Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Yuhei Tokunaga"'
Autor:
Toshifumi Imagawa, Masahiko Ito, Mami Matsuda, Kenji Nakashima, Yuhei Tokunaga, Isao Ohta, Tian-Cheng Li, Ryosuke Suzuki, Tetsuro Suzuki
Publikováno v:
Scientific Reports, Vol 11, Iss 1, Pp 1-10 (2021)
Abstract The global incidence of dengue, which is caused by dengue virus (DENV) infection, has grown dramatically in recent decades and secondary infection with heterologous serotype of the virus may cause severe symptoms. Efficacious dengue vaccines
Externí odkaz:
https://doaj.org/article/0567ac1e974b4525bd4bf3c91772a513
Autor:
Makoto Ogata, Takashi Onoda, Ami Koizumi, Yuhei Tokunaga, Isao Ohta, Souichi Nukuzuma, Enoch Y. Park, Taichi Usui, Tetsuro Suzuki
Publikováno v:
ACS Omega, Vol 5, Iss 34, Pp 21940-21947 (2020)
Externí odkaz:
https://doaj.org/article/2d815a4a13324a1885ffb8e758338e82
Autor:
Ami Koizumi, Souichi Nukuzuma, Takashi Onoda, Isao Ohta, Makoto Ogata, Taichi Usui, Tetsuro Suzuki, Yuhei Tokunaga, Enoch Y. Park
Publikováno v:
ACS Omega, Vol 5, Iss 34, Pp 21940-21947 (2020)
ACS Omega
ACS Omega
Two kinds of tetravalent double-headed sialo-glycosides with short/long spacers between the Neu5Acα2,6Galβ1,4GlcNAc unit and ethylene glycol tetraacetic acid (EGTA) scaffold were found to be capable of binding to virus-like particles of Merkel cell
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::14d22f5e15610b7f1a66cfd5d252bdd6
https://doi.org/10.1021/acsomega.0c03269
https://doi.org/10.1021/acsomega.0c03269
Autor:
Kenji Nakashima, Tetsuro Suzuki, Mami Matsuda, Masahiko Ito, Tian-Cheng Li, Yuhei Tokunaga, Ryosuke O. Suzuki, Toshifumi Imagawa, Isao Ohta
Publikováno v:
Scientific Reports, Vol 11, Iss 1, Pp 1-10 (2021)
Scientific Reports
Scientific Reports
The global incidence of dengue, which is caused by dengue virus (DENV) infection, has grown dramatically in recent decades and secondary infection with heterologous serotype of the virus may cause severe symptoms. Efficacious dengue vaccines should b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f0e132d382f38463a22796490ceea56e
https://doi.org/10.1038/s41598-021-97038-4
https://doi.org/10.1038/s41598-021-97038-4
Publikováno v:
Protein expression and purification. 156
Insoluble expression of intrinsically soluble proteins with native activity is potentially a promising alternative to soluble expression of folded protein or insoluble expression of unfolded protein requiring refolding. Here, we attempted to express
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::516362b5cc27ec5b1884bd506584da27
https://pubmed.ncbi.nlm.nih.gov/30615940
https://pubmed.ncbi.nlm.nih.gov/30615940
Publikováno v:
Protein Science. 22:1582-1591
Halophilic proteins are characterized by high net negative charges and relatively small fraction of hydrophobic amino acids, rendering them aggregation resistant. These properties are also shared by histidine-rich metal binding protein (HP) from mode
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::056074560e50e828bac31f67fd2d4e7d
https://doi.org/10.1002/pro.2359
https://doi.org/10.1002/pro.2359
Publikováno v:
International journal of biological macromolecules. 80
Hen egg white lysozyme (HEWL) readily forms amyloid fibrils in vitro . We have previously identified a core structure, termed HEWL K-peptide, involved in fibril formation. Two major peptides, peptide #3 (50th–102nd residues of human lysozyme (hLZ))
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d7381b586b9d69d701d472c28aa56416
https://pubmed.ncbi.nlm.nih.gov/26092172
https://pubmed.ncbi.nlm.nih.gov/26092172
Publikováno v:
International Journal of Biological Sciences
Some of the lysozyme mutants in humans cause systemic amyloidosis. Hen egg white lysozyme (HEWL) has been well studied as a model protein of amyloid fibrils formation. We previously identified an amyloid core region consisting of nine amino acids (de
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::98c8f407fddebc54ab97275a78d7d6dd
https://pubmed.ncbi.nlm.nih.gov/23459392
https://pubmed.ncbi.nlm.nih.gov/23459392
Autor:
Yasushi Sugimoto, Tadashi Ueda, Yoshiki Kamada, Mitsuharu Matsumoto, Takahiro Kusakabe, Hiroshi Shinohara, Yuhei Tokunaga, Takatoshi Ohkuri
Publikováno v:
Biochemistry and cell biology = Biochimie et biologie cellulaire. 89(6)
The interaction of egg-white lysozyme with N-ovalbumin, the native form of egg-white ovalbumin with the denaturation temperature, Tm, of 78 °C, was investigated by the inhibition of lysozyme muramidase activity, differential scanning calorimetry, an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::edfb079866d7c6dc432c40d0c5396bcd
https://pubmed.ncbi.nlm.nih.gov/22004604
https://pubmed.ncbi.nlm.nih.gov/22004604