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Article ; Online: Prominent J Waves and Ventricular Fibrillation Caused by Myocarditis and Pericarditis After BNT162b2 mRNA COVID-19 Vaccination.

Uesako, Hayata / Fujikawa, Hirohisa / Hashimoto, Satoshi / Wakabayashi, Tadamasa

2022 Volume 38, Issue 6, Page(s) 844–847

MeSH term(s)	Arrhythmias, Cardiac/complications ; BNT162 Vaccine ; COVID-19/prevention & control ; COVID-19 Vaccines/adverse effects ; Humans ; Myocarditis/complications ; Myocarditis/etiology ; Pericarditis/diagnosis ; Pericarditis/etiology ; RNA, Messenger ; Vaccination/adverse effects ; Ventricular Fibrillation/complications
Chemical Substances	COVID-19 Vaccines ; RNA, Messenger ; BNT162 Vaccine (N38TVC63NU)
Language	English
Publishing date	2022-02-10
Publishing country	England
Document type	Case Reports
ZDB-ID	632813-1
ISSN	1916-7075 ; 0828-282X
ISSN (online)	1916-7075
ISSN	0828-282X
DOI	10.1016/j.cjca.2022.02.005
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Article: Ranking important predictors of the need for a high-acuity psychiatry unit among 2,064 inpatients admitted to psychiatric emergency hospitals: a random forest model.

Iwanaga, Mai / Yamaguchi, Sosei / Hashimoto, Satoshi / Hanaoka, Shimpei / Kaneyuki, Hiroshi / Fujita, Kiyoshi / Kishi, Yoshiki / Hirata, Toyoaki / Fujii, Chiyo / Sugiyama, Naoya

Frontiers in psychiatry

2024 Volume 15, Page(s) 1303189

Abstract: Aims: In order to uphold and enhance the emergency psychiatric care system, a thorough comprehension of the characteristics of patients who require a high-acuity psychiatry unit is indispensable. We aimed to clarify the most important predictors of the ... ...

Abstract	Aims: In order to uphold and enhance the emergency psychiatric care system, a thorough comprehension of the characteristics of patients who require a high-acuity psychiatry unit is indispensable. We aimed to clarify the most important predictors of the need for a high-acuity psychiatry unit using a random forest model. Methods: This cross-sectional study encompassed patients admitted to psychiatric emergency hospitals at 161 medical institutions across Japan between December 8, 2022, and January 31, 2023. Questionnaires were completed by psychiatrists, with a maximum of 30 patients assessed per medical institution. The questionnaires included psychiatrists' assessment of the patient's condition (exposure variables) and the need for a high-acuity psychiatry unit (outcome variables). The exposure variables consisted of 32 binary variables, including age, diagnoses, and clinical condition (i.e., factors on the clinical profile, emergency treatment requirements, and purpose of hospitalization). The outcome variable was the need for a high-acuity psychiatry unit, scored from 0 to 10. To identify the most important predictors of the need for a high-acuity psychiatry unit, we used a random forest model. As a sensitivity analysis, multivariate linear regression analysis was performed. Results: Data on 2,164 patients from 81 medical institutions were obtained (response rate, 50.3%). After excluding participants with missing values, this analysis included 2,064 patients. Of the 32 items, the top-5 predictors of the need for a high-acuity psychiatry unit were the essentiality of inpatient treatment (otherwise, symptoms will worsen or linger), need for 24-hour professional care, symptom severity, safety ensured by specialized equipment, and medication management. These items were each significantly and positively associated with the need for a high-acuity psychiatry unit in linear regression analyses (p < 0.001 for all). Conversely, items on age and diagnosis were lower in the ranking and were not statistically significant in linear regression models. Conclusion: Items related to the patient's clinical profile might hold greater importance in predicting the need for a high-acuity psychiatry unit than do items associated with age and diagnosis.
Language	English
Publishing date	2024-02-08
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2564218-2
ISSN	1664-0640
ISSN	1664-0640
DOI	10.3389/fpsyt.2024.1303189
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Article ; Online: Coronary microcirculatory dysfunction can be assessed by positive dicrotic wave and amplitude index on resting distal coronary pressure waveform, a newly developed index.

Fujimori, Yoshiharu / Hashimoto, Satoshi / Takahashi, Miki / Hoshino, Hirotada / Shimizu, Kenji / Terasawa, Yuya / Wakabayashi, Tadamasa / Imai, Taku

European heart journal open

2023 Volume 3, Issue 4, Page(s) oead070

Abstract: Aims: Some lesions have high resting distal coronary pressure/aortic pressure (Pd/Pa) despite low fractional flow reserve (FFR). This study aimed to assess microcirculatory dysfunction as a possible basal mechanism.: Methods and results: Patients ... ...

Abstract	Aims: Some lesions have high resting distal coronary pressure/aortic pressure (Pd/Pa) despite low fractional flow reserve (FFR). This study aimed to assess microcirculatory dysfunction as a possible basal mechanism. Methods and results: Patients were grouped into two according to coffee intake (caffeine 222 mg) before coronary angiography. Through an adenosine-induced Pd/Pa decrease, amplitude index was calculated by dividing the difference between the highest pressure after the inflection point and the minimal diastolic pressure by the pulse pressure on the Pd waveform. In 130 coronary lesions (caffeine group, Conclusion: In severe coronary stenosis, a high-remaining resting Pd/Pa with a high amplitude index or a positive dicrotic wave on the resting Pd waveform suggests microcirculatory dysfunction, such as insufficient arteriolar dilation reactive to myocardial ischaemia. Registration: UMIN000046883.
Language	English
Publishing date	2023-07-03
Publishing country	England
Document type	Journal Article
ISSN	2752-4191
ISSN (online)	2752-4191
DOI	10.1093/ehjopen/oead070
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Article ; Online: Experimental Demonstration to Control the Pulse Length of Coherent Undulator Radiation by Chirped Microbunching.

Tanaka, Takashi / Kida, Yuichiro / Hashimoto, Satoshi / Miyamoto, Shuji / Togashi, Tadashi / Tomizawa, Hiromitsu / Gocho, Aoi / Kaneshima, Keisuke / Tanaka, Yoshihito

Physical review letters

2023 Volume 131, Issue 14, Page(s) 145001

Abstract: In seeded free electron lasers (FELs), the temporal profile of FEL pulses usually reflects that of the seed pulse, and, thus, shorter FEL pulses are available with shorter seed pulses. In an extreme condition, however, this correlation is violated; the ... ...

Abstract	In seeded free electron lasers (FELs), the temporal profile of FEL pulses usually reflects that of the seed pulse, and, thus, shorter FEL pulses are available with shorter seed pulses. In an extreme condition, however, this correlation is violated; the FEL pulse is stretched by the so-called slippage effect in undulators, when the seed pulse is ultimately short, e.g., few-cycles long. In a previous Letter, we have proposed a scheme to suppress the slippage effect and reduce the pulse length of FELs ultimately down to a single-cycle duration, which is based on "chirped microbunching," or an electron density modulation with a varying modulation period. Toward realization of FELs based on the proposed scheme, experiments have been carried out to demonstrate its fundamental mechanism in the NewSUBARU synchrotron radiation facility, using an ultrashort seed pulse with the pulse length shorter than five cycles. Experimental results of spectral and cross-correlation measurements have been found to be in reasonable agreement with the theoretical predictions, which strongly suggests the successful demonstration of the proposed scheme.
Language	English
Publishing date	2023-10-20
Publishing country	United States
Document type	Journal Article
ZDB-ID	208853-8
ISSN	1079-7114 ; 0031-9007
ISSN (online)	1079-7114
ISSN	0031-9007
DOI	10.1103/PhysRevLett.131.145001
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Article ; Online: Translation arrest as a protein quality control system for aberrant translation of the 3'-UTR in mammalian cells.

Hashimoto, Satoshi / Nobuta, Risa / Izawa, Toshiaki / Inada, Toshifumi

FEBS letters

2019 Volume 593, Issue 8, Page(s) 777–787

Abstract: Read-through or mutations of a stop codon resulting in translation of the 3'-UTR produce potentially toxic C-terminally extended proteins. However, quality control mechanisms for such proteins are poorly understood in mammalian cells. Here, a ... ...

Abstract	Read-through or mutations of a stop codon resulting in translation of the 3'-UTR produce potentially toxic C-terminally extended proteins. However, quality control mechanisms for such proteins are poorly understood in mammalian cells. Here, a comprehensive analysis of the 3'-UTRs of genes associated with hereditary diseases identified novel arrest-inducing sequences in the 3'-UTRs of 23 genes that can repress the levels of their protein products. In silico analysis revealed that the hydrophobicity of the polypeptides encoded in the 3'-UTRs is correlated with arrest efficiency. These results provide new insight into quality control mechanisms mediated by 3'-UTRs to prevent the production of C-terminally extended cytotoxic proteins.
MeSH term(s)	3' Untranslated Regions/genetics ; HEK293 Cells ; Humans ; Hydrophobic and Hydrophilic Interactions ; Intracellular Signaling Peptides and Proteins/biosynthesis ; Intracellular Signaling Peptides and Proteins/chemistry ; LIM Domain Proteins/biosynthesis ; LIM Domain Proteins/chemistry ; Muscle Proteins/biosynthesis ; Muscle Proteins/chemistry ; N-Acetylgalactosamine-4-Sulfatase/biosynthesis ; N-Acetylgalactosamine-4-Sulfatase/chemistry ; Protein Biosynthesis/genetics ; Quality Control
Chemical Substances	3' Untranslated Regions ; FHL1 protein, human ; Intracellular Signaling Peptides and Proteins ; LIM Domain Proteins ; Muscle Proteins ; N-Acetylgalactosamine-4-Sulfatase (EC 3.1.6.12) ; ARSB protein, human (EC 3.1.6.12.)
Language	English
Publishing date	2019-03-23
Publishing country	England
Document type	Editorial ; Research Support, Non-U.S. Gov't
ZDB-ID	212746-5
ISSN	1873-3468 ; 0014-5793
ISSN (online)	1873-3468
ISSN	0014-5793
DOI	10.1002/1873-3468.13362
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Article ; Online: Anti-biofouling performance and microbial communities of an integrated fixed-film activated sludge membrane bioreactor with a fibrous carrier material: Pilot-scale demonstration.

Yoshino, Hiroyuki / Van Phan, Hop / Mori, Naomichi / Ohkuma, Naoki / Kawakami, Masaki / Nihei, Masahiko / Hashimoto, Satoshi / Wakabayashi, Ken / Hori, Tomoyuki / Terada, Akihiko

The Science of the total environment

2024 Volume 918, Page(s) 170291

Abstract: Widespread use of membrane bioreactors for high-performance wastewater treatment depends on the prevention of biofouling during membrane filtration, which can reduce operating costs. Biofouling is usually prevented using mechanical and chemical membrane ... ...

Abstract	Widespread use of membrane bioreactors for high-performance wastewater treatment depends on the prevention of biofouling during membrane filtration, which can reduce operating costs. Biofouling is usually prevented using mechanical and chemical membrane treatment methods, which can be time-consuming and expensive. In this study, we developed bio-capsules as a fluidizing carrier material in an integrated fixed-film activated sludge membrane bioreactor (IFAS-MBR). The bio-capsules were prepared from moniliform polyvinylidene chloride fibrous balls enclosed in a spherical plastic basket, and could harbor protozoa and metazoa. A pilot-scale anoxic-oxic IFAS-MBR system with a total volume of 132 m
MeSH term(s)	Animals ; Sewage ; Biofouling ; Biofilms ; RNA, Ribosomal, 16S ; Membranes, Artificial ; Bioreactors ; Microbiota ; Nitrogen ; Carbon
Chemical Substances	Sewage ; RNA, Ribosomal, 16S ; Membranes, Artificial ; Nitrogen (N762921K75) ; Carbon (7440-44-0)
Language	English
Publishing date	2024-01-23
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	121506-1
ISSN	1879-1026 ; 0048-9697
ISSN (online)	1879-1026
ISSN	0048-9697
DOI	10.1016/j.scitotenv.2024.170291
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Article: Translation arrest as a protein quality control system for aberrant translation of the 3′‐UTR in mammalian cells

Hashimoto, Satoshi / Nobuta, Risa / Izawa, Toshiaki / Inada, Toshifumi

FEBS letters. 2019 Apr., v. 593, no. 8

2019

Abstract: Read‐through or mutations of a stop codon resulting in translation of the 3′‐UTR produce potentially toxic C‐terminally extended proteins. However, quality control mechanisms for such proteins are poorly understood in mammalian cells. Here, a ... ...

Abstract	Read‐through or mutations of a stop codon resulting in translation of the 3′‐UTR produce potentially toxic C‐terminally extended proteins. However, quality control mechanisms for such proteins are poorly understood in mammalian cells. Here, a comprehensive analysis of the 3′‐UTRs of genes associated with hereditary diseases identified novel arrest‐inducing sequences in the 3′‐UTRs of 23 genes that can repress the levels of their protein products. In silico analysis revealed that the hydrophobicity of the polypeptides encoded in the 3′‐UTRs is correlated with arrest efficiency. These results provide new insight into quality control mechanisms mediated by 3′‐UTRs to prevent the production of C‐terminally extended cytotoxic proteins.
Keywords	computer simulation ; cytotoxicity ; hydrophobicity ; mammals ; polypeptides ; protein value ; quality control ; stop codon
Language	English
Dates of publication	2019-04
Size	p. 777-787.
Publishing place	John Wiley & Sons, Ltd
Document type	Article
Note	JOURNAL ARTICLE
ZDB-ID	212746-5
ISSN	1873-3468 ; 0014-5793
ISSN (online)	1873-3468
ISSN	0014-5793
DOI	10.1002/1873-3468.13362
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Article ; Online: Identification of a novel trigger complex that facilitates ribosome-associated quality control in mammalian cells.

Hashimoto, Satoshi / Sugiyama, Takato / Yamazaki, Reina / Nobuta, Risa / Inada, Toshifumi

Scientific reports

2020 Volume 10, Issue 1, Page(s) 3422

Abstract: Ribosome stalling triggers the ribosome-associated quality control (RQC) pathway, which targets collided ribosomes and leads to subunit dissociation, followed by proteasomal degradation of the nascent peptide. In yeast, RQC is triggered by Hel2-dependent ...

Abstract	Ribosome stalling triggers the ribosome-associated quality control (RQC) pathway, which targets collided ribosomes and leads to subunit dissociation, followed by proteasomal degradation of the nascent peptide. In yeast, RQC is triggered by Hel2-dependent ubiquitination of uS10, followed by subunit dissociation mediated by the RQC-trigger (RQT) complex. In mammals, ZNF598-dependent ubiquitination of collided ribosomes is required for RQC, and activating signal cointegrator 3 (ASCC3), a component of the ASCC complex, facilitates RQC. However, the roles of other components and associated factors of the ASCC complex remain unknown. Here, we demonstrate that the human RQC-trigger (hRQT) complex, an ortholog of the yeast RQT complex, plays crucial roles in RQC. The hRQT complex is composed of ASCC3, ASCC2, and TRIP4, which are orthologs of the RNA helicase Slh1(Rqt2), ubiquitin-binding protein Cue3(Rqt3), and zinc-finger type protein yKR023W(Rqt4), respectively. The ATPase activity of ASCC3 and the ubiquitin-binding activity of ASCC2 are crucial for triggering RQC. Given the proposed function of the RQT complex in yeast, we propose that the hRQT complex recognizes the ubiquitinated stalled ribosome and induces subunit dissociation to facilitate RQC.
MeSH term(s)	DNA Helicases/genetics ; DNA Helicases/metabolism ; HEK293 Cells ; Humans ; Multiprotein Complexes/genetics ; Multiprotein Complexes/metabolism ; Nuclear Proteins/genetics ; Nuclear Proteins/metabolism ; Ribosomes/genetics ; Ribosomes/metabolism ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Transcription Factors/genetics ; Transcription Factors/metabolism
Chemical Substances	ASCC2 protein, human ; Multiprotein Complexes ; Nuclear Proteins ; Saccharomyces cerevisiae Proteins ; TRIP4 protein, human ; Transcription Factors ; ASCC3 protein, human (EC 3.6.1.-) ; DNA Helicases (EC 3.6.4.-)
Language	English
Publishing date	2020-02-25
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-020-60241-w
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Article ; Online: Two modes of Cue2-mediated mRNA cleavage with distinct substrate recognition initiate no-go decay.

Tomomatsu, Shota / Watanabe, Atsuya / Tesina, Petr / Hashimoto, Satoshi / Ikeuchi, Ken / Li, Sihan / Matsuo, Yoshitaka / Beckmann, Roland / Inada, Toshifumi

Nucleic acids research

2022 Volume 51, Issue 1, Page(s) 253–270

Abstract: Ribosome collisions are recognized by E3 ubiquitin ligase Hel2/ZNF598, leading to RQC (ribosome-associated quality control) and to endonucleolytic cleavage and degradation of the mRNA termed NGD (no-go decay). NGD in yeast requires the Cue2 endonuclease ... ...

Abstract	Ribosome collisions are recognized by E3 ubiquitin ligase Hel2/ZNF598, leading to RQC (ribosome-associated quality control) and to endonucleolytic cleavage and degradation of the mRNA termed NGD (no-go decay). NGD in yeast requires the Cue2 endonuclease and occurs in two modes, either coupled to RQC (NGDRQC+) or RQC uncoupled (NGDRQC-). This is mediated by an unknown mechanism of substrate recognition by Cue2. Here, we show that the ubiquitin binding activity of Cue2 is required for NGDRQC- but not for NGDRQC+, and that it involves the first two N-terminal Cue domains. In contrast, Trp122 of Cue2 is crucial for NGDRQC+. Moreover, Mbf1 is required for quality controls by preventing +1 ribosome frameshifting induced by a rare codon staller. We propose that in Cue2-dependent cleavage upstream of the collided ribosomes (NGDRQC-), polyubiquitination of eS7 is recognized by two N-terminal Cue domains of Cue2. In contrast, for the cleavage within collided ribosomes (NGDRQC+), the UBA domain, Trp122 and the interaction between Mbf1 and uS3 are critical.
MeSH term(s)	Protein Biosynthesis ; Ribosomes/genetics ; Ribosomes/metabolism ; RNA, Messenger/genetics ; RNA, Messenger/metabolism ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/metabolism ; Ubiquitin-Protein Ligases/genetics ; Ubiquitin-Protein Ligases/metabolism ; Ubiquitination ; Endonucleases/metabolism
Chemical Substances	Hel2 protein, S cerevisiae (EC 2.3.2.27) ; RNA, Messenger ; Saccharomyces cerevisiae Proteins ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; Endonucleases (EC 3.1.-)
Language	English
Publishing date	2022-11-17
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	186809-3
ISSN	1362-4962 ; 1362-4954 ; 0301-5610 ; 0305-1048
ISSN (online)	1362-4962 ; 1362-4954
ISSN	0301-5610 ; 0305-1048
DOI	10.1093/nar/gkac1172
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Article: Crucial role of leaky initiation of uORF3 in the downregulation of HNT1 by ER stress

Matsuki, Yasuko / Saito, Taishi / Nakano, Yu / Hashimoto, Satoshi / Matsuo, Yoshitaka / Inada, Toshifumi

Biochemical and biophysical research communications. 2020 July 12, v. 528, no. 1

2020

Abstract: eIF2α phosphorylation-mediated translational regulation is crucial for global repression of translation by various stresses, including the unfolded protein response (UPR) in eukaryotes. Although translational control during UPR has not been extensively ... ...

Abstract	eIF2α phosphorylation-mediated translational regulation is crucial for global repression of translation by various stresses, including the unfolded protein response (UPR) in eukaryotes. Although translational control during UPR has not been extensively investigated in S. cerevisiae, Hac1-mediated production of long transcripts containing uORFs was shown to repress the translation of histidine triad nucleotide-binding 1 (HNT1) mRNA. The present study showed that uORF3 is required for HNT1 expression, as well as down-regulating HNT1 translation. Translation initiation by uORF3 is inefficient, with uORF3 having a strong Kozak sequence efficiently repressing the translation of HNT1. We propose that leaky scanning of uORF3 is responsible for the downregulation of HNT1 during UPR.
Keywords	eukaryotic cells ; histidine ; research ; unfolded protein response
Language	English
Dates of publication	2020-0712
Size	p. 186-192.
Publishing place	Elsevier Inc.
Document type	Article
Note	NAL-AP-2-clean
ZDB-ID	205723-2
ISSN	0006-291X ; 0006-291X
ISSN (online)	0006-291X
ISSN	0006-291X
DOI	10.1016/j.bbrc.2020.04.104
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