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Author Noriyuki Nishida

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Biomarkers and diagnostic guidelines for sporadic Creutzfeldt-Jakob disease.

Peter Hermann, Brian Appleby, Jean-Philippe Brandel, Byron Caughey, Steven Collins, Michael D Geschwind, Alison Green, Stephane Haïk, Gabor G Kovacs, Anna Ladogana, Franc Llorens, Simon Mead, Noriyuki Nishida, Suvankar Pal, Piero Parchi, Maurizio Pocchiari, Katsuya Satoh, Gianluigi Zanusso, Inga Zerr,

Sporadic Creutzfeldt-Jakob disease is a fatal neurodegenerative disease caused by misfolded prion proteins (PrP<sup>Sc</sup>). Effective therapeutics are currently not available and accurate diagnosis can be challenging. Clinical diagnostic criteria use a combination of characteristic neuropsychiatric symptoms, CSF proteins 14-3-3, MRI, and EEG. Supportive biomarkers, such as high CSF total tau, ... Read more >>

Lancet Neurol (The Lancet. Neurology)
[2021, 20(3):235-246]

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Liquid-liquid phase separation of full-length prion protein initiates conformational conversion in vitro.

Hiroya Tange, Daisuke Ishibashi, Takehiro Nakagaki, Yuzuru Taguchi, Yuji O Kamatari, Hiroki Ozawa, Noriyuki Nishida,

Prion diseases are characterized by the accumulation of amyloid fibrils. The causative agent is an infectious amyloid that is comprised solely of misfolded prion protein (PrP<sup>Sc</sup>). Prions can convert normal cellular prion protein (PrP<sup>C</sup>) to proteinase-resistant PrP (PrP-res) in vitro; however, the intermediate steps involved in this spontaneous conversion still ... Read more >>

J Biol Chem (The Journal of biological chemistry)
[2021, :100367]

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Dextran sulphate inhibits an association of prions with plasma membrane at the early phase of infection.

Takayuki Fuse, Takehiro Nakagaki, Takujiro Homma, Hiroya Tange, Naohiro Yamaguchi, Ryuichiro Atarashi, Daisuke Ishibashi, Noriyuki Nishida,

The defining characteristic of prion diseases is conversion of a cellular prion protein (PrP<sup>C</sup>) to an abnormal prion protein (PrP<sup>Sc</sup>). The exogenous attachment of PrP<sup>Sc</sup> to the surface of a target cell is critical for infection. However, the initial interaction of PrP<sup>Sc</sup> with the cell surface is poorly characterized. In ... Read more >>

Neurosci Res (Neuroscience research)
[2021, :]

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Abnormal prion protein deposits with high seeding activities in the skeletal muscle, femoral nerve, and scalp of an autopsied case of sporadic Creutzfeldt-Jakob disease.

Hiroyuki Honda, Shinichiro Mori, Akihiro Watanabe, Naokazu Sasagasako, Shoko Sadashima, Trang Đồng, Katsuya Satoh, Noriyuki Nishida, Toru Iwaki,

We report the general autopsy findings of abnormal prion protein (PrP) deposits with their seeding activities, as assessed by the real-time quaking-induced conversion (RT-QuIC) method, in a 72-year-old female patient with sporadic Creutzfeldt-Jakob disease (sCJD). At 68 years of age, she presented with gait disturbance and visual disorders. Electroencephalography showed periodic ... Read more >>

Neuropathology (Neuropathology : official journal of the Japanese Society of Neuropathology)
[2021, :]

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Novel Compounds Identified by Structure-Based Prion Disease Drug Discovery Using In Silico Screening Delay the Progression of an Illness in Prion-Infected Mice.

Daisuke Ishibashi, Takeshi Ishikawa, Satoshi Mizuta, Hiroya Tange, Takehiro Nakagaki, Tsuyoshi Hamada, Noriyuki Nishida,

The accumulation of abnormal prion protein (PrP<sup>Sc</sup>) produced by the structure conversion of PrP (PrP<sup>C</sup>) in the brain induces prion disease. Although the conversion process of the protein is still not fully elucidated, it has been known that the intramolecular chemical bridging in the most fragile pocket of PrP, known ... Read more >>

Neurotherapeutics (Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics)
[2020, 17(4):1836-1849]

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Feasibility studies of radioiodinated pyridyl benzofuran derivatives as potential SPECT imaging agents for prion deposits in the brain.

Takeshi Fuchigami, Masao Kawasaki, Hiroyuki Watanabe, Takehiro Nakagaki, Kodai Nishi, Kazunori Sano, Ryuichiro Atarashi, Mari Nakaie, Sakura Yoshida, Masahiro Ono, Noriyuki Nishida, Morio Nakayama,

<h4>Introduction</h4>Prion diseases are fatal neurodegenerative disorders caused by the deposition of abnormal prion protein aggregates (PrP<sup>Sc</sup>) in the central nervous system. This study aimed to evaluate the use of iodinated pyridyl benzofuran (IPBF) derivatives as single-photon emission computed tomography (SPECT) probes for the detection of cerebral PrP<sup>Sc</sup> deposits.<h4>Methods</h4>In vitro binding ... Read more >>

Nucl Med Biol (Nuclear medicine and biology)
[2020, 90-91:41-48]

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Administration of FK506 from Late Stage of Disease Prolongs Survival of Human Prion-Inoculated Mice.

Takehiro Nakagaki, Daisuke Ishibashi, Tsuyoshi Mori, Yukiko Miyazaki, Hanae Takatsuki, Hiroya Tange, Yuzuru Taguchi, Katsuya Satoh, Ryuichiro Atarashi, Noriyuki Nishida,

Human prion diseases are etiologically categorized into three forms: sporadic, genetic, and infectious. Sporadic Creutzfeldt-Jakob disease (sCJD) is the most common type of human prion disease that manifests as subacute progressive dementia. No effective therapy for sCJD is currently available. Potential therapeutic compounds are frequently tested in rodents infected with ... Read more >>

Neurotherapeutics (Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics)
[2020, 17(4):1850-1860]

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Correction to: Intra-Arterial Transplantation of Low-Dose Stem Cells Provides Functional Recovery Without Adverse Effects After Stroke.

Yuhtaka Fukuda, Nobutaka Horie, Katsuya Satoh, Susumu Yamaguchi, Youichi Morofuji, Takeshi Hiu, Tsuyoshi Izumo, Kentaro Hayashi, Noriyuki Nishida, Izumi Nagata,

The original version of this article unfortunately contained an error in affiliation of Yuhtaka Fukuda. ... Read more >>

Cell Mol Neurobiol (Cellular and molecular neurobiology)
[2020, 40(6):1057]

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Generation, optimization and characterization of novel anti-prion compounds.

Andrea Altieri, Evgeny A Spiridonov, Semen I Sivtzev, Daisuke Ishibashi, Silvia Biggi, Noriyuki Nishida, Emiliano Biasini, Alexander V Kurkin,

Prions are misfolded proteins involved in neurodegenerative diseases of high interest in veterinary and public health. In this work, we report the chemical space exploration around the anti-prion compound BB 0300674 in order to gain an understanding of its Structure Activity Relationships (SARs). A series of 43 novel analogues, based ... Read more >>

Bioorg Med Chem (Bioorganic & medicinal chemistry)
[2020, 28(21):115717]

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Difference in driver gene expression patterns between perihilar and peripheral intrahepatic cholangiocarcinoma in an experimental mouse model.

Toshiyuki Adachi, Tomohiko Adachi, Takehiro Nakagaki, Shinichiro Ono, Masaaki Hidaka, Shinichiro Ito, Kengo Kanetaka, Mitsuhisa Takatsuki, Noriyuki Nishida, Susumu Eguchi,

BACKGROUND:The prognosis of intrahepatic cholangiocarcinoma (ICC) is based on tumor localization; however, the mechanism remains unknown. Therefore, we investigated the biological characteristics of perihilar and peripheral ICC in a mouse model. METHODS:The model was established by the administration of three oncogenic plasmids harboring myristoylated AKT, mutated human YAP, and pCMV-Sleeping ... Read more >>

J Hepatobiliary Pancreat Sci (Journal of hepato-biliary-pancreatic sciences)
[2020, 27(8):477-486]

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Discrimination between L-type and C-type bovine spongiform encephalopathy by the strain-specific reactions of real-time quaking-induced conversion.

Kaori Ubagai, Shigeo Fukuda, Tsuyoshi Mori, Hanae Takatsuki, Yuzuru Taguchi, Soichi Kageyama, Noriyuki Nishida, Ryuichiro Atarashi,

Real-time quaking-induced conversion (RT-QUIC) assays using Escherichia coli-derived purified recombinant prion protein (rPrP) enable us to amplify a trace amount of the abnormal form of PrP (PrPSc) from specimens. This technique can be useful for the early diagnosis of both human and animal prion diseases and the assessment of prion ... Read more >>

Biochem Biophys Res Commun (Biochemical and biophysical research communications)
[2020, 526(4):1049-1053]

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Prion protein interacts with the metabotropic glutamate receptor 1 and regulates the organization of Ca2+ signaling.

Takehiro Matsubara, Katsuya Satoh, Takujiro Homma, Takehiro Nakagaki, Naohiro Yamaguchi, Ryuichiro Atarashi, Yuka Sudo, Yasuhito Uezono, Daisuke Ishibashi, Noriyuki Nishida,

Cellular prion protein (PrP) is a membrane protein that is highly conserved among mammals and mainly expressed on the cell surface of neurons. Despite its reported interactions with various membrane proteins, no functional studies have so far been carried out on it, and its physiological functions remain unclear. Neuronal cell ... Read more >>

Biochem Biophys Res Commun (Biochemical and biophysical research communications)
[2020, 525(2):447-454]

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Molecular dynamics simulation of local structural models of PrPSc reveals how codon 129 polymorphism affects propagation of PrPSc

Hiroki Otaki, Yuzuru Taguchi, Noriyuki Nishida,

Prions are unconventional pathogen without nucleotide genome and their pathogenic properties are defined by the primary structure and the conformation of the constituent abnormal isoform (PrP Sc ) of prion protein (PrP). A polymorphic codon 129 of human PrP that is valine (V129) or methionine (M129) is particularly influential on ... Read more >>

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Postmortem Quantitative Analysis of Prion Seeding Activity in the Digestive System.

Katsuya Satoh, Takayuki Fuse, Toshiaki Nonaka, Trong Dong, Masaki Takao, Takehiro Nakagaki, Daisuke Ishibashi, Yuzuru Taguchi, Ban Mihara, Yasushi Iwasaki, Mari Yoshida, Noriyuki Nishida,

Human prion diseases are neurodegenerative disorders caused by prion protein. Although infectivity was historically detected only in the central nervous system and lymphoreticular tissues of patients with sporadic Creutzfeldt-Jakob disease, recent reports suggest that the seeding activity of Creutzfeldt-Jakob disease prions accumulates in various non-neuronal organs including the liver, kidney, ... Read more >>

Molecules (Molecules (Basel, Switzerland))
[2019, 24(24):]

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Liquid-liquid phase separation of full-length prion protein initiates conformational conversion in vitro

Hiroya Tange, Daisuke Ishibashi, Takehiro Nakagaki, Yuzuru Taguchi, Yuji Kamatari, Hiroki Ozawa, Noriyuki Nishida,

Prion diseases are characterized by accumulation of amyloid fibrils. The causative agent is an infectious amyloid that is comprised solely of misfolded prion protein (PrP Sc ). Prions can convert PrP C to proteinase-resistant PrP (PrP-res) in vitro ; however, the intermediate steps involved in the spontaneous conversion remain unknown. ... Read more >>

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Conformation-dependent influences of hydrophobic amino acids in two in-register parallelβ-sheet amyloids, anα-synuclein amyloid and a local structural model of PrPSc

Hiroki Otaki, Yuzuru Taguchi, Noriyuki Nishida,

Prions are pathogens that consist solely of abnormal isoforms of prion protein (PrP Sc ) without any genetic material. Therefore, they depend on purely protein-based mechanisms for diversification and maintenance of the pathogenetic information of prion strains. According to the protein-only hypothesis, the pathogenic properties of prions are determined by ... Read more >>

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Development of Radioiodinated Benzofuran Derivatives for in Vivo Imaging of Prion Deposits in the Brain.

Takeshi Fuchigami, Masao Kawasaki, Ryusuke Koyama, Mari Nakaie, Takehiro Nakagaki, Kazunori Sano, Ryuichiro Atarashi, Sakura Yoshida, Mamoru Haratake, Masahiro Ono, Noriyuki Nishida, Morio Nakayama,

Prion diseases are fatal neurodegenerative disorders associated with the deposition of abnormal prion protein aggregates (PrP<sup>Sc</sup>) in the brain tissue. Here, we report the development of <sup>125</sup>I-labeled iodobenzofuran (IBF) derivatives as single photon emission computed tomography (SPECT) imaging probes to detect cerebral PrP<sup>Sc</sup> deposits. We synthesized and radioiodinated several 5-IBF ... Read more >>

ACS Infect Dis (ACS infectious diseases)
[2019, 5(12):2003-2013]

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In silico evidence of unique behaviors of methionine in an in-register parallel beta-sheet amyloid, suggestive of its possible contribution to strain diversity of amyloids

Hiroki Otaki, Yuzuru Taguchi, Noriyuki Nishida,

Mechanism of strain diversity of prions is a long-standing conundrum, because prions consist solely of abnormal isoform of prion protein (PrP Sc ) devoid of genetic material. Pathogenic properties of prions are determined by conformations of the constituent PrP Sc according to the protein-only hypothesis, and alterations to even a ... Read more >>

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A designer molecular chaperone against transmissible spongiform encephalopathy slows disease progression in mice and macaques.

Keiichi Yamaguchi, Yuji O Kamatari, Fumiko Ono, Hiroaki Shibata, Takayuki Fuse, Abdelazim Elsayed Elhelaly, Mayuko Fukuoka, Tsutomu Kimura, Junji Hosokawa-Muto, Takeshi Ishikawa, Minoru Tobiume, Yoshinori Takeuchi, Yutaka Matsuyama, Daisuke Ishibashi, Noriyuki Nishida, Kazuo Kuwata,

Transmissible spongiform encephalopathies (TSEs) are fatal neurodegenerative diseases that lack therapeutic solutions. Here, we show that the molecular chaperone (N,N'-([cyclohexylmethylene]di-4,1-phenylene)bis(2-[1-pyrrolidinyl]acetamide)), designed via docking simulations, molecular dynamics simulations and quantum chemical calculations, slows down the progress of TSEs. In vitro, the designer molecular chaperone stabilizes the normal cellular prion protein, eradicates ... Read more >>

Nat Biomed Eng (Nature biomedical engineering)
[2019, 3(3):206-219]

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Mechanisms of Strain Diversity of Disease-Associated in-Register Parallel β-Sheet Amyloids and Implications About Prion Strains.

Yuzuru Taguchi, Hiroki Otaki, Noriyuki Nishida,

The mechanism of prion strain diversity remains unsolved. Investigation of inheritance and diversification of protein-based pathogenic information demands the identification of the detailed structures of abnormal isoforms of the prion protein (PrPSc); however, achieving purification is difficult without affecting infectivity. Similar prion-like properties are recognized also in other disease-associated in-register ... Read more >>

Viruses (Viruses)
[2019, 11(2):]

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Mechanisms of strain diversity of disease-associated in-register parallel β-sheet amyloids and implications about prion strains

Yuzuru Taguchi, Hiroki Otaki, Noriyuki Nishida,

The mechanism of strain diversity of prions still remains unsolved, because the investigation of inheritance and diversification of the protein-based pathogenic information demands identification of the detailed structures of abnormal isoform of prion protein (PrP Sc ), while it is difficult to purify for analysis without affecting the infectious nature. ... Read more >>

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Disulfide-crosslink scanning reveals prion-induced conformational changes and prion strain-specific structures of the pathological prion protein PrPSc.

Yuzuru Taguchi, Li Lu, Cristobal Marrero-Winkens, Hiroki Otaki, Noriyuki Nishida, Hermann M Schatzl,

Prions are composed solely of the pathological isoform (PrP<sup>Sc</sup>) of the normal cellular prion protein (PrP<sup>C</sup>). Identification of different PrP<sup>Sc</sup> structures is crucially important for understanding prion biology because the pathogenic properties of prions are hypothesized to be encoded in the structures of PrP<sup>Sc</sup> However, these structures remain yet to ... Read more >>

J Biol Chem (The Journal of biological chemistry)
[2018, 293(33):12730-12740]

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Correction: Disulfide-crosslink scanning reveals prion-induced conformational changes and prion strain-specific structures of the pathological prion protein PrPSc.

Yuzuru Taguchi, Li Lu, Cristobal Marrero-Winkens, Hiroki Otaki, Noriyuki Nishida, Hermann M Schatzl,

J Biol Chem (The Journal of biological chemistry)
[2018, 293(38):14925]

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Antiviral Activity of Peanut (Arachis hypogaea L.) Skin Extract Against Human Influenza Viruses.

Juliann Nzembi Makau, Ken Watanabe, Magdy M D Mohammed, Noriyuki Nishida,

The high propensity of influenza viruses to develop resistance to antiviral drugs necessitates the continuing search for new therapeutics. Peanut skins, which are low-value byproducts of the peanut industry, are known to contain high levels of polyphenols. In this study, we investigated the antiviral activity of ethanol extracts of peanut ... Read more >>

J Med Food (Journal of medicinal food)
[2018, 21(8):777-784]

Cited: 5 times

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Molecular dynamics simulation reveals that switchable combinations of β-sheets underlie the prion-like properties of α-synuclein amyloids

Hiroki Otaki, Yuzuru Taguchi, Noriyuki Nishida,

Diversity of prion strains is one of the most mysterious traits of prions because they are mere aggregates of abnormally-folded forms of single protein species, prion protein (PrP Sc ), without genome. Although the strain-specific properties are hypothesized to be enciphered in the strain-specific structures of PrP Sc instead of ... Read more >>

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