Výsledky vyhledávání - "Masuhiro Takata"

Conformational Change in Hamster Scrapie Prion Protein (PrP27-30) Associated with Proteinase K Resistance and Prion Infectivity

Autor: Kenta Teruya, Morikazu Shinagawa, Takashi Yokoyama, Shirou Mohri, Masuhiro Takata, Sachiko Y. Suzuki

Publikováno v: Journal of Veterinary Medical Science. 70:159-165

The scrapie prion protein (PrP27-30) is a crucial component of the prion and is responsible for its transmissibility. Structural information on this protein is limited because it is insoluble and shows aggregated properties. In this study, PrP27-30 w

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5a60b72ee5a2b73953ba992fabd9c18c
https://doi.org/10.1292/jvms.70.159

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Tumor necrosis factor alpha is not a pathogenic determinant in acute lethal encephalitis induced by a highly neurovirulent strain of mouse hepatitis virus

Autor: Kazuya Shirato, Masuhiro Takata, Eiichi Momotani, Takahide Taniguchi, Kenji Sekikawa

Publikováno v: Archives of Virology. 153:549-553

To investigate the role of tumor necrosis factor alpha (TNFalpha) in the pathogenesis of acute viral encephalitis, TNFalpha-deficient mice were infected with a highly neurovirulent strain of mouse hepatitis virus, JHM, and compared with JHM-infected

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https://doi.org/10.1007/s00705-007-0006-5

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Assessment of Prion Inactivation by Combined Use ofBacillus-Derived Protease and SDS

Autor: Takashi Yokoyama, Miyako Yoshioka, Koji Nishizawa, Shirou Mohri, Yuichi Murayama, Masuhiro Takata, Katsuhiro Miura, Takehiro Miwa

Publikováno v: Bioscience, Biotechnology, and Biochemistry. 71:2565-2568

Prions, infectious agents causing transmissible spongiform encephalopathy, retain infectivity even after undergoing routine sterilization processes. We found that MSK103 protease, identified in our previous study, effectively reduces infectivity and

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9b4f4e2fa77c1e0ae576ee11b18c2207
https://doi.org/10.1271/bbb.70257

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Prion inactivation by the Maillard reaction

Autor: Shirou Mohri, Takashi Yokoyama, Mitsugu Akagawa, Kyozo Suyama, Yuichi Murayama, Masuhiro Takata, Hiroko Horii, Miyako Yoshioka

Publikováno v: Biochemical and Biophysical Research Communications. 356:245-248

Since variant Creutzfeldt-Jakob disease (vCJD) has been suspected to be attributable to the infectious agents associated with bovine spongiform encephalopathy (BSE), it is important to prevent the transmission of pathogenic forms of prion protein (Pr

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::97651425f375533048305676ba63a571
https://doi.org/10.1016/j.bbrc.2007.02.113

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Protein misfolding cyclic amplification as a rapid test for assessment of prion inactivation

Autor: Koichi Sato, Morikazu Shinagawa, Takashi Sudo, Miyako Yoshioka, Masuhiro Takata, Yuichi Murayama, Shirou Mohri, Hiroko Horii, Takashi Yokoyama

Publikováno v: Biochemical and Biophysical Research Communications. 348:758-762

Abnormal isoform of prion proteins (PrP(Sc)), which are infectious agents associated with prion diseases, retain infectivity after undergoing routine sterilization processes. A sensitive method to detect the infectivity is a bioassay, and it has been

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4817ea227213f4c84ff50fd4f39e4834
https://doi.org/10.1016/j.bbrc.2006.07.130

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Rapid PrPScDetection in Lymphoid Tissue and Application to Scrapie Surveillance of Fallen Stock in Japan: Variable PrPScAccumulation in Palatal Tonsil in Natural Scrapie

Autor: Takashi Yokoyama, Hiroko Hayashi, Kimi Shimada, Masuhiro Takata, Yoshifumi Iwamaru, Morikazu Imamura, Morikazu Shinagawa, Yuka Ookubo, Mary Jo Schmerr

Publikováno v: Microbiology and Immunology. 49:801-804

Rapid western blot (WB) procedure for an abnormal isoform of prion protein (PrP(Sc) ) detection in lymphoid tissues was established and has been applied to the surveillance of fallen stock. In this program, brain and palatal tonsil were examined by W

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https://doi.org/10.1111/j.1348-0421.2005.tb03660.x

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The N-terminal cleavage site of PrPSc from BSE differs from that of PrPSc from scrapie

Autor: Morikazu Shinagawa, Hiroko Hayashi, Yuko Ushiki, Morikazu Imamura, Yoshifumi Iwamaru, Masuhiro Takata, Takashi Yokoyama

Publikováno v: Biochemical and Biophysical Research Communications. 328:1024-1027

Heterogeneity in transmissible spongiform encephalopathy is thought to have derived from conformational variation in an abnormal isoform of the prion protein (PrPSc). To characterize PrPSc in bovine spongiform encephalopathy (BSE) and scrapie, we ana

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https://doi.org/10.1016/j.bbrc.2005.01.065

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Effect of Tissue Deterioration on Postmortem BSE Diagnosis by Immunobiochemical Detection of an Abnormal Isoform of Prion Protein

Autor: Kumiko M. Kimura, Takashi Yokoyama, Masuhiro Takata, Yuichi Tagawa, Morikazu Shinagawa, Yoshifumi Iwamaru, Hiroko Hayashi, Yuko Ushiki

Publikováno v: Journal of Veterinary Medical Science. 66:515-520

Surveillance for bovine spongiform encephalopathy (BSE) in fallen stock in Japan is conducted with a commercial enzyme-linked immunosorbent assay (ELISA) for mass screening, with Western blotting (WB) and immunohistochemistry performed for confirmati

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https://doi.org/10.1292/jvms.66.515

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A Catalytic Amino Acid and Primary Structure of Active Site inAspevgillus nigerα-Glucosidase

Autor: Masuhiro Takata, Seiya Chiba, Hirokazu Matsui, Haruhide Mori, Atsuo Kimura, Yukiharu Fukushi

Publikováno v: Bioscience, Biotechnology, and Biochemistry. 61:1091-1098

The catalytic amino acid residue of Aspergillus niger alpha-glucosidase (ANGase) was identified by modification with conduritol B epoxide (CBE), a mechanism-based irreversible inactivator. The inactivation by CBE followed pseudo-first order kinetics.

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https://doi.org/10.1271/bbb.61.1091

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Substrate Specificity and Subsite Affinities of Crystalline α-Glucosidase fromAspergillus niger

Autor: Akishige Somoto, Hirokazu Matsui, Akihiko Kita, Seiya Chiba, Masuhiro Takata, Atsuo Kimura

Publikováno v: Agricultural and Biological Chemistry. 55:2327-2335

Asp. niger α-glucosidase was crystallized in ammonium sulfate solution after chromatographies on DEAE-Sepharose CL-6B and TOYOPEARL HW-55 columns. The crystalline α-glucosidase, which was a glycoprotein containing 25.5% carbohydrate as glucose, gav

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https://doi.org/10.1080/00021369.1991.10870952

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