Zobrazeno 1 - 10
of 136
pro vyhledávání: '"Shun‐ichi Kidokoro"'
Autor:
Thao Tu, Tharangani Rathnayaka, Toshiyo Kato, Kenji Mizutani, Tomonori Saotome, Keiichi Noguchi, Shun-ichi Kidokoro, Yutaka Kuroda
Publikováno v:
International Journal of Molecular Sciences, Vol 25, Iss 7, p 3943 (2024)
Refolding multi-disulfide bonded proteins expressed in E. coli into their native structure is challenging. Nevertheless, because of its cost-effectiveness, handiness, and versatility, the E. coli expression of viral envelope proteins, such as the RBD
Externí odkaz:
https://doaj.org/article/3d6fdab8b22c4140a27227cd9a1d5c54
Autor:
Sawaros Onchaiya, Tomonori Saotome, Kenji Mizutani, Jose C. Martinez, Jeremy R. H. Tame, Shun-ichi Kidokoro, Yutaka Kuroda
Publikováno v:
Molecules, Vol 27, Iss 9, p 2813 (2022)
PSD95-PDZ3, the third PDZ domain of the post-synaptic density-95 protein (MW 11 kDa), undergoes a peculiar three-state thermal denaturation (N ↔ In ↔ D) and is amyloidogenic. PSD95-PDZ3 in the intermediate state (I) is reversibly oligomerized (RO
Externí odkaz:
https://doaj.org/article/f72d3a7b048d47d8b2bf5bcaaa958c38
Autor:
Kodai Fujiwara, Michiko Ryuzaki, Masaru Yamanaka, Tsuyoshi Mashima, Tomonori Saotome, Shun-ichi Kidokoro, Shun Hirota
Publikováno v:
Chemistry Letters; Aug2024, Vol. 53 Issue 8, p1-4, 4p
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
https://doi.org/10.1111/febs.16339
Autor:
Shun-ichi Kidokoro
Publikováno v:
Seibutsu Butsuri. 61:370-373
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::29b4d94e0e29d2511582b8f01dc9a380
https://doi.org/10.2142/biophys.61.370
https://doi.org/10.2142/biophys.61.370
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
https://doi.org/10.1016/j.bpj.2020.08.023
Autor:
null Tomonori Saotome, null Sawaros Onchaiya, null Brindha Subbaian, null Taichi Mezaki, null Satoru Unzai, null Keiichi Noguchi, null Jose C. Martinez, null Shun‐ichi Kidokoro, null Yutaka Kuroda
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::82d7c45d26162686eac7b594102e19c1
https://doi.org/10.1111/febs.16339/v2/response1
https://doi.org/10.1111/febs.16339/v2/response1
Publikováno v:
Journal of Thermal Analysis and Calorimetry. 135:2625-2628
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a68a44578a730518963f5f66c32c75de
https://doi.org/10.1007/s10973-018-7987-z
https://doi.org/10.1007/s10973-018-7987-z
Publikováno v:
Biochemistry. 59(39)
Protein amorphous aggregation has become the focus of great attention, as it can impair the ability of cells to function properly. Here, we evaluated the effects of three peptide tags, consisting of one, three, and five consecutive isoleucines attach
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d9811aad9cfb0d7cbfea6ebda45b300a
https://pubmed.ncbi.nlm.nih.gov/32924442
https://pubmed.ncbi.nlm.nih.gov/32924442
Autor:
Satoru Unzai, T. Mezaki, Tomonori Saotome, B. Subbaian, Yutaka Kuroda, Shun-ichi Kidokoro, Jose C. Martinez
Differential scanning calorimetry (DSC) indicated that PDZ3 undergoes a peculiar thermal denaturation exhibiting two endothermic peaks due to the formation of reversible oligomers at high temperature (N↔I6↔D). This contrasts sharply with the stan
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::299a9786d77a5cff637f9b4b439f1a8d
https://doi.org/10.1101/2020.06.24.169607
https://doi.org/10.1101/2020.06.24.169607