholz, A. Dorszewski, C. Mornos, D. Cozma, A. Ionac, L. Petrescu, A. Mornos, S. Pescariu, M. Benser, G. Roscoe, S. De Jong, G. Roberts, P. Boileau, A. Rec, C. Folman, A. Morttada, M. Abd El Kader, R. Samir, R. Roushdy, S. Khaled, M. Abo El Maaty, B. Van Gelder, P. Houthuizen, F. A. Bracke, J. Osca Asensi, D. Tejada, J. M. Sanchez, B. Munoz, O. Cano, M. Rodriguez, M. J. Sancho-Tello, J. Olague, W. Hou, S. Rosenberg, S. Koh, J. Poore, J. Snell, M. Yang, D. Nirav, G. Bornzin, T. Deering, D. Dan, A. C. Wickliffe, S. Cazeau, K. Karimzadeh, S. Mukerji, C. Loghin, B. Kantharia, M. A. Jones, J. Lamba, C. S. Simpson, D. P. Redfearn, K. A. Michael, M. Fitzpatrick, A. Baranchuk, M. Heinke, B. Ismer, H. Kuehnert, R. Surber, A. M. Haltenberger, D. Prochnau, H. R. Figulla, N. Delarche, O. Bizeau, P. Couderc, A. Chapelet, W. Amara, A. Lazarus, S. Krupickova, C. J. M. Van Deursen, M. Strik, K. Vernooy, A. Van Hunnik, M. Kuiper, H. J. G. M. Crijns, F. W. Prinzen, N. Islam, D. Gras, W. Abraham, L. Calo, U. Birgersdotter-Green, C. Clyne, J. Herre, N. Klein, O. Kowalski, R. Lenarczyk, P. Pruszkowska, A. Sokal, T. Kukulski, T. Zielinska, S. Pluta, Z. Kalarus, J. O. Schwab, M. Gasparini, F. Anselme, J. Clementy, M. Santini, J. Martinez Ferrer, V. Burrone, E. Santi, R. Nevzorov, A. Porter, J. Kusniec, G. Golovchiner, T. Ben-Gal, B. Strasberg, M. Haim, R. Rordorf, S. Savastano, A. Sanzo, A. Vicentini, B. Petracci, M. De Amici, L. Striuli, M. Landolina, J. M. Tolosana, A. M. Martin, A. Hernandez-Madrid, A. Macias, I. Fernandez-Lozano, J. Osca, A. Quesada, Y. Noguchi, S. Shahrzad, N. Karim Soleiman, A. Tavoosi, S. Taban, Z. Emkanjoo, M. Fukunaga, M. Goya, K. Hiroshima, M. Ohe, K. Hayashi, M. Iwabuchi, H. Nosaka, M. Nobuyoshi, D. Doiny, A. Perez-Silva, S. Castrejon Castrejon, A. Estrada, M. Ortega, J. L. Lopez-Sendon, J. L. Merino, F. J. Garcia Fernandez, R. Gallardo, M. Pachon, J. Almendral, J. Martin, D. Yahya, B. Al-Mogheer, S. Gouda, E. Eweis, M. El Ramly, A. Abdelwahab, W. Kassenberg, F. H. M. Wittkampf, I. E. Hof, J. H. Heijden, K. G. E. J. Neven, R. N. W. Hauer, F. Baratto, E. Bignami, F. Pappalardo, G. Maccabelli, D. Nicolotti, A. Zangrillo, M. Nagashima, Y. An, A. Okreglicki, C. Russouw, R. Tilz, Y. Yoshiga, S. Mathew, A. Fuernkranz, A. Rillig, E. Wissner, F. Ouyang, A. De Sisti, J. Tonet, F. Gueffaf, F. Touil, P. Aouate, F. Hidden-Lucet, H. Makimoto, K. Satomi, Y. Yamada, H. Okamura, T. Noda, W. Shimizu, N. Aihara, S. Kamakura, A. Perez Silva, S. Castrejon, M. Gonzalez Vasserot, J. Senges, J. Brachmann, D. Andresen, E. Hoffmann, B. Schumacher, S. Willems, B. Springer, C. Kolb, F. Akca, T. Bauernfeind, N. M. S. De Groot, B. Schwagten, M. Witsenburg, L. Jordaens, T. Szili-Torok, Y. Hata, R. Nakagami, T. Watanabe, A. Sato, H. Watanabe, T. Kabutoya, T. Mituhashi, D. A. M. J. Theuns, T. Smith, S. S. Pedersen, L. Dabiri-Abkenari, M. W. Prull, S. Unverricht, A. Bittlinsky, H. Wirdemann, B. Sasko, S. Wirdeier, H. J. Trappe, E. Zorio Grima, J. Rueda, P. Medina, T. Jaijo, T. Sevilla, M. A. Arnau, A. Salvador, A. H. Starrenburg, K. Kraaier, M. F. Scholten, J. Van Der Palen, S. De Haan, J. Commandeur, K. De Boer, A. M. Beek, A. C. Van Rossum, C. P. Allaart, P. Berne, J. M. Porres, J. A. Arnaiz, R. Brugada, S. Man, A. C. Maan, J. Thijssen, E. E. Van Der Wall, M. J. Schalij, L. Burattini, R. Burattini, C. A. Swenne, A. Bonny, I. Ditah, F. Larrazet, R. Frank, G. Fontaine, P. H. Van Der Voort, M. Alings, A. Shimane, K. Okajima, G. Kanda, K. Yokoi, S. Yamada, Y. Taniguchi, T. Hayashi, T. Kajiya, M. C. Santos, J. Wright, J. Betts, R. Denman, L. Dominguez-Perez, M. A. Arias Palomares, J. Toquero, E. Diaz-Infante, L. Tercedor, I. Valverde, A. Napp, S. Joosten, D. Stunder, M. Zink, N. Marx, P. Schauerte, J. Silny, M. E. Trucco, M. Arce, J. Palazzolo, F. Femenia, J. M. Glad, S. J. Szymkiewicz, J. Fernandez-Armenta, O. Camara, L. L. Mont, E. Diaz, E. Silva, A. Frangi, B. Brembilla-Perrot, F. Laporte, J. Morinigo, C. Ledesma, C. Hadid, M. Ortiz, C. Wolpert, E. Cobo, X. Navarro, F. Arribas, Y. Miki, S. Naitoh, K. Kumagai, K. Goto, K. Kaseno, S. Oshima, K. Taniguchi, S. Rivera, G. Albina, A. Klein, R. Laino, V. Sammartino, A. Giniger, M. Muggenthaler, H. Raju, M. Papadakis, N. Chandra, R. Bastiaenen, E. R. Behr, S. Sharma, N. Samniah, Y. Radezishvsky, H. Omari, U. Rosenschein, A. R. Perez Riera, M. Ferreira, W. M. Hopman, W. F. Mcintyre, A. R. Baranchuk, W. Wongcharoen, K. Keanprasit, A. Phrommintikul, R. Chaiwarith, A. Yagishita, H. Hachiya, T. Nakamura, Y. Tanaka, K. Higuchi, M. Kawabata, K. Hirao, M. Isobe, V. Stoickov, S. Ilic, M. Deljanin Ilic, P. Aagaard, A. Sahlen, L. Bergfeldt, F. Braunschweig, A. Sousa, A. Lebreiro, C. Sousa, S. Oliveira, A. S. Correia, I. Rangel, J. Freitas, M. J. Maciel, E. Asensio Lafuente, A. A. C. Aguilera, M. A. C. C. Corral, K. L. M. C. Mendoza, P. E. N. D. Nava, A. L. R. C. Rendon, L. V. C. Villegas, L. C. M. Castillo, R. Schaerf, R. Develle, C. Oliver, P. Y. Zinzius, R. A. Providencia, A. Botelho, J. Trigo, J. Nascimento, N. Quintal, P. Mota, A. M. Leitao-Marques, J. Borbola, P. Abraham, C. S. Foldesi, A. Kardos, S. Almeida, M. B. Santos, R. Quaresma, F. B. Morgado, P. Adragao, M. Fatemi, R. Didier, G. Le Gal, Y. Etienne, Y. Jobic, M. Gilard, J. Boschat, J. Mansourati, M. Zubaid, W. Rashed, A. Alsheikh-Ali, W. Almahmeed, A. Shehab, K. Sulaiman, N. Asaad, H. Amin, L. V. A. Boersma, M. Swaans, M. Post, B. Rensing, K. Jarverud, M. Broome, K. Noren, T. Svensson, S. Hjelm, M. Hollmark, A. Bjorling, K. Maeda, M. Takagi, K. Suzuki, H. Tatsumi, M. Yoshiyama, E. Simeonidou, C. Michalakeas, S. Kastellanos, C. Varounis, A. Nikolopoulou, C. Koniari, M. Anastasiou-Nana, T. Furukawa, R. Maggi, C. Bertolone, D. Fontana, M. Brignole, A. Z. Pietrucha, M. Wnuk, I. Bzukala, D. Mroczek-Czernecka, E. Konduracka, O. Kruszelnicka, W. Piwowarska, J. Nessler, N. Edvardsson, G. Rieger, C. Garutti, N. Linker, C. Jorge, J. Silva Marques, A. Veiga, J. Cruz, M. J. Correia, J. Sousa, G. Miltenberger-Miltenyi, A. Nunes Diogo, D. Matic, I. Mrdovic, G. Stankovic, M. Asanin, N. Antonijevic, M. Matic, N. Kocev, Z. Vasiljevic, M. A. Ramirez-Marrero, B. Perez-Villardon, J. L. Delgado-Prieto, M. Jimenez-Navarro, E. De Teresa-Galvan, M. De Mora-Martin, K. Sztefko, A. Malek, N. De Groot, T. Shalganov, M. Schalij, N. Rivas, J. Casaldaliga, I. Roca, A. Pijuan, J. Perez-Rodon, L. Dos, D. Garcia-Dorado, A. Moya, A.- E. Baruteau, A. Behaghel, S. Chatel, J. J. Schott, J. C. Daubert, H. Le Marec, V. Probst, J. Navarro-Manchon, P. Molina, B. Igual, M. Bermejo, J. Giner, V. J. A. Bourgonje, M. A. Vos, S. Ozdemir, N. Doisne, M. A. G. Van Der Heyden, A. A. B. Van Veen, K. Sipido, G. Antoons, P. I. Altieri, N. Escobales, M. Crespo, H. L. Banchs, L. Sciarra, R. Bloise, G. Allocca, E. Marras, E. Lioy, P. Delise, S. Priori, and L. Calo'

Subjects
medicine.medical_specialty, business.industry, Physiology (medical), Internal medicine, Diastole, medicine, Cardiology, Cardiology and Cardiovascular Medicine, business
Abstract

spectively), (p

Published
2011
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35. Mutation of histidine 373 to leucine in cytochrome P450c17 causes 17 alpha-hydroxylase deficiency

Author

S, Monno, H, Ogawa, T, Date, M, Fujioka, W L, Miller, and M, Kobayashi

Subjects
Adult, Male, Adolescent, Molecular Sequence Data, Restriction Mapping, Transfection, Polymerase Chain Reaction, Cell Line, Leucine, Leukocytes, Animals, Humans, Point Mutation, Histidine, Amino Acid Sequence, Codon, Alleles, DNA Primers, Adrenal Hyperplasia, Congenital, Base Sequence, Steroid 17-alpha-Hydroxylase, DNA, Exons, Blotting, Southern, Mutagenesis, Site-Directed, Female
Abstract

We identified a new homozygous missense mutation His373--Leu in the CYP17 gene of two sisters with 17 alpha-hydroxylase deficiency with an elevated plasma aldosterone concentration by sequencing their genomic DNAs amplified by polymerase chain reaction. Using polymerase chain reaction-based site-directed mutagenesis, we prepared a DNA that encoded the Leu373 mutant protein. COS-1 cells transfected with the mutant DNA, despite having an RNA hybridizable to the P450c17 cDNA, did not show 17 alpha-hydroxylase and 17,20-lyase activities. Also, the cells were devoid of 11 beta-hydroxylase and aldosterone synthase activities. To examine the mechanism by which the single amino acid change His373--Leu eliminates activity, we expressed N-terminally modified P450c17 proteins with and without the Leu373 mutation in Escherichia coli and performed spectral studies. Membrane preparations from E. coli cells expressing the wild-type form of the modified enzyme showed an absorption peak at 449 nm upon addition of carbon monoxide in the reduced state and produced characteristic substrate-induced difference spectra, whereas those from the cells expressing the mutant form did not show these spectral changes. The 17 alpha-hydroxylase and 17,20-lyase activities were observed only in E. coli cells expressing the wild-type enzyme. These results show that the His373--Leu mutant does not incorporate the heme prosthetic group properly and suggest a critical role of His373 in heme binding.

Published
1993

36. Expression of active human DNA ligase I in Escherichia coli cells that harbor a full-length DNA ligase I cDNA construct

Author

H, Teraoka, H, Minami, S, Iijima, K, Tsukada, O, Koiwai, and T, Date

Subjects
DNA, Complementary, Base Sequence, DNA Ligases, Molecular Sequence Data, Chromatography, Ion Exchange, Recombinant Proteins, DNA Ligase ATP, Escherichia coli, Humans, Electrophoresis, Polyacrylamide Gel, Amino Acid Sequence, Cloning, Molecular, Codon, Protein Processing, Post-Translational, Plasmids
Abstract

A recombinant plasmid for expression of full-length human DNA ligase I (phLig-I) was constructed in a plasmid/phage chimeric vector, pTD-T7N, which was derived from pUC118 by oligonucleotide-directed mutagenesis. The insert contained a 2757-base pair coding sequence for a whole human DNA ligase I and an extra ACC codon adjacent to the ATG initiation codon. This ACC codon was required for achieving high levels of expression of full-length DNA ligase I in Escherichia coli strain BL21. The recombinant plasmid, which was designed to exploit the T7 late promoter and the ATG initiation codon for beta-galactosidase was transfected into E. coli BL21 cells that express T7 RNA polymerase. The recombinant clone produced relatively high levels of DNA ligase I with a molecular mass of 130 kDa, as estimated by SDS-polyacrylamide gel electrophoresis. The DNA ligase was purified to near-homogeneity by the two-step column chromatographic procedure from BLphLig-I cells that had been induced with isopropyl beta-D-thiogalactoside. The specific activity, chromatographic behavior, kinetic properties, molecular mass, and antigenicity of the recombinant human DNA ligase I were indistinguishable from those of purified mammalian DNA ligase I. Metabolically labeling experiments with 32P(i) indicate that the recombinant DNA ligase I was present as an enzyme-AMP reaction intermediate, but not as a phosphoprotein, in the E. coli cells.

Published
1993

37. Molecular dissection of the beta subunit of F1-ATPase into peptide fragments

Author

K, Tozawa, M, Odaka, T, Date, and M, Yoshida

Subjects
Proton-Translocating ATPases, Base Sequence, Oligodeoxyribonucleotides, Macromolecular Substances, Endopeptidases, Molecular Sequence Data, Mutagenesis, Site-Directed, Bacillus, Electrophoresis, Polyacrylamide Gel, Amino Acid Sequence, Peptide Fragments, Plasmids, Substrate Specificity
Abstract

Partial digestion of the native beta subunit of F1-ATPase from the thermophilic Bacillus strain PS3 by three different proteases produced a limited number of peptide fragments. In most cases, the peptides remained associated, and the gross structure of the beta subunit was not destroyed. Furthermore, most peptides were able to reassociate into the form of the beta subunit after denaturating urea treatment. Therefore, the cleaved sites are most likely located in water-exposed loop regions in the tertiary structure of the protein. Almost all peptides were analyzed, and 17 cleaved sites were determined. From the analysis of the distribution of cleaved sites and deletions or insertions in the multiple amino acid sequence alignment of proteins homologous to the beta subunit, locations of five loops and four candidate loops in the beta subunit are suggested. There are two large loops in the central region of the beta subunit sequence, and dicyclohexylcarbodiimide-reactive Glu190 is located in one of them. Tyr341, involved in putative catalytic ATP binding, is also found in one of the loops. Then, taking cleaved sites as a reference, two kinds of expression plasmids, each of which carried genes of two complementary peptide fragments, 1-193 and 198-473 or 1-284 and 285-473, were constructed and expressed in Escherichia coli. For each plasmid, two peptides were coexpressed, associated into a stable beta subunit form in E. coli cells, and purified without dissociation. When these beta subunits were denatured by urea and applied to polyacrylamide gel without denaturant, a protein band with the same mobility as that of the beta subunit appeared, indicating that reassociation of peptide fragments into the form of the beta subunit occurred upon removal of urea. These beta subunits retained the ability to reconstitute the alpha 3 beta 3 gamma complexes even though the efficiency of reconstitution and the recovered ATPase activities were decreased. These complexes were stable at high or low temperature, and ATPase activities were sensitive to inhibition by N3-.

Published
1992

38. Distribution of PCNA in Drosophila embryo during nuclear division cycles

Author

Masamitsu Yamaguchi, T. Date, and Akio Matsukage

Subjects
Cytoplasm, Embryo, Nonmammalian, Cell division, Mitosis, Biology, Giant Cells, Antibody Specificity, Proliferating Cell Nuclear Antigen, medicine, Animals, Telophase, Metaphase, Interphase, Anaphase, Cell Nucleus, Nuclear Proteins, Biological Transport, Cell Biology, Cell cycle, Molecular biology, Immunohistochemistry, Cell nucleus, medicine.anatomical_structure, Drosophila, Cell Division
Abstract

An immunocytochemical method using a specific antibody was employed to detect the proliferating cell nuclear antigen (PCNA) in Drosophila embryos during the first 13 nuclear division cycles. Strong nuclear staining with the anti-PCNA antibody was observed at interphase throughout 13 cycles. Metaphase chromosomes were not stained throughout these cycles. The chromosomal (nuclear) staining reappeared at anaphase until cycle 10 and at telophase in cycle 11. During cycles 12 and 13, nuclear staining was detected exclusively at interphase. Relatively uniform staining of syncytial cytoplasm was observed throughout mitotic phases until cycle 9. In the following cycles, strong staining in both the central yolk mass and the cortical layer of cytoplasm was detected at metaphase and telophase. During interphase of cycles later than the 9th, staining in the central yolk mass got much fainter and that in the cortical cytoplasm completely disappeared. These results suggest that the PCNA dissociates from chromosomes at metaphase; then in later mitotic phases, it is transported from the syncytial cytoplasm into nuclei to participate in formation of the active DNA-replication enzyme complexes.

Published
1991

39. Inactivation of DNA polymerase beta by in vitro phosphorylation with protein kinase C

Author

T, Tokui, M, Inagaki, K, Nishizawa, R, Yatani, M, Kusagawa, K, Ajiro, Y, Nishimoto, T, Date, and A, Matsukage

Subjects
Binding Sites, Macromolecular Substances, Myocardium, Molecular Sequence Data, Brain, DNA, Single-Stranded, Alkaline Phosphatase, DNA Polymerase I, Chromatography, Affinity, Recombinant Proteins, Rats, Substrate Specificity, Kinetics, Escherichia coli, Animals, Amino Acid Sequence, Phosphorylation, Protein Kinase C
Abstract

The Mr = 38,300 polypeptide of the purified recombinant rat DNA polymerase beta served as an excellent substrate for protein kinase C (PKC) in vitro but not for the catalytic subunit of cAMP-dependent protein kinase. The phosphorylation by PKC resulted in inactivation of DNA polymerase beta activity, and recovery was achieved by dephosphorylation with alkaline phosphatase. Since the phosphorylated DNA polymerase beta was retained with use of a single-stranded DNA-cellulose column, inactivation might occur at a site different from that for the DNA binding. Amino acid sequence analysis of the phosphopeptides revealed that the phosphorylated sites were 2 serine residues at positions 44 and 55 from the NH2 terminus, either or both of which might be involved in the catalytic activity of DNA polymerase beta. Thus, the inactivation of the DNA repair enzyme, DNA polymerase beta, by PKC may be an important process in the modification of DNA metabolism in the nucleus through signal transduction processes.

Published
1991

40. [Genotype of hepatitis C virus in Japan]

Author

T, Nakao, T, Date, N, Enomoto, and A, Takada

Subjects
Genes, Viral, Genotype, Japan, Hepacivirus, Polymerase Chain Reaction, Polymorphism, Restriction Fragment Length
Published
1991

41. Synthesis of halogen-substituted 1,5-benzothiazepine derivatives and their vasodilating and hypotensive activities

Author

Sakae Murata, T Date, H. Otsuka, T. Hashiyama, K. Takahashi, H. Inoue, K Aoe, M. Gaino, M Konda, and Mikio Takeda

Subjects
Male, Chemical Phenomena, medicine.drug_class, Thiazepines, Guinea Pigs, Stereoisomerism, Vasodilation, Calcium channel blocker, chemistry.chemical_compound, Diltiazem, Structure-Activity Relationship, Dogs, Coronary Circulation, Rats, Inbred SHR, Drug Discovery, medicine, Structure–activity relationship, Animals, Antihypertensive Agents, Bicyclic molecule, Chemistry, Biological activity, Calcium Channel Blockers, Combinatorial chemistry, Rats, Lactam, Molecular Medicine, medicine.drug
Abstract

In an attempt to improve the effectiveness and duration of the action of diltiazem (1), a 1,5-benzothiazepine calcium channel blocker, its derivatives (2) with halogen substituents on the fused benzene ring were synthesized. These compounds were evaluated for their effects on vertebral and coronary blood flows and antihypertensive activity. The structure-activity relationships are discussed. The 8-chloro derivative ((+)-2b), the most potent compound in this series, was selected for clinical evaluation as a cerebral vasodilating and antihypertensive agent.

Published
1991

42. Structure of an ATPase operon of an acidothermophilic archaebacterium, Sulfolobus acidocaldarius

Author

T Date, Tairo Oshima, Jin Konishi, K Hajiro, Kimitoshi Denda, and Masasuke Yoshida

Subjects
Sulfolobus acidocaldarius, DNA, Bacterial, Operon, ATPase, Protein subunit, Molecular Sequence Data, Regulatory Sequences, Nucleic Acid, Biochemistry, trp operon, gal operon, Amino Acid Sequence, Amino Acids, Cloning, Molecular, Promoter Regions, Genetic, Molecular Biology, Adenosine Triphosphatases, Terminator Regions, Genetic, biology, Base Sequence, ATPase complex, Nucleic acid sequence, Cell Biology, Molecular biology, Archaea, Genes, Bacterial, biology.protein, Ribosomes
Abstract

The nucleotide sequence of the operon of the ATPase complex of an acidothermophilic archaebacterium, Sulfolobus acidocaldarius, has been determined. In addition to the three previously reported genes for the alpha, beta, and c (proteolipid) subunits of the ATPase complex (Denda, K., Konishi, J., Oshima, T., Date, T., and Yoshida, M. (1989) J. Biol. Chem. 264, 7119-7121), the operon contained three other genes encoding hydrophilic proteins with molecular masses 25, 13, and 7 kDa. The 25-kDa protein is the third largest subunit (gamma), the 13-kDa protein is most likely the fourth subunit (delta), and the 7-kDa protein may correspond to an unknown subunit of the ATPase, tentatively named as epsilon subunit. They do not have significant sequence similarity to subunits in F0F1-ATPases and eukaryotic V-type ATPases, whereas the other three subunits, alpha, beta, and c, have homologous counterparts in F0F1- and V-type ATPases. The order of the genes in the operon was delta alpha beta gamma epsilon c. The S. acidocaldarius ATPase operon differed from the eucabacterial F0F1-ATPase operon in that the former contains only one gene for a hydrophobic subunit at the most downstream part of the operon whereas the latter has three hydrophobic F0 genes preceding five hydrophilic F1 genes.

Published
1990

43. Site-directed mutagenesis of rat liver S-adenosylhomocysteinase. Effect of conversion of aspartic acid 244 to glutamic acid on coenzyme binding

Author

T, Gomi, Y, Takata, T, Date, M, Fujioka, R R, Aksamit, P S, Backlund, and G L, Cantoni

Subjects
Aspartic Acid, Binding Sites, Base Sequence, Hydrolases, Adenosylhomocysteinase, Molecular Sequence Data, Glutamic Acid, NAD, Recombinant Proteins, Molecular Weight, Kinetics, Apoenzymes, Glutamates, Liver, Mutation, Escherichia coli, Cloning, Molecular, Oligonucleotide Probes
Abstract

Aspartic acid 244 that occurs at the putative NAD(+)-binding site of rat liver S-adenosylhomocysteinase was replaced by glutamic acid by oligonucleotide-directed mutagenesis. The mutant enzyme was purified to homogeneity as judged by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Gel permeation chromatography showed that the purified mutant enzyme was a tetramer as is the wild-type enzyme. In contrast to the wild-type enzyme, which possesses 1 mol of tightly bound NAD+ per mol of enzyme subunit, the mutant enzyme had only 0.05 mol of NAD+ but contained about 0.6 mol each of NADH and adenine per mol of subunit. The mutant enzyme, after removal of the bound compounds by acid-ammonium sulfate treatment, exhibited S-adenosylhomocysteinase activity when assayed in the presence of NAD+. From the appearance of activity as a function of NAD+ concentration, the enzyme was shown to bind NAD+ with a Kd of 23.0 microM at 25 degrees C, a value greater than 280-fold greater than that of the wild-type enzyme. In the presence of a saturating concentration of NAD+, the mutant enzyme showed apparent Km values for substrates similar to those of the wild-type enzyme. Moderate decreases of 8- and 15-fold were observed in Vmax values for the synthetic and hydrolytic directions, respectively. These results indicate the importance of Asp-244 in binding NAD+, and are consistent with the idea that the region of S-adenosylhomocysteinase from residues 213 to 244 is part of the NAD+ binding site. This region has structural features characteristic of the dinucleotide-binding domains of NAD(+)- and FAD-binding proteins (Ogawa, H., Gomi, T., Mueckler, M. M., Fujioka, M., Backlund, P.S., Jr., Aksamit, R.R., Unson, C.G., and Cantoni, G.L. (1987) Proc. Natl. Acad. Sci. U.S.A. 84, 719-723).

Published
1990

45. An autopsy case of cardiac sarcoidosis with refractory ventricular tachycardia

Author

T, Takahashi, S, Fukuta, T, Date, T, Hamamoto, T, Yoshinaga, S, Kohtoku, S, Ono, M, Matsuzaki, and R, Kusukawa

Subjects
Adult, Male, Sarcoidosis, Tachycardia, Humans, Cardiomyopathies, Ultrasonography
Abstract

A case of cardiac sarcoidosis with refractory ventricular tachycardia is presented. This case was followed up for 6 years and was autopsied. The cephalad portion of the interventricular septum and the right ventricular outflow tract were markedly thinned, and sarcoid granulomas were also found in the lung.

Published
1990

46. Single crystal x-ray study of pressure-induced metal-insulator transition in (DMeDCNQI)2Cu

Author

O Arimoto, Kazumasa Oshima, T. Date, and Yoshio Nogami

Subjects
Condensed matter physics, Chemistry, Mechanical Engineering, Superlattice, Metals and Alloys, X-ray, Condensed Matter Physics, Electronic, Optical and Magnetic Materials, Metal, Mechanics of Materials, Phase (matter), visual_art, Atom, Materials Chemistry, visual_art.visual_art_medium, Metal–insulator transition, Deformation (engineering), Single crystal
Abstract

The structures of the metallic and the insulating phases of (DMeDCNQI) 2 Cu were solved under pressures of up to 15.8 kbar at room temperature. An angle α representing the deformation of CuN 4 tetrahedron around the Cu atom increases almost linearly with pressure at the rate of about 0.6 deg./ kbar. Furthermore, an X-ray diffuse scattering study revealed the presence of a 3 c CDW superlattice structure above 12 kbar in the high pressure insulating phase.

Published
1997
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47. Enantioselective catalytic Diels–Alder reaction of ethyl 2-benzoylacrylate with chiral bis(oxazoline)– or mono(oxazoline)–magnesium complex

Author

Hajime Hiramatsu, Masashige Yamauchi, Yuko Honda, and T. Date

Subjects
Magnesium, Ligand, fungi, Metals and Alloys, Enantioselective synthesis, chemistry.chemical_element, General Chemistry, Oxazoline, Medicinal chemistry, Catalysis, Surfaces, Coatings and Films, Electronic, Optical and Magnetic Materials, chemistry.chemical_compound, chemistry, Materials Chemistry, Ceramics and Composites, Organic chemistry, Diels–Alder reaction
Abstract

The magnesium catalysed Diels–Alder reaction of 2-benzoylacrylate gave the endo-adduct enantioselectively with bis(oxazoline) 5 as a C 2 -symmetric ligand or mono(oxazoline) 4 as a non-C 2 -symmetric ligand.

Published
1997
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