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Article: Corrigendum to: Contribution of histone N-terminal tails to the structure and stability of nucleosomes.

Iwasaki, Wakana / Miya, Yuta / Horikoshi, Naoki / Osakabe, Akihisa / Taguchi, Hiroyuki / Tachiwana, Hiroaki / Shibata, Takehiko / Kagawa, Wataru / Kurumizaka, Hitoshi

FEBS open bio

2018 Volume 8, Issue 9, Page(s) 1567

Abstract: This corrects the article DOI: 10.1016/j.fob.2013.08.007.]. ...

Abstract	[This corrects the article DOI: 10.1016/j.fob.2013.08.007.].
Language	English
Publishing date	2018-08-23
Publishing country	England
Document type	Journal Article ; Published Erratum
ISSN	2211-5463
ISSN	2211-5463
DOI	10.1002/2211-5463.12508
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Article ; Online: N-acetyl cysteine prolonged the developmental ability of mouse two-cell embryos against oxidative stress at refrigerated temperatures.

Horikoshi, Yuka / Takeo, Toru / Nakagata, Naomi

Cryobiology

2016 Volume 72, Issue 3, Page(s) 198–204

Abstract: ... the effect of oxidative and investigated the efficacy of adding N-acetyl cysteine (NAC) to the preservation ...

Abstract	Cold storage of two-cell embryos at refrigerated temperatures is a useful means to ship genetically engineered mice. We previously reported that M2 medium maintained the developmental ability of two-cell embryos for 48 h at 4 °C, and offspring were obtained from embryos transported by a courier service under refrigerated temperatures. The limitation of 48 h practically restricts the shipping destination of the embryos. To enhance the applicability of the cold-storage technique, prolonging the time to maintain developmental ability of the embryos is required. Oxidative stress may be a cause of the declining developmental ability of cold-stored embryos. However, the effect of oxidative stress on developmental ability of embryos has not been investigated. We examined intracellular glutathione (GSH) levels of cold-stored two-cell embryos to evaluate the effect of oxidative and investigated the efficacy of adding N-acetyl cysteine (NAC) to the preservation medium on the developmental ability of cold-stored embryos and transported two-cell embryos at refrigerated temperatures. Intracellular GSH levels of two-cell embryos decreased by cold storage for longer than 72 h, whereas NAC recovered this reduction and improved the developmental ability of embryos cold-stored for 96 h. In the transport experiment, the developmental rate of transported two-cell embryos to offspring was increased by adding NAC to the preservation medium. We found that NAC prolonged the storage period of two-cell embryos and maintained the developmental ability by alleviating the reduction of intracellular GSH. These findings will improve the technique of cold-storage of two-cell embryos to facilitate efficient transport of genetically engineered mice worldwide.
MeSH term(s)	Acetylcysteine/pharmacology ; Animals ; Antioxidants/pharmacology ; Cold Temperature ; Cryopreservation/methods ; Embryo, Mammalian ; Female ; Glutathione/metabolism ; Male ; Mice, Inbred C57BL ; Mice, Inbred ICR ; Oxidative Stress/drug effects
Chemical Substances	Antioxidants ; Glutathione (GAN16C9B8O) ; Acetylcysteine (WYQ7N0BPYC)
Language	English
Publishing date	2016
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	80098-3
ISSN	1090-2392 ; 0011-2240
ISSN (online)	1090-2392
ISSN	0011-2240
DOI	10.1016/j.cryobiol.2016.05.002
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Article ; Online: Facile preparation of N-doped TiO2 at ambient temperature and pressure under UV light with 4-nitrophenol as the nitrogen source and its photocatalytic activities.

Horikoshi, Satoshi / Shirasaka, Yutaro / Uchida, Hiroshi / Horikoshi, Natsuko / Serpone, Nick

Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology

2016 Volume 15, Issue 8, Page(s) 1061–1070

Abstract: ... for the first time the facile preparation of N-doped TiO2 (P25 titania) in aqueous media at ambient temperature ... nitrobenzaldehyde) as the nitrogen source. The resulting N-doped P25 TiO2 materials were characterized by UV/Vis and ... The photocatalytic activity of N-doped TiO2 was assessed through examining the photodegradation of 4-chlorophenol in aqueous ...

Abstract	To date syntheses of nitrogen-doped TiO2 photocatalysts (TiO2-xNx) have been carried out under high temperatures and high pressures with either NH3 or urea as the nitrogen sources. This article reports for the first time the facile preparation of N-doped TiO2 (P25 titania) in aqueous media at ambient temperature and pressure under inert conditions (Ar- and N2-purged dispersions) with 4-nitrophenol (or 4-nitrobenzaldehyde) as the nitrogen source. The resulting N-doped P25 TiO2 materials were characterized by UV/Vis and X-ray photoelectron spectroscopies (XPS) that confirmed the presence of nitrogen within the photocatalyst; X-ray diffraction (XRD) techniques confirmed the crystalline phases of the doped material. The photocatalytic activity of N-doped TiO2 was assessed through examining the photodegradation of 4-chlorophenol in aqueous media and iso-propanol as a volatile pollutant under UV/Vis and visible-light irradiation. Under visible light irradiation, undoped P25 was inactive contrary to N-doped P25 that successfully degraded 95% of the 4-chlorophenol (after 10 h) and 23% of iso-propanol (after 2.5 h).
Language	English
Publishing date	2016--04
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2072584-X
ISSN	1474-9092 ; 1474-905X
ISSN (online)	1474-9092
ISSN	1474-905X
DOI	10.1039/c6pp00167j
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Article: Contribution of histone N-terminal tails to the structure and stability of nucleosomes.

Iwasaki, Wakana / Miya, Yuta / Horikoshi, Naoki / Osakabe, Akihisa / Taguchi, Hiroyuki / Tachiwana, Hiroaki / Shibata, Takehiko / Kagawa, Wataru / Kurumizaka, Hitoshi

FEBS open bio

2013 Volume 3, Page(s) 363–369

Abstract: ... histones, H2A, H2B, H3, or H4, lacked the N-terminal tail. We found that the deletion of the H2B or H3 N ...

Abstract	Histones are the protein components of the nucleosome, which forms the basic architecture of eukaryotic chromatin. Histones H2A, H2B, H3, and H4 are composed of two common regions, the "histone fold" and the "histone tail". Many efforts have been focused on the mechanisms by which the post-translational modifications of histone tails regulate the higher-order chromatin architecture. On the other hand, previous biochemical studies have suggested that histone tails also affect the structure and stability of the nucleosome core particle itself. However, the precise contributions of each histone tail are unclear. In the present study, we determined the crystal structures of four mutant nucleosomes, in which one of the four histones, H2A, H2B, H3, or H4, lacked the N-terminal tail. We found that the deletion of the H2B or H3 N-terminal tail affected histone-DNA interactions and substantially decreased nucleosome stability. These findings provide important information for understanding the complex roles of histone tails in regulating chromatin structure.
Language	English
Publishing date	2013-08-22
Publishing country	England
Document type	Journal Article
ZDB-ID	2651702-4
ISSN	2211-5463
ISSN	2211-5463
DOI	10.1016/j.fob.2013.08.007
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Article ; Online: Multiple Enlarged Aneurysms in Primary Racemose Hemangioma of the Bronchial Artery: Successful Prophylactic Transcatheter Arterial Embolization Using N-butyl-2-cyanoacrylate and Coils.

Saiga, Atsushi / Sugiura, Toshihiko / Higashide, Takashi / Tsuchiya, Satoshi / Nishiyama, Akira / Kubota, Yoshihiro / Horikoshi, Takuro / Uno, Takashi

Cardiovascular and interventional radiology

2018 Volume 41, Issue 5, Page(s) 811–815

Abstract: ... balloon-occluded embolization using a mixture of N-butyl-2-cyanoacrylate (NBCA) and iodized oil. For four ...

Abstract	An asymptomatic 48-year-old man presented with multiple aneurysms in a primary racemose hemangioma of the right bronchial artery. Bronchial arteriography revealed a tortuous artery with four fusiform aneurysms of varying sizes and aneurysmal dilatation with marked thrombus formation in the long segment of the distal portion. Because the tip of catheter could not pass beyond the aneurysmal dilatation, we performed balloon-occluded embolization using a mixture of N-butyl-2-cyanoacrylate (NBCA) and iodized oil. For four other aneurysms, we performed embolization using a coil alone or with NBCA. After 6 months, right bronchial arteriography revealed no enhancement of the aneurysms. Despite the rarity of this procedure, embolization with NBCA is a good option for bronchial artery aneurysm embolization.
MeSH term(s)	Aneurysm/complications ; Aneurysm/diagnostic imaging ; Aneurysm/therapy ; Bronchial Arteries/diagnostic imaging ; Bronchial Diseases/complications ; Bronchial Diseases/diagnostic imaging ; Bronchial Diseases/therapy ; Computed Tomography Angiography/methods ; Diagnosis, Differential ; Embolization, Therapeutic/methods ; Enbucrilate/therapeutic use ; Hemangioma/complications ; Hemangioma/diagnostic imaging ; Hemangioma/therapy ; Humans ; Iodized Oil/therapeutic use ; Male ; Middle Aged
Chemical Substances	Iodized Oil (8001-40-9) ; Enbucrilate (F8CEP82QNP)
Language	English
Publishing date	2018-01-17
Publishing country	United States
Document type	Case Reports ; Journal Article
ZDB-ID	603082-8
ISSN	1432-086X ; 0342-7196 ; 0174-1551
ISSN (online)	1432-086X
ISSN	0342-7196 ; 0174-1551
DOI	10.1007/s00270-018-1878-3
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Article: N-acetyl cysteine prolonged the developmental ability of mouse two-cell embryos against oxidative stress at refrigerated temperatures

Horikoshi, Yuka / Toru Takeo / Naomi Nakagata

Cryobiology. 2016 June, v. 72, no. 3

2016

Abstract: ... the effect of oxidative and investigated the efficacy of adding N-acetyl cysteine (NAC) to the preservation ...

Abstract	Cold storage of two-cell embryos at refrigerated temperatures is a useful means to ship genetically engineered mice. We previously reported that M2 medium maintained the developmental ability of two-cell embryos for 48 h at 4 °C, and offspring were obtained from embryos transported by a courier service under refrigerated temperatures. The limitation of 48 h practically restricts the shipping destination of the embryos. To enhance the applicability of the cold-storage technique, prolonging the time to maintain developmental ability of the embryos is required. Oxidative stress may be a cause of the declining developmental ability of cold-stored embryos. However, the effect of oxidative stress on developmental ability of embryos has not been investigated. We examined intracellular glutathione (GSH) levels of cold-stored two-cell embryos to evaluate the effect of oxidative and investigated the efficacy of adding N-acetyl cysteine (NAC) to the preservation medium on the developmental ability of cold-stored embryos and transported two-cell embryos at refrigerated temperatures. Intracellular GSH levels of two-cell embryos decreased by cold storage for longer than 72 h, whereas NAC recovered this reduction and improved the developmental ability of embryos cold-stored for 96 h. In the transport experiment, the developmental rate of transported two-cell embryos to offspring was increased by adding NAC to the preservation medium. We found that NAC prolonged the storage period of two-cell embryos and maintained the developmental ability by alleviating the reduction of intracellular GSH. These findings will improve the technique of cold-storage of two-cell embryos to facilitate efficient transport of genetically engineered mice worldwide.
Keywords	cold storage ; cysteine ; genetic engineering ; glutathione ; mice ; oxidation ; oxidative stress ; progeny ; storage time ; temperature
Language	English
Dates of publication	2016-06
Size	p. 198-204.
Publishing place	Elsevier Inc.
Document type	Article
ZDB-ID	80098-3
ISSN	1090-2392 ; 0011-2240
ISSN (online)	1090-2392
ISSN	0011-2240
DOI	10.1016/j.cryobiol.2016.05.002
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Higher Activity of Ni/g-Al 2 O 3 over Fe/g-Al 2 O 3 and Ru/g-Al 2 O 3 for Catalytic Ammonia Synthesis in Nonthermal Atmospheric-Pressure Plasma of N 2 and H 2

Masakazu Iwamoto / Masataka Horikoshi / Ryu Hashimoto / Kaori Shimano / Tomiko Sawaguchi / Harunobu Teduka / Masahiko Matsukata

Catalysts, Vol 10, Iss 590, p

2020 Volume 590

Abstract: Developing a novel ammonia synthesis process from N 2 and H 2 is of interest to the catalysis and ...

Abstract	Developing a novel ammonia synthesis process from N 2 and H 2 is of interest to the catalysis and hydrogen research communities. g-Alumina-supported nickel was determined capable of serving as an efficient catalyst for ammonia synthesis using nonthermal plasma under atmospheric pressure without heating. The catalytic activity was almost unrelated to the crystal structure and the surface area of the alumina carrier. The activity of Ni/Al 2 O 3 was quantitatively compared with that of Fe/Al 2 O 3 and Ru/Al 2 O 3 , which contained active metals for the conventional Haber–Bosch process. The activity sequence was Ni/Al 2 O 3 > Al 2 O 3 > Fe/Al 2 O 3 > no additive > Ru/Al 2 O 3 , surprisingly indicating that the loading of Fe and Ru decreased the activity of Al 2 O 3 . The catalytic activity of Ni/Al 2 O 3 was dependent on the amount of loaded Ni, the calcination temperature, and the reaction time. XRD, visual, and XPS observations of the catalysts before the plasma reaction indicated the generation of NiO and NiAl 2 O 4 on Al 2 O 3 , the latter of which was generated upon high-temperature calcination. The NiO species was readily reduced to Ni metal in the plasma reaction, whereas the NiAl 2 O 4 species was difficult to reduce. The catalytic behavior could be attributed to the production of fine Ni metal particles that served as active sites. The P N2 /P H2 ratio dependence and rate constants of formation and decomposition of ammonia were finally determined for 5.0 wt % Ni/Al 2 O 3 calcined at 773 K. The ammonia yield was 6.3% at an applied voltage of 6.0 kV, a residence time of reactant gases of 0.12 min, and P H2 /P N2 = 1.
Keywords	ammonia synthesis ; nonthermal plasma ; atmospheric pressure ; nickel ; alumina ; Chemical technology ; TP1-1185 ; Chemistry ; QD1-999
Subject code	290
Language	English
Publishing date	2020-05-01T00:00:00Z
Publisher	MDPI AG
Document type	Article ; Online
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Article: Contribution of histone N-terminal tails to the structure and stability of nucleosomes

Iwasaki, Wakana / Miya, Yuta / Horikoshi, Naoki / Osakabe, Akihisa / Taguchi, Hiroyuki / Tachiwana, Hiroaki / Shibata, Takehiko / Kagawa, Wataru / Kurumizaka, Hitoshi

FEBS Open Bio. 2013, v. 3

2013

Abstract: ... histones, H2A, H2B, H3, or H4, lacked the N-terminal tail. We found that the deletion of the H2B or H3 N ...

Abstract	Histones are the protein components of the nucleosome, which forms the basic architecture of eukaryotic chromatin. Histones H2A, H2B, H3, and H4 are composed of two common regions, the “histone fold” and the “histone tail”. Many efforts have been focused on the mechanisms by which the post-translational modifications of histone tails regulate the higher-order chromatin architecture. On the other hand, previous biochemical studies have suggested that histone tails also affect the structure and stability of the nucleosome core particle itself. However, the precise contributions of each histone tail are unclear. In the present study, we determined the crystal structures of four mutant nucleosomes, in which one of the four histones, H2A, H2B, H3, or H4, lacked the N-terminal tail. We found that the deletion of the H2B or H3 N-terminal tail affected histone–DNA interactions and substantially decreased nucleosome stability. These findings provide important information for understanding the complex roles of histone tails in regulating chromatin structure.
Keywords	crystal structure ; histones ; mutants ; nucleosomes ; post-translational modification
Language	English
Size	p. 363-369.
Publishing place	Elsevier B.V.
Document type	Article
ZDB-ID	2651702-4
ISSN	2211-5463
ISSN	2211-5463
DOI	10.1016/j.fob.2013.08.007
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Article: Abeta N-terminal-end specific antibody reduced beta-amyloid in Alzheimer-model mice.

Horikoshi, Yuko / Mori, Takashi / Maeda, Masahiro / Kinoshita, Noriaki / Sato, Kumiko / Yamaguchi, Haruyasu

Biochemical and biophysical research communications

2004 Volume 325, Issue 2, Page(s) 384–387

Abstract: ... Abeta) vaccine is considered to be the most potent candidate. To cure AD, we developed Abeta N-terminal ...

Abstract	Alzheimer's disease (AD) is a neurodegenerative disease with memory dysfunction that is causing serious medical problems in modern society. For the fundamental treatment of AD, an amyloid beta protein (Abeta) vaccine is considered to be the most potent candidate. To cure AD, we developed Abeta N-terminal-end specific monoclonal antibody named 82E1, which does not cross-react with full-length Abeta precursor. Passive intraperitoneal administration of 82E1 markedly reduced total plaque area (Abeta burden) in the Tg2576 mouse brains. This was confirmed by the ELISA measurement of insoluble Abeta in the brain homogenates. The density of diffuse plaques, which increases in the late stage, was markedly reduced by the administration of 82E1, suggesting that the reduction of the Abeta burden was due to the prevention of newly developed diffuse plaques. Above results provide an insight into the further therapeutic intervention in AD with few adverse effects.
MeSH term(s)	Alzheimer Disease/metabolism ; Amyloid beta-Peptides/antagonists & inhibitors ; Amyloid beta-Peptides/immunology ; Amyloid beta-Peptides/metabolism ; Animals ; Antibodies, Monoclonal/chemistry ; Antibodies, Monoclonal/immunology ; Antibodies, Monoclonal/pharmacology ; Antibody Specificity ; Basal Ganglia/metabolism ; Basal Ganglia/pathology ; Basal Ganglia/ultrastructure ; Cerebral Cortex/metabolism ; Cerebral Cortex/pathology ; Cerebral Cortex/ultrastructure ; Disease Models, Animal ; Enzyme-Linked Immunosorbent Assay ; Hippocampus/metabolism ; Hippocampus/pathology ; Hippocampus/ultrastructure ; Immunohistochemistry ; Mice ; Mice, Transgenic
Chemical Substances	Amyloid beta-Peptides ; Antibodies, Monoclonal
Language	English
Publishing date	2004-12-10
Publishing country	United States
Document type	Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	205723-2
ISSN	0006-291X ; 0006-291X
ISSN (online)	0006-291X
ISSN	0006-291X
DOI	10.1016/j.bbrc.2004.10.039
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Article ; Online: Structural insight into replicative helicase loading in Escherichia coli.

Horikoshi, Naoki / Kurumizaka, Hitoshi

Journal of biochemistry

2022 Volume 171, Issue 6, Page(s) 605–607

Abstract: DNA replication is an essential, precisely regulated process that occurs once in a cell cycle. In the Gram-negative bacterium Escherichia coli, the replicative helicase EcDnaB and the helicase loader EcDnaC play key roles in the initiation step at the ... ...

Abstract	DNA replication is an essential, precisely regulated process that occurs once in a cell cycle. In the Gram-negative bacterium Escherichia coli, the replicative helicase EcDnaB and the helicase loader EcDnaC play key roles in the initiation step at the replication origin, oriC. EcDnaB and EcDnaC form a heterododecamer, in which hexameric EcDnaB is bound to hexameric EcDnaC. Using genetic, biochemical and structural biology approaches, many groups have probed the mechanism of replicative helicase loading, using helicases and helicase loaders from various species. Recent X-ray crystallography and cryogenic electron microscopy (cryo-EM) structural studies of the EcDnaB-EcDnaC complex revealed that the interaction of DnaC with DnaB triggers distortion accumulation on the closed ring of hexameric DnaB, inducing DnaB subunits to adopt the open helical form for replication progression. The high-resolution crystal structure of the DnaB-DnaC complex solved by Nagata et al. contributed to a better understanding of the conformational rearrangement of the DnaB ring. In addition to the structural alterations in DnaB subunits by DnaC, the binding of single-stranded DNA (ssDNA) substrates alters the ATP- and ADP-bound forms of DnaB and DnaC. These studies have proposed mechanisms by which DnaC regulates helicase loading onto ssDNA.
MeSH term(s)	Bacterial Proteins/metabolism ; DNA Helicases/metabolism ; DNA Replication ; DNA, Single-Stranded ; DnaB Helicases/chemistry ; Escherichia coli/metabolism ; Escherichia coli Proteins/metabolism
Chemical Substances	Bacterial Proteins ; DNA, Single-Stranded ; Escherichia coli Proteins ; DNA Helicases (EC 3.6.4.-) ; DnaB Helicases (EC 3.6.4.12)
Language	English
Publishing date	2022-03-02
Publishing country	England
Document type	Journal Article
ZDB-ID	218073-x
ISSN	1756-2651 ; 0021-924X
ISSN (online)	1756-2651
ISSN	0021-924X
DOI	10.1093/jb/mvac023
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