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359 results on '"Ogata, Hideaki"'

112. Comparison between a new assay system, Elecsys® Anti-p53, and conventional MESACUP™ for the detection of serum anti-p53 antibodies: A multi-institutional study.

Author

Suzuki, Takashi, Oshima, Yoko, Shiratori, Fumiaki, Nanami, Tatsuki, Yajima, Satoshi, Sumazaki, Makoto, Ushigome, Mitsunori, Sugita, Hironobu, Eberl, Magdalena, Ogata, Hideaki, Hayashida, Tetsu, Nakamura, Seigo, Nakagawa, Tsuyoshi, and Shimada, Hideaki

Subjects
ENZYME-linked immunosorbent assay, ESOPHAGUS diseases, IMMUNOGLOBULINS, COLORECTAL cancer, BREAST cancer
Abstract

The sensitivity and specificity of a new automated electrochemiluminescence immunoassay system, Elecsys® Anti-p53 (Elecsys), were compared with that of the conventional serum anti-p53 antibody (s-p53-Ab) enzyme-linked immunosorbent assay kit [MESACUP anti-p53 test (MESACUP)]. Elecsys and MESACUP were used to analyze the levels of s-p53-Abs in patients with esophageal, colorectal and breast cancer. A total of 532 controls and 288, 235 and 329 patients with esophageal, colorectal and breast cancer, respectively, were enrolled. Additionally, the sera of patients with benign diseases of the esophagus, colorectal system and breast, patients with autoimmune diseases and healthy volunteers were analyzed as controls. Sensitivity and specificity were compared between the two assay systems. Positive agreement rates were 58.7% in all samples, 71.2% in esophageal samples, 73.6% in colorectal samples and 35.1% in breast samples. Negative agreement rates for the different cancer types were ≥97.1% and the overall agreement rates were ≥92.3%. When the specificities of the two assays were aligned for all samples, Elecsys demonstrated higher sensitivities for all types of analyzed cancer together, as well as for esophageal, colorectal and breast cancer, respectively. Although positive concordance between the two assay systems was low in terms of specificity, Elecsys had a higher sensitivity than the MESACUP. [ABSTRACT FROM AUTHOR]

Published
2022
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116. Crystallization and preliminary X-ray crystallographic studies of the axin DIX domain

Author

Shibata, Naoki, primary, Tomimoto, Yusuke, additional, Hanamura, Toru, additional, Yamamoto, Ryo, additional, Ueda, Mai, additional, Ueda, Yasufumi, additional, Mizuno, Nobuhiro, additional, Ogata, Hideaki, additional, Komori, Hirofumi, additional, Shomura, Yasuhito, additional, Kataoka, Michihiko, additional, Shimizu, Sakayu, additional, Kondo, Jun, additional, Yamamoto, Hideki, additional, Kikuchi, Akira, additional, and Higuchi, Yoshiki, additional

Published
2007
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118. Promyelocytic Crisis of Chronic Myelogenous Leukaemia during Imatinib Mesylate Treatment

Author

Oku, Eijiro, primary, Imamura, Rie, additional, Nagata, Shuichiro, additional, Takata, Yuka, additional, Seki, Ritsuko, additional, Otsubo, Korenori, additional, Hashiguchi, Michitoshi, additional, Osaki, Koichi, additional, Yakushiji, Kazuaki, additional, Yoshimoto, Kohji, additional, Ogata, Hideaki, additional, Sata, Michio, additional, and Okamura, Takashi, additional

Published
2006
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120. Simultaneous Hepatic Relapse of Non-Hodgkin’s Lymphoma and Hepatocellular Carcinoma in a Patient with Hepatitis C Virus-Related Cirrhosis

Author

Ohtsubo, Korenori, primary, Oku, Eijiro, additional, Imamura, Rie, additional, Seki, Ritsuko, additional, Hashiguchi, Michitoshi, additional, Osaki, Koichi, additional, Yakushiji, Kazuaki, additional, Yoshimoto, Kohji, additional, Ogata, Hideaki, additional, Nagamatsu, Hiroaki, additional, Ando, Eiji, additional, Shimamatsu, Kazuhide, additional, Okamura, Takashi, additional, and Sata, Michio, additional

Published
2006
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131. Structural Studies of the Carbon Monoxide Complex of [NiFe]hydrogenase fromDesulfovibriovulgarisMiyazaki F: Suggestion for the Initial Activation Site for Dihydrogen

Author

Ogata, Hideaki, primary, Mizoguchi, Yasutaka, additional, Mizuno, Nobuhiro, additional, Miki, Kunio, additional, Adachi, Shin-ichi, additional, Yasuoka, Noritake, additional, Yagi, Tatsuhiko, additional, Yamauchi, Osamu, additional, Hirota, Shun, additional, and Higuchi, Yoshiki, additional

Published
2002
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133. Importance of Hydrogen Bonding in Fine Tuning the [2Fe-2S] Cluster Redox Potential of HydC from Thermotoga maritima

Author

Birrell, James A., Laurich, Christoph, Reijerse, Edward J., Ogata, Hideaki, and Lubitz, Wolfgang

Abstract

Iron–sulfur clusters form one of the largest and most diverse classes of enzyme cofactors in nature. They may serve as structural factors, form electron transfer chains between active sites and external redox partners, or form components of enzyme active sites. Their specific role is a consequence of the cluster type and the surrounding protein environment. The relative effects of these factors are not completely understood, and it is not yet possible to predict the properties of iron–sulfur clusters based on amino acid sequences or rationally tune their properties to generate proteins with new desirable functions. Here, we generate mutations in a [2Fe-2S] cluster protein, the TmHydC subunit of the trimeric [FeFe]-hydrogenase from Thermotoga maritima, to study the factors that affect its redox potential. Saturation mutagenesis of Val131 was used to tune the redox potential over a 135 mV range and revealed that cluster redox potential and electronic properties correlate with amino acid hydrophobicity and the ability to form hydrogen bonds to the cluster. Proline scanning mutagenesis between pairs of ligating cysteines was used to remove backbone amide hydrogen bonds to the cluster and decrease the redox potential by up to 132 mV, without large structural changes in most cases. However, substitution of Gly83 with proline caused a change of HydC to a [4Fe-4S] cluster protein with a redox potential of −526 mV. Together, these results confirm the importance of hydrogen bonding in tuning cluster redox potentials and demonstrate the versatility of iron–sulfur cluster protein folds at binding different types of clusters.

Published
2016
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137. Inflammatory Pseudotumor of the Liver. MR imaging Findings.

Author

IJUIN, HIROYASU, primary, ONO, NAOFUMI, additional, KOGA, KENSI, additional, YOSHIDA, TOMOYUKI, additional, OHNISHI, HIROYUKI, additional, MIYAZAKI, SHIROH, additional, OGATA, HIDEAKI, additional, KOHAKURA, MAKOTO, additional, OGAWA, KOHEI, additional, YAMAWAKI, MAKOTO, additional, KUSABA, TAKU, additional, and TANIKAWA, KYUICHI, additional

Published
1997
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140. Observation of the FeCN and FeCO Vibrations in the Active Site of [NiFe] Hydrogenase by Nuclear Resonance Vibrational Spectroscopy.

Author

Kamali, Saeed, Wang, Hongxin, Mitra, Devrani, Ogata, Hideaki, Lubitz, Wolfgang, Manor, Brian C., Rauchfuss, Thomas B., Byrne, Deborah, Bonnefoy, Violaine, Jenney, Francis E., Adams, Michael W. W., Yoda, Yoshitaka, Alp, Ercan, Zhao, Jiyong, and Cramer, Stephen P.

Abstract

Nuclear inelastic scattering of 57Fe labeled [NiFe] hydrogenase is shown to give information on different states of the enzyme. It was thus possible to detect and assign FeCO and FeCN bending and stretching vibrations of the active site outside the spectral range of the FeS cluster normal modes. [ABSTRACT FROM AUTHOR]

Published
2013
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141. Detektion von Fe-CN- und Fe-CO-Schwingungen im aktiven Zentrum der [NiFe]-Hydrogenase durch inelastische kernresonante Streuung.

Author

Kamali, Saeed, Wang, Hongxin, Mitra, Devrani, Ogata, Hideaki, Lubitz, Wolfgang, Manor, Brian C., Rauchfuss, Thomas B., Byrne, Deborah, Bonnefoy, Violaine, Jenney, Francis E., Adams, Michael W. W., Yoda, Yoshitaka, Alp, Ercan, Zhao, Jiyong, and Cramer, Stephen P.

Abstract

Blick ins Zentrum: Die Methode der inelastischen kernresonanten Streuung (NRVS) wurde genutzt, um 57Fe ‐ markierte [NiFe] ‐ Hydrogenase in unterschiedlichen Zuständen des Enzyms zu untersuchen. Damit gelang es, die Fe ‐ CO ‐ und Fe ‐ CN ‐ Beuge ‐ und ‐ Streckschwingung außerhalb des Spektralbereichs der Normalmoden der Fe ‐ S ‐ Cluster zu detektieren und zuzuordnen (siehe Spektrum). [ABSTRACT FROM AUTHOR]

Published
2013
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142. A CASE OF MORGAGNI HERNIA

Author

DEGUCHI, Hisatsugu, primary, ISOGAI, Masahiro, additional, OGATA, Hideaki, additional, TSUGU, Yukio, additional, OHTAKI, Kazuhiko, additional, and ASAKURA, Takeshi, additional

Published
1993
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143. Probing intermediates in the activation cycle of [NiFe] hydrogenase by infrared spectroscopy: the Ni-SIr state and its light sensitivity.

Author

Pandelia, Maria-Eirini, Ogata, Hideaki, Currell, Leslie J., Flores, Marco, and Lubitz, Wolfgang

Subjects
*HYDROGENASE, *INFRARED spectroscopy, *DESULFOVIBRIO vulgaris, *AMINO acids, *SULFUR bacteria, *NONMETALS
Abstract

The [NiFe] hydrogenase from the sulphate-reducing bacterium Desulfovibrio vulgaris Miyazaki F is reversibly inhibited in the presence of molecular oxygen. A key intermediate in the reactivation process, Ni-SIr, provides the link between fully oxidized (Ni-A, Ni-B) and active (Ni-SIa, Ni-C and Ni-R) forms of hydrogenase. In this work Ni-SIr was found to be light-sensitive ( T ≤ 110 K), similar to the active Ni-C and the CO-inhibited states. Transition to the final photoproduct state (Ni-SL) was shown to involve an additional transient light-induced state (Ni-SI1961). Rapid scan kinetic infrared measurements provided activation energies for the transition from Ni-SL to Ni-SIr in protonated as well as in deuterated samples. The inhibitor CO was found not to react with the active site of the Ni-SL state. The wavelength dependence of the Ni-SIr photoconversion was examined in the range between 410 and 680 nm. Light-induced effects were associated with a nickel-centred electronic transition, possibly involving a change in the spin state of nickel (Ni2+). In addition, at T ≤ 40 K the CN− stretching vibrations of Ni-SL were found to be dependent on the colour of the monochromatic light used to irradiate the species, suggesting a change in the interaction of the hydrogen-bonding network of the surrounding amino acids. A possible mechanism for the photochemical process, involving displacement of the oxygen-based ligand, is discussed. [ABSTRACT FROM AUTHOR]

Published
2009
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144. Promyelocytic Crisis of Chronic Myelogenous Leukaemia during Imatinib Mesylate Treatment.

Author

Oku, Eijiro, Imamura, Rie, Nagata, Shuichiro, Takata, Yuka, Seki, Ritsuko, Otsubo, Korenori, Hashiguchi, Michitoshi, Osaki, Koichi, Yakushiji, Kazuaki, Yoshimoto, Kohji, Ogata, Hideaki, Sata, Michio, and Okamura, Takashi

Subjects
CHRONIC myeloid leukemia, PROTEIN-tyrosine kinases, LEUKEMIA, DRUGS, THERAPEUTICS
Abstract

An untreated 66-year-old woman with chronic myelogenous leukaemia (CML) in the chronic phase was initially given imatinib mesylate, rapidly achieving a good cytogenetic response with treatment. However, acute promyelocytic leukaemia complicated by a disseminated intravascular coagulation occurred 9 months after beginning imatinib treatment. Promyelocytic crisis of CML was diagnosed by demonstration of both BCR/ABL and PML/RARα chimeric genes in leukaemic cells by karyotypic and fluorescence in situ hybridization analysis. Clonal evolution with addition of the PML/RARα translocation may have arisen in the early chronic phase of CML, with expansion of this clone during imatinib treatment. Promyelocytic crisis of CML is rare; furthermore, we know of no previous report of promyelocytic crisis occurring during treatment with imatinib. Copyright © 2007 S. Karger AG, Basel [ABSTRACT FROM AUTHOR]

Published
2007
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146. Structural Studies of the Carbon Monoxide Complex of [NiFe]hydrogenase from Desulfovibrio vulgaris Miyazaki F: Suggestion for the Initial Activation Site for Dihydrogen.

Author

Ogata, Hideaki, Mizoguchi, Yasutaka, Mizuno, Nobuhiro, Miki, Kunio, Adachi, Shin-ichi, Yasuoka, Noritake, Yagi, Tatsuoko, Yamauchi, Osamu, Hirota, Shun, and Higuchi, Yoshiki

Subjects
*CARBON monoxide, *HYDROGENASE
Abstract

Characterizes the carbon monoxide complex of [NiFe]hydrogenase from Desulfovibrio vulgaris Miyazaki F. Use of X-ray crystallography and absorption and resonance Raman spectroscopy; Determination of the nine crystals of hydrogenase; Observation of distinct changes in electron density distribution.

Published
2002
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147. Annexin V inhibits the 12-O-tetradecanoylphorbol-13-acetate-induced activation of Ras/extracellular signal-regulated kinase (ERK) signaling pathway upstream of Shc in MCF-7 cells.

Author

Sato, Hirokazu, Ogata, Hideaki, and De Luca, Luigi M

Subjects
ANNEXINS, PHOSPHOLIPIDS
Abstract

Annexin V is a Ca2+-dependent phospholipid binding protein. Although it has been shown to inhibit protein kinase C (PKC) in cell-free systems, its role in the intact cell is unclear. A stable MCF-7 human breast cancer cell overexpression system was established to investigate the function of annexin V. In these cells, 12-O-tetradecanoylphorbol-13-acetate (TPA)-induced phosphorylation and kinase activity of ERK1/2 were suppressed. Morphological changes induced by TPA were reduced by annexin V overexpression as well as by the pan-PKC inhibitor, bisindolylmaleimide I, and by the mitogen-activated protein kinase/extracellular signal-regulated kinase kinase (MEK) inhibitor, PD98059. TPA-induced MEK1/2 and Raf-1 phosphorylation were reduced in these cells. The TPA-enhanced active Ras, and its association with Raf-1, were reduced. TPA treatment of MCF-7 cells caused an increased association of Shc with Grb2. However, this increased association was prevented in the annexin V-overexpressors. p21WAF/CIP1 is responsible for inhibition of cell cycle progression in MCF-7 cells. TPA induced the expression of p21WAF/CIP1 to a greater extent in MCF-7 parent and control plasmid cells than in annexin V overexpressors. PD98059 inhibited this increase, suggesting that TPA upregulation of p21WAF/CIP1 occurs via the MEK pathway, and that annexin V overexpression blunts it. This work shows that annexin V overexpression suppresses the TPA-induced Ras/ERK signaling by inhibiting at/or upstream of Shc, possibly through the inhibition of PKCs. Oncogene (2000) 19, 2904–2912 [ABSTRACT FROM AUTHOR]

Published
2000
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148. Role of the Aromatic Ring of Tyr43 in Tetraheme Cytochrome c3 from Desulfovibrio vulgaris Miyazaki F

Author

Ozawa, Kiyoshi, Takayama, Yuki, Yasukawa, Fumiko, Ohmura, Tomoaki, Cusanovich, Michael A., Tomimoto, Yusuke, Ogata, Hideaki, Higuchi, Yoshiki, and Akutsu, Hideo

Abstract

Tyrosine 43 is positioned parallel to the fifth heme axial ligand, His34, of heme 1 in the tetraheme cytochrome c3. The replacement of tyrosine with leucine increased the redox potential of heme 1 by 44 and 35mV at the first and last reduction steps, respectively; its effects on the other hemes are small. In contrast, the Y43F mutation hardly changed the potentials. It shows that the aromatic ring at this position contributes to lowering the redox potential of heme 1 locally, although this cannot be the major contribution to the extremely low redox potentials of cytochrome c3. Furthermore, temperature-dependent line-width broadening in partially reduced samples established that the aromatic ring at position 43 participates in the control of the kinetics of intramolecular electron transfer. The rate of reduction of Y43L cytochrome c3 by 5-deazariboflavin semiquinone under partially reduced conditions was significantly different from that of the wild type in the last stage of the reduction, supporting the involvement of Tyr43 in regulation of reduction kinetics. The mutation of Y43L, however, did not induce a significant change in the crystal structure.

Published
2003
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149. The Palladium-Catalyzed Vinylation and Carbonylation of Bromoindoles and N-Acety1-bromoindoline

Author

Kasahara, Akira, Izumi, Taeko, and Ogata, Hideaki

Subjects
inorganic chemicals
Abstract

論文(Article), s The palladium-catalyzed vinylic substitution reaction of alkenes has been shown to proceed in moderate yields with 5- and 6-bromoindols, and N-acetyl-5-bromoindoline. 4-, 5-, 6-, and 7-Bromoindoles also undergo facile palladium-assisted carbonylation with carbon monoxide in methanol to produce methoxycarbonylindoles in moderate yields.

Published
1989

150. Purification, crystallization and preliminary X-ray analysis of the dissimilatory sulfite reductase from Desulfovibrio vulgaris Miyazaki F.

Author

Ogata, Hideaki, Shomura, Yasuhito, Goenka Agrawal, Aruna, Kaur, Amrit Pal, Gärtner, Wolfgang, Higuchi, Yoshiki, and Lubitz, Wolfgang

Subjects
*DESULFOVIBRIO vulgaris, *SULFITES, *REDUCTASES, *CRYSTALLIZATION, *CRYSTAL structure research
Abstract

Dissimilatory sulfite reductase (Dsr) plays an important role in sulfate respiration in many sulfate-reducing bacteria. Dsr from Desulfovibrio vulgaris Miyazaki F has been purified and crystallized at 277 K using the sitting-drop vapour-diffusion method with PEG 3350 and potassium thiocyanate as precipitants. A data set was collected to 3.7 Å resolution from a single crystal at 100 K using synchrotron radiation. The Dsr crystal belonged to space group P41212, with unit-cell parameters a = b = 163.26, c = 435.32 Å. The crystal structure of Dsr was determined by the molecular-replacement method based on the three-dimensional structure of Dsr from D. vulgaris Hildenborough. The crystal contained three α2β2γ2 units per asymmetric unit, with a Matthews coefficient ( VM) of 2.35 Å3 Da−1; the solvent content was estimated to be 47.7%. [ABSTRACT FROM AUTHOR]

Published
2010
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