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of 6
pro vyhledávání: '"Tomoki Shiratori"'
Autor:
Takahiro Kasai, Takashi Wada, Tsubasa Iijima, Yoshiko Minami, Tomoyo Sakaguchi, Ryotaro Koga, Tomoki Shiratori, Yuta Otsuka, Yohsuke Shimada, Yukiko Okayama, Satoru Goto
Publikováno v:
BBA Advances, Vol 2, Iss , Pp 100036- (2022)
Amyloid fibrillation is provoked by the conformational rearrangement of its source. In our previous study, we claimed that the conformational rearrangement of hen egg white lysozyme requires intermolecular aggregation/packing induced. Our proposed ca
Externí odkaz:
https://doaj.org/article/9621626ab6ac4705b0095199980e6f01
Autor:
Tomoki Shiratori, Satoru Goto, Tomoyo Sakaguchi, Takahiro Kasai, Yuta Otsuka, Kyohei Higashi, Kosho Makino, Hideyo Takahashi, Kazushi Komatsu
Publikováno v:
Biochemistry and Biophysics Reports, Vol 28, Iss , Pp 101153- (2021)
Amyloid fibril formation occurs in restricted environment, such as the interface between intercellular fluids and bio-membranes. Conformational interconversion from α-helix to β-structure does not progress in fluids; however, it can occur after sed
Externí odkaz:
https://doaj.org/article/2d5b84231758438e87537b0bea2bcb01
Autor:
Takahiro Kasai, Takashi Wada, Tsubasa Iijima, Yoshiko Minami, Tomoyo Sakaguchi, Ryotaro Koga, Tomoki Shiratori, Yuta Otsuka, Yohsuke Shimada, Yukiko Okayama, Satoru Goto
Publikováno v:
BBA Adv
BBA Advances, Vol 2, Iss, Pp 100036-(2022)
BBA Advances, Vol 2, Iss, Pp 100036-(2022)
Amyloid fibrillation is provoked by the conformational rearrangement of its source. In our previous study, we claimed that the conformational rearrangement of hen egg white lysozyme requires intermolecular aggregation/packing induced. Our proposed ca
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::50645a59099387c81bcc80e71105ca57
https://europepmc.org/articles/PMC10074904/
https://europepmc.org/articles/PMC10074904/
Autor:
Yuta Otsuka, Kazushi Komatsu, Hideyo Takahashi, Takahiro Kasai, Kosho Makino, Tomoyo Sakaguchi, Tomoki Shiratori, Kyohei Higashi, Satoru Goto
Publikováno v:
Biochemistry and Biophysics Reports
Biochemistry and Biophysics Reports, Vol 28, Iss, Pp 101153-(2021)
Biochemistry and Biophysics Reports, Vol 28, Iss, Pp 101153-(2021)
Amyloid fibril formation occurs in restricted environment, such as the interface between intercellular fluids and bio-membranes. Conformational interconversion from α-helix to β-structure does not progress in fluids; however, it can occur after sed
Autor:
Yuta Otsuka, Takahiro Kasai, Takashi Wada, Kazushi Komatsu, Yoshiko Minami, Tomoyo Sakaguchi, Satoru Goto, Tomoki Shiratori, Yohsuke Shimada
Publikováno v:
Colloids and surfaces. B, Biointerfaces. 190
In this study, the combined effects of pH and salt concentration on the aggregation and amyloid formation of a charge-bearing protein (hen egg white lysozyme, HEWL) were investigated, as well as the inhibition of amyloid formation by using dithiothre
Conference
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