Zobrazeno 1 - 10 of 10 pro vyhledávání: '"Rawiwan Wongnak"'
1
Akademický článek
Non-Glycosylated SARS-CoV-2 Omicron BA.5 Receptor Binding Domain (RBD) with a Native-like Conformation Induces a Robust Immune Response with Potent Neutralization in a Mouse Model
Autor: Rawiwan Wongnak, Subbaian Brindha, Mami Oba, Takahiro Yoshizue, Md. Din Islam, M. Monirul Islam, Hitoshi Takemae, Tetsuya Mizutani, Yutaka Kuroda
Publikováno v: Molecules, Vol 29, Iss 11, p 2676 (2024)
The Omicron BA.5 variant of SARS-CoV-2 is known for its high transmissibility and its capacity to evade immunity provided by vaccine protection against the (original) Wuhan strain. In our prior research, we successfully produced the receptor-binding
Externí odkaz: https://doaj.org/article/db540d4fcff048e2bb9197300c2132bb
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2
Akademický článek
E. coli production of a multi-disulfide bonded SARS-CoV-2 Omicron BA.5 RBD exhibiting native-like biochemical and biophysical properties
Autor: Rawiwan Wongnak, Subbaian Brindha, Takahiro Yoshizue, Sawaros Onchaiya, Kenji Mizutani, Yutaka Kuroda
Publikováno v: Biophysics and Physicobiology, Vol 20 (2023)
Low-cost bacterial production of the receptor binding domain (RBD) of the SARS-CoV-2 Omicron spike protein holds significant potential in expediting the development of therapeutics against COVID-19. However, RBD contains eight cysteines forming four
Externí odkaz: https://doaj.org/article/819f364e4fc448989118ac605516667c
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3
Akademický článek
Antisera Produced Using an E. coli-Expressed SARS-CoV-2 RBD and Complemented with a Minimal Dose of Mammalian-Cell-Expressed S1 Subunit of the Spike Protein Exhibits Improved Neutralization
Autor: Takahiro Yoshizue, Subbaian Brindha, Rawiwan Wongnak, Hitoshi Takemae, Mami Oba, Tetsuya Mizutani, Yutaka Kuroda
Publikováno v: International Journal of Molecular Sciences, Vol 24, Iss 13, p 10583 (2023)
E. coli-expressed proteins could provide a rapid, cost-effective, and safe antigen for subunit vaccines, provided we can produce them in a properly folded form inducing neutralizing antibodies. Here, we use an E. coli-expressed SARS-CoV-2 receptor-bi
Externí odkaz: https://doaj.org/article/b61963e48757446c80e24adff2a8bff3
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4
Akademický článek
An Escherichia coli Expressed Multi-Disulfide Bonded SARS-CoV-2 RBD Shows Native-like Biophysical Properties and Elicits Neutralizing Antisera in a Mouse Model
Autor: Subbaian Brindha, Takahiro Yoshizue, Rawiwan Wongnak, Hitoshi Takemae, Mami Oba, Tetsuya Mizutani, Yutaka Kuroda
Publikováno v: International Journal of Molecular Sciences, Vol 23, Iss 24, p 15744 (2022)
A large-scale Escherichia coli (E. coli) production of the receptor-binding domain (RBD) of the SARS-CoV-2 could yield a versatile and low-cost antigen for a subunit vaccine. Appropriately folded antigens can potentially elicit the production of neut
Externí odkaz: https://doaj.org/article/08ae189b284c4520923e0290d33b30fa
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5
Antisera Produced Using an E. coli-Expressed SARS-CoV-2 RBD and Complemented with a Minimal Dose of Mammalian-Cell-Expressed S1 Subunit of the Spike Protein Exhibits Improved Neutralization
Autor: Kuroda, Takahiro Yoshizue, Subbaian Brindha, Rawiwan Wongnak, Hitoshi Takemae, Mami Oba, Tetsuya Mizutani, Yutaka
Publikováno v: International Journal of Molecular Sciences; Volume 24; Issue 13; Pages: 10583
E. coli-expressed proteins could provide a rapid, cost-effective, and safe antigen for subunit vaccines, provided we can produce them in a properly folded form inducing neutralizing antibodies. Here, we use an E. coli-expressed SARS-CoV-2 receptor-bi
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=multidiscipl::33dda14d46abba9a3315a8cba2833c81
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7
Akademický článek
Non-Glycosylated SARS-CoV-2 Omicron BA.5 Receptor Binding Domain (RBD) with a Native-like Conformation Induces a Robust Immune Response with Potent Neutralization in a Mouse Model.
Autor: Wongnak, Rawiwan1 (AUTHOR) s218131w@st.go.tuat.ac.jp, Brindha, Subbaian1,2 (AUTHOR) brindha@m2.tuat.ac.jp, Oba, Mami2,3 (AUTHOR) fy7210@go.tuat.ac.jp, Yoshizue, Takahiro1 (AUTHOR) jimoxianguang@gmail.com, Islam, Md. Din1 (AUTHOR) s224333x@st.go.tuat.ac.jp, Islam, M. Monirul4 (AUTHOR) islammm@cu.ac.bd, Takemae, Hitoshi2,3 (AUTHOR) tmizutan@cc.tuat.ac.jp, Mizutani, Tetsuya2,3 (AUTHOR), Kuroda, Yutaka1,2 (AUTHOR) ykuroda@cc.tuat.ac.jp
Publikováno v: Molecules. Jun2024, Vol. 29 Issue 11, p2676. 13p.
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8
Akademický článek
Design and Escherichia coli Expression of a Natively Folded Multi-Disulfide Bonded Influenza H1N1-PR8 Receptor-Binding Domain (RBD).
Autor: Tu, Thao1 (AUTHOR) s224725u@st.go.tuat.ac.jp, Rathnayaka, Tharangani1 (AUTHOR) tharangi15@yahoo.co.jp, Kato, Toshiyo2 (AUTHOR) fq4611@go.tuat.ac.jp, Mizutani, Kenji3 (AUTHOR) mizutani@yokohama-cu.ac.jp, Saotome, Tomonori4 (AUTHOR) t_saotome@vos.nagaokaut.ac.jp, Noguchi, Keiichi2 (AUTHOR) knoguchi@cc.tuat.ac.jp, Kidokoro, Shun-ichi4 (AUTHOR) kidokoro@vos.nagaokaut.ac.jp, Kuroda, Yutaka1 (AUTHOR) ykuroda@cc.tuat.ac.jp
Publikováno v: International Journal of Molecular Sciences. Apr2024, Vol. 25 Issue 7, p3943. 12p.
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9
Akademický článek
Antisera Produced Using an E. coli -Expressed SARS-CoV-2 RBD and Complemented with a Minimal Dose of Mammalian-Cell-Expressed S1 Subunit of the Spike Protein Exhibits Improved Neutralization.
Autor: Yoshizue, Takahiro1 (AUTHOR) s214129v@st.go.tuat.ac.jp, Brindha, Subbaian1,2 (AUTHOR) fy7210@go.tuat.ac.jp, Wongnak, Rawiwan1 (AUTHOR), Takemae, Hitoshi2,3 (AUTHOR) mamioba@go.tuat.ac.jp, Oba, Mami2,3 (AUTHOR) tmizutan@cc.tuat.ac.jp, Mizutani, Tetsuya2,3 (AUTHOR), Kuroda, Yutaka1,2 (AUTHOR) ykuroda@cc.tuat.ac.jp
Publikováno v: International Journal of Molecular Sciences. Jul2023, Vol. 24 Issue 13, p10583. 11p.
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10
Akademický článek
An Escherichia coli Expressed Multi-Disulfide Bonded SARS-CoV-2 RBD Shows Native-like Biophysical Properties and Elicits Neutralizing Antisera in a Mouse Model.
Autor: Brindha, Subbaian1 (AUTHOR), Yoshizue, Takahiro1 (AUTHOR), Wongnak, Rawiwan1 (AUTHOR), Takemae, Hitoshi2 (AUTHOR), Oba, Mami2 (AUTHOR), Mizutani, Tetsuya2 (AUTHOR), Kuroda, Yutaka1 (AUTHOR) ykuroda@cc.tuat.ac.jp
Publikováno v: International Journal of Molecular Sciences. Dec2022, Vol. 23 Issue 24, p15744. 13p.
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