Zobrazeno 1 - 10 of 15 pro vyhledávání: '"Subbaian Brindha"'
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
Zobrazit plný text záznamu
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
Zobrazit plný text záznamu
3
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
Zobrazit plný text záznamu
4
Blocking PSD95‐PDZ3's amyloidogenesis through point mutations that inhibit high‐temperature reversible oligomerization (RO)
Autor: Tomonori Saotome, Sawaros Onchaiya, Subbaian Brindha, Taichi Mezaki, Satoru Unzai, Keiichi Noguchi, Jose C. Martinez, Shun‐ichi Kidokoro, Yutaka Kuroda
Publikováno v: The FEBS Journal. 289:3205-3216
The third PDZ domain of the postsynaptic density protein 95 (PSD95-PDZ3; 11 kDa, 103 residues) has a propensity to form amyloid fibrils at high temperatures. At neutral pH, PDZ3 is natively folded, but it exhibits a peculiar three-state thermal unfol
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a1df6769e87f0df593aa867e72b7e838
https://doi.org/10.1111/febs.16339
Zobrazit plný text záznamu
5
The biophysical nature and not only the size of protein aggregates determines the strength of the immune response against dengue ED3
Autor: Md. Golam Kibria, Yukari Shiwaku, Subbaian Brindha, Yutaka Kuroda
Here we used domain 3 of dengue virus serotype 3 envelope protein (D3ED3), a natively folded globular low-immunogenicity protein, to ask whether the biophysical nature of amorphous aggregates can affect immunogenicity. We prepared amorphous oligomers
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::624fb77efdd012b06faab57e57a42929
https://doi.org/10.1101/2022.11.02.514810
Zobrazit plný text záznamu
7
Thermodynamic Analysis of Point Mutations Inhibiting High-Temperature Reversible Oligomerization of PDZ3
Autor: Jose C. Martinez, Tomonori Saotome, Yutaka Kuroda, Shun-ichi Kidokoro, Satoru Unzai, Subbaian Brindha, Taichi Mezaki
Publikováno v: Biophys J
Differential scanning calorimetry (DSC) indicated that PDZ3 undergoes a peculiar thermal denaturation, exhibiting two endothermic peaks because of the formation of reversible oligomers at high temperature (N↔I(6)↔D). This contrasts sharply with t
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::565515de4e910e8f8352ef1cba9a1449
https://doi.org/10.1016/j.bpj.2020.08.023
Zobrazit plný text záznamu
8
A Multi-Disulfide Receptor-Binding Domain (RBD) of the SARS-CoV-2 Spike Protein Expressed in E. coli Using a SEP-Tag Produces Antisera Interacting with the Mammalian Cell Expressed Spike (S1) Protein
Autor: Subbaian Brindha, Yutaka Kuroda
Publikováno v: International Journal of Molecular Sciences; Volume 23; Issue 3; Pages: 1703
International Journal of Molecular Sciences, Vol 23, Iss 1703, p 1703 (2022)
An Escherichia coli (E. coli) production of the receptor-binding domain (RBD) of the SARS-CoV-2 (isolate Wuhan-Hu-1) spike protein would significantly accelerate the search for anti-COVID-19 therapeutics because of its versatility and low cost. Howev
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::be4e1b9eb767d3602957f44c6d1aff6e
Zobrazit plný text záznamu
9
The Immunogenicity of DENV1–4 ED3s Strongly Differ despite Their Almost Identical Three-Dimensional Structures and High Sequence Similarities
Autor: Md. Din Islam, Tahmina Sharmin, Imrul Hasan Tipo, Antara Saha, Sanjida Yesmin, Moushumi Ghosh Roy, Subbaian Brindha, Yutaka Kuroda, M. Monirul Islam
Publikováno v: International Journal of Molecular Sciences
Volume 24
Issue 3
Pages: 2393
The development of a dengue (DENV) vaccine remains challenging due to the heteroserotypic infection, which can result in a potentially deadly hemorrhagic fever or dengue shock syndrome, and only a tetravalent vaccine can overcome this issue. Here, we
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ac6a1bf880c8bfbb874973530744b644
https://doi.org/10.3390/ijms24032393
Zobrazit plný text záznamu
10
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; Volume 23; Issue 24; Pages: 15744
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://explore.openaire.eu/search/publication?articleId=doi_dedup___::2bba6b2e7319178db6361de5d753cea5
https://doi.org/10.3390/ijms232415744
Zobrazit plný text záznamu

Vyhledávací nástroje:

Upřesnit hledání

Omezení vyhledávání
Plný text Recenzováno Digitální knihovna AV ČR
Zdroje