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Article ; Online: Discovery of moganite in a lunar meteorite as a trace of H

Kayama, Masahiro / Tomioka, Naotaka / Ohtani, Eiji / Seto, Yusuke / Nagaoka, Hiroshi / Götze, Jens / Miyake, Akira / Ozawa, Shin / Sekine, Toshimori / Miyahara, Masaaki / Tomeoka, Kazushige / Matsumoto, Megumi / Shoda, Naoki / Hirao, Naohisa / Kobayashi, Takamichi

Science advances

2018 Volume 4, Issue 5, Page(s) eaar4378

Abstract: Moganite, a monoclinic ... ...

Abstract	Moganite, a monoclinic SiO
Language	English
Publishing date	2018-05-02
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2810933-8
ISSN	2375-2548 ; 2375-2548
ISSN (online)	2375-2548
ISSN	2375-2548
DOI	10.1126/sciadv.aar4378
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Article: Photoredox ketone catalysis for the direct C-H imidation and acyloxylation of arenes.

Tripathi, Chandra Bhushan / Ohtani, Tsuyoshi / Corbett, Michael T / Ooi, Takashi

Chemical science

2017 Volume 8, Issue 8, Page(s) 5622–5627

Abstract: The photoexcited aryl ketone-catalyzed C-H imidation of arenes and heteroarenes is reported. Using ...

Abstract	The photoexcited aryl ketone-catalyzed C-H imidation of arenes and heteroarenes is reported. Using 3,6-dimethoxy-9
Language	English
Publishing date	2017-06-05
Publishing country	England
Document type	Journal Article
ZDB-ID	2559110-1
ISSN	2041-6539 ; 2041-6520
ISSN (online)	2041-6539
ISSN	2041-6520
DOI	10.1039/c7sc01700f
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Article: Molecular diversities of RNases H.

Ohtani, N / Haruki, M / Morikawa, M / Kanaya, S

Journal of bioscience and bioengineering

2005 Volume 88, Issue 1, Page(s) 12–19

Abstract: RNase H is an enzyme that specifically cleaves RNA hybridized to DNA. The enzyme is ubiquitously ... present in various organisms. Single bacterial and eucaryotic cells often contain two RNases H ... ancestor, we carried out phylogenetic analyses of the RNase H sequences. In this report, we demonstrated ...

Abstract	RNase H is an enzyme that specifically cleaves RNA hybridized to DNA. The enzyme is ubiquitously present in various organisms. Single bacterial and eucaryotic cells often contain two RNases H, whereas single archaeal cells contain only one. To determine whether there is a physiological significance in the ubiquity and multiplicity of the enzyme, and whether all enzymes are evolutionarily diverged from a common ancestor, we carried out phylogenetic analyses of the RNase H sequences. In this report, we demonstrated that RNases H are classified into two major families, Type 1 and Type 2 RNases H, of which only the Type 2 enzymes are present in all living organisms, including bacteria, archaea, and eucaryotes, suggesting that they represent an ancestral form of RNases H. Based on this information, we discuss the evolutionary relationships and possible cellular functions of RNases H.
Language	English
Publishing date	2005-10-03
Publishing country	Japan
Document type	Journal Article
ZDB-ID	1465387-4
ISSN	1347-4421 ; 1389-1723
ISSN (online)	1347-4421
ISSN	1389-1723
DOI	10.1016/s1389-1723(99)80168-6
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Article ; Online: Early depth assessment of local burns by videomicroscopy: 24 h after injury is a critical time point.

Mihara, Kyomi / Shindo, Hajime / Ohtani, Minako / Nagasaki, Kotaro / Nakashima, Reiko / Katoh, Norito / Kishimoto, Saburo

Burns : journal of the International Society for Burn Injuries

2011 Volume 37, Issue 6, Page(s) 986–993

Abstract: ... <24 h group compared with post-injury ≥24 h group (p=0.004).: Conclusion: Videomicroscopy is ... by videomicroscopy is 24 h after injury. ...

Abstract	Purpose: Videomicroscopy has simple and prompt operability, and useful in the burn depth assessment in its early phase. A burn wound is, however, a dynamic environment in the first few days and the critical time to assess a burn wound by videomicroscopy has not been investigated. The aim of this study is to investigate the critical time point to assess the burn depth by videomicroscopy. Methods: Forty one patients with 44 intermediate depth burns admitted within 7 days after injury were included. Accuracies were assessed by comparison with clinical outcome: healing within 21 days after injury or not with conservative treatment. We prospectively evaluated and compared the accuracy of the videomicroscopy measurements with the clinical assessments. All findings were serialized in order of time after injury and divided into three groups, and we compared the appreciation of burn depth by videomicroscopy findings among groups. Results: The videomicroscopy measurements is significantly accurate compared with clinical assessments (p=0.001). The accuracy of videomicroscopy measurements was significantly lower in the post-injury <24 h group compared with post-injury ≥24 h group (p=0.004). Conclusion: Videomicroscopy is effective tool in assessment of early burn depth and the critical time point to assess the burn depth by videomicroscopy is 24 h after injury.
MeSH term(s)	Adolescent ; Adult ; Aged ; Aged, 80 and over ; Burns/pathology ; Female ; Humans ; Japan ; Male ; Microscopy, Video/instrumentation ; Microscopy, Video/methods ; Middle Aged ; Prospective Studies ; Sensitivity and Specificity ; Time Factors ; Young Adult
Language	English
Publishing date	2011-09
Publishing country	Netherlands
Document type	Comparative Study ; Evaluation Studies ; Journal Article
ZDB-ID	197308-3
ISSN	1879-1409 ; 0305-4179
ISSN (online)	1879-1409
ISSN	0305-4179
DOI	10.1016/j.burns.2011.03.007
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Article: [Analysis of the pathophysiology of H. pylori infection].

Azuma, T / Ito, S / Ito, Y / Suto, H / Ohtani, M / Kuriyama, M / Keida, Y

Rinsho byori. The Japanese journal of clinical pathology

1999 Volume 47, Issue 8, Page(s) 719–723

Abstract: Vacuolating cytotoxin is an important virulence factor in H. pylori infection. Cytotoxin-producing ... H. pylori were more prevalent in patients with severe atrophic gastritis and cytotoxin activities ... in H. pylori isolates from patients with severe atrophic gastritis were much higher ...

Abstract	Vacuolating cytotoxin is an important virulence factor in H. pylori infection. Cytotoxin-producing H. pylori were more prevalent in patients with severe atrophic gastritis and cytotoxin activities in H. pylori isolates from patients with severe atrophic gastritis were much higher than those from patients with mild atrophic gastritis. It has also been suggested that there are host-related immunogenetic factors for susceptibility or resistance to diseases caused by H. pylori. The allele frequency of HLA-DQA10102 was significantly lower in the H. pylori(+) atrophic gastritis and H. pylori(+) intestinal type gastric adenocarcinoma than in the H. pylori(-) normal control and H. pylori(+) superficial gastritis. The HLA-DQA10102 allele may contribute to resistance against H. pylori-associated gastric atrophy and its association with intestinal type gastric adenocarcinoma.
MeSH term(s)	Bacterial Proteins/analysis ; Cytotoxins/analysis ; Disease Susceptibility ; Gastritis/etiology ; HLA-DQ Antigens/analysis ; HLA-DQ alpha-Chains ; Helicobacter Infections/etiology ; Helicobacter Infections/immunology ; Helicobacter pylori/chemistry ; Humans
Chemical Substances	Bacterial Proteins ; Cytotoxins ; HLA-DQ Antigens ; HLA-DQ alpha-Chains ; HLA-DQA1 antigen ; VacA protein, Helicobacter pylori
Language	Japanese
Publishing date	1999-08
Publishing country	Japan
Document type	English Abstract ; Journal Article ; Review
ZDB-ID	604196-6
ISSN	0047-1860 ; 0485-1404
ISSN	0047-1860 ; 0485-1404
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Article ; Online: Innate production of T(H)2 cytokines by adipose tissue-associated c-Kit(+)Sca-1(+) lymphoid cells.

Moro, Kazuyo / Yamada, Taketo / Tanabe, Masanobu / Takeuchi, Tsutomu / Ikawa, Tomokatsu / Kawamoto, Hiroshi / Furusawa, Jun-Ichi / Ohtani, Masashi / Fujii, Hideki / Koyasu, Shigeo

Nature

2009 Volume 463, Issue 7280, Page(s) 540–544

Abstract: ... proliferate in response to IL2 and produce large amounts of T(H)2 cytokines such as IL5, IL6 and IL13. IL5 and ... hyperplasia was not induced. Thus, FALC Lin(-)c-Kit(+)Sca-1(+) cells are T(H)2-type innate lymphocytes, and ...

Abstract	Innate immune responses are important in combating various microbes during the early phases of infection. Natural killer (NK) cells are innate lymphocytes that, unlike T and B lymphocytes, do not express antigen receptors but rapidly exhibit cytotoxic activities against virus-infected cells and produce various cytokines. Here we report a new type of innate lymphocyte present in a novel lymphoid structure associated with adipose tissues in the peritoneal cavity. These cells do not express lineage (Lin) markers but do express c-Kit, Sca-1 (also known as Ly6a), IL7R and IL33R. Similar lymphoid clusters were found in both human and mouse mesentery and we term this tissue 'FALC' (fat-associated lymphoid cluster). FALC Lin(-)c-Kit(+)Sca-1(+) cells are distinct from lymphoid progenitors and lymphoid tissue inducer cells. These cells proliferate in response to IL2 and produce large amounts of T(H)2 cytokines such as IL5, IL6 and IL13. IL5 and IL6 regulate B-cell antibody production and self-renewal of B1 cells. Indeed, FALC Lin(-)c-Kit(+)Sca-1(+) cells support the self-renewal of B1 cells and enhance IgA production. IL5 and IL13 mediate allergic inflammation and protection against helminth infection. After helminth infection and in response to IL33, FALC Lin(-)c-Kit(+)Sca-1(+) cells produce large amounts of IL13, which leads to goblet cell hyperplasia-a critical step for helminth expulsion. In mice devoid of FALC Lin(-)c-Kit(+)Sca-1(+) cells, such goblet cell hyperplasia was not induced. Thus, FALC Lin(-)c-Kit(+)Sca-1(+) cells are T(H)2-type innate lymphocytes, and we propose that these cells be called 'natural helper cells'.
MeSH term(s)	Adipose Tissue/cytology ; Adipose Tissue/immunology ; Animals ; Antigens, Ly/genetics ; Antigens, Ly/immunology ; Antigens, Ly/metabolism ; B-Lymphocytes/cytology ; B-Lymphocytes/immunology ; Cell Proliferation ; Cytokines/immunology ; Gene Expression Regulation ; Humans ; Lymphocytes/immunology ; Membrane Proteins/genetics ; Membrane Proteins/immunology ; Mesentery/immunology ; Mice ; Mice, Inbred C57BL ; Nematoda/physiology ; Nematode Infections/immunology ; Proto-Oncogene Proteins c-kit/genetics ; Proto-Oncogene Proteins c-kit/immunology ; Th2 Cells/immunology
Chemical Substances	Antigens, Ly ; Cytokines ; Ly6a protein, mouse ; Membrane Proteins ; Proto-Oncogene Proteins c-kit (EC 2.7.10.1)
Language	English
Publishing date	2009-12-20
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	120714-3
ISSN	1476-4687 ; 0028-0836
ISSN (online)	1476-4687
ISSN	0028-0836
DOI	10.1038/nature08636
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Article ; Online: Earth's Mantle Melting in the Presence of C-O-H-Bearing Fluid

Litasov, Konstantin D. / Shatskiy, Anton / Ohtani, Eiji

2013

Abstract: ... and eclogite systems with a C–O–H fluid at pressures up to about 30 GPa with special attention ... with H2O, CO2 and reduced C–O–H fluid (CH4–H2O–H2). Melting in the H2O‐bearing systems is controlled ...

Abstract	This chapter reviews recent experimental data on phase transformations and melting in peridotite and eclogite systems with a C–O–H fluid at pressures up to about 30 GPa with special attention to the effect of redox conditions. It outlines the fundamental differences for partial melting in systems with H2O, CO2 and reduced C–O–H fluid (CH4–H2O–H2). Melting in the H2O‐bearing systems is controlled by hydrogen solubility in nominally anhydrous silicates and occurs when silicates are supersaturated with H2O at definite P, T, X, and fO2. Melting in CO2‐bearing systems is determined by alkali carbonate stability and controlled mainly by Na2O, K2O, and H2O. The chapter also argues that subducted carbonates should play a major role in the “big mantle wedge” model for stagnant or deeply‐sinking slabs and proposes a new mechanism for generating slab‐derived carbonate bearing diapirs in the transition zone.
Language	English
Publisher	Wiley
Publishing country	de
Document type	Article ; Online
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Article: Identification of RNase HII from psychrotrophic bacterium, Shewanella sp. SIB1 as a high-activity type RNase H.

Chon, Hyongi / Tadokoro, Takashi / Ohtani, Naoto / Koga, Yuichi / Takano, Kazufumi / Kanaya, Shigenori

The FEBS journal

2006 Volume 273, Issue 10, Page(s) 2264–2275

Abstract: ... much more active than SIB1 RNase HI, RNases HI and HII represent low- and high-activity type RNases H ... respectively, in SIB1. In contrast, RNases HI and HII represent high- and low-activity type RNases H ... respectively, in E. coli. We propose that bacterial cells usually contain low- and high-activity type RNases H ...

Abstract	The gene encoding RNase HII from the psychrotrophic bacterium, Shewanella sp. SIB1 was cloned, overexpressed in Escherichia coli, and the recombinant protein was purified and biochemically characterized. SIB1 RNase HII is a monomeric protein with 212 amino acid residues and shows an amino acid sequence identity of 64% to E. coli RNase HII. The enzymatic properties of SIB1 RNase HII, such as metal ion preference, pH optimum, and cleavage mode of substrate, were similar to those of E. coli RNase HII. SIB1 RNase HII was less stable than E. coli RNase HII, but the difference was marginal. The half-lives of SIB1 and E. coli RNases HII at 30 degrees C were approximately 30 and 45 min, respectively. The midpoint of the urea denaturation curve and optimum temperature of SIB1 RNase HII were lower than those of E. coli RNase HII by approximately 0.2 M and approximately 5 degrees C, respectively. However, SIB1 RNase HII was much more active than E. coli RNase HII at all temperatures studied. The specific activity of SIB1 RNase HII at 30 degrees C was 20 times that of E. coli RNase HII. Because SIB1 RNase HII was also much more active than SIB1 RNase HI, RNases HI and HII represent low- and high-activity type RNases H, respectively, in SIB1. In contrast, RNases HI and HII represent high- and low-activity type RNases H, respectively, in E. coli. We propose that bacterial cells usually contain low- and high-activity type RNases H, but these types are not correlated with RNase H families.
MeSH term(s)	Amino Acid Sequence ; Cloning, Molecular ; Enzyme Activation ; Escherichia coli/genetics ; Molecular Sequence Data ; Ribonuclease H/chemistry ; Ribonuclease H/genetics ; Ribonuclease H/metabolism ; Sequence Alignment ; Shewanella/classification ; Shewanella/enzymology ; Species Specificity ; Substrate Specificity ; Up-Regulation
Chemical Substances	ribonuclease HII (EC 3.1.26.-) ; Ribonuclease H (EC 3.1.26.4)
Language	English
Publishing date	2006-05
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2173655-8
ISSN	1742-4658 ; 1742-464X
ISSN (online)	1742-4658
ISSN	1742-464X
DOI	10.1111/j.1742-4658.2006.05241.x
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Conference proceedings ; Online: X-ray Photoemission Spectroscopy of Nitrogen-Doped UNCD /a-C:H Films Prepared by Pulse Laser Deposition

Al-Riyami, S. / Yoshitake, T. / Ohmagari, S. / Ohtani, R. / Setoyama, H. / Kobayashi, E. / Nagayama, K.

Proceedings

2009

Publishing country	de
Document type	Conference proceedings ; Online
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Article ; Online: Identification of the first archaeal Type 1 RNase H gene from Halobacterium sp. NRC-1: archaeal RNase HI can cleave an RNA-DNA junction.

Ohtani, Naoto / Yanagawa, Hiroshi / Tomita, Masaru / Itaya, Mitsuhiro

The Biochemical journal

2004 Volume 381, Issue Pt 3, Page(s) 795–802

Abstract: All the archaeal genomes sequenced to date contain a single Type 2 RNase H gene. We found ... to Type 1 RNase H. The protein encoded by the Vng0255c gene, possessed amino acid sequence identities ... a complete loss of RNase H activity on the B. subtilis RNase HI homologue protein, the Vng0255c product was ...

Abstract	All the archaeal genomes sequenced to date contain a single Type 2 RNase H gene. We found that the genome of a halophilic archaeon, Halobacterium sp. NRC-1, contains an open reading frame with similarity to Type 1 RNase H. The protein encoded by the Vng0255c gene, possessed amino acid sequence identities of 33% with Escherichia coli RNase HI and 34% with a Bacillus subtilis RNase HI homologue. The B. subtilis RNase HI homologue, however, lacks amino acid sequences corresponding to a basic protrusion region of the E. coli RNase HI, and the Vng0255c has the similar deletion. As this deletion apparently conferred a complete loss of RNase H activity on the B. subtilis RNase HI homologue protein, the Vng0255c product was expected to exhibit no RNase H activity. However, the purified recombinant Vng0255c protein specifically cleaved an RNA strand of the RNA/DNA hybrid in vitro, and when the Vng0255c gene was expressed in an E. coli strain MIC2067 it could suppress the temperature-sensitive growth defect associated with the loss of RNase H enzymes of this strain. These results in vitro and in vivo strongly indicate that the Halobacterium Vng0255c is the first archaeal Type 1 RNase H. This enzyme, unlike other Type 1 RNases H, was able to cleave an Okazaki fragment-like substrate at the junction between the 3'-side of ribonucleotide and 5'-side of deoxyribonucleotide. It is likely that the archaeal Type 1 RNase H plays a role in the removal of the last ribonucleotide of the RNA primer from the Okazaki fragment during DNA replication.
MeSH term(s)	Amino Acid Sequence/genetics ; Bacillus subtilis/enzymology ; Bacterial Proteins/metabolism ; Cations, Divalent/chemistry ; Cloning, Molecular/methods ; DNA/chemistry ; Escherichia coli/enzymology ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Evolution, Molecular ; Genetic Complementation Test/methods ; Genome, Archaeal ; Halobacterium/enzymology ; Halobacterium/genetics ; Molecular Sequence Data ; Nucleic Acid Heteroduplexes/chemistry ; RNA/chemistry ; RNA/metabolism ; Ribonuclease H/biosynthesis ; Ribonuclease H/chemistry ; Ribonuclease H/genetics ; Ribonuclease H/metabolism ; Sequence Homology, Amino Acid ; Substrate Specificity/genetics
Chemical Substances	Bacterial Proteins ; Cations, Divalent ; Nucleic Acid Heteroduplexes ; RNA (63231-63-0) ; DNA (9007-49-2) ; Ribonuclease H (EC 3.1.26.4)
Language	English
Publishing date	2004-08-01
Publishing country	England
Document type	Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2969-5
ISSN	1470-8728 ; 0006-2936 ; 0306-3275 ; 0264-6021
ISSN (online)	1470-8728
ISSN	0006-2936 ; 0306-3275 ; 0264-6021
DOI	10.1042/BJ20040153
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