Zobrazeno 1 - 10
of 118
pro vyhledávání: '"Masamichi Ikeguchi"'
Autor:
Masamichi Ikeguchi
Publikováno v:
Biomolecules, Vol 4, Iss 1, Pp 202-216 (2014)
In ideal proteins, only native interactions are stabilized step-by-step in a smooth funnel-like energy landscape. In real proteins, however, the transient formation of non-native structures is frequently observed. In this review, the transient format
Externí odkaz:
https://doaj.org/article/fef7f674fdf047c39db65ffa8f8cac51
Autor:
Takumi Kuwata, Daisuke Sato, Yuki Yanagida, Eriko Aoki, Kazuo Fujiwara, Hideyuki Yoshimura, Masamichi Ikeguchi
Publikováno v:
JBIC Journal of Biological Inorganic Chemistry. 27:583-594
The iron core of Escherichia coli ferritin was reconstituted in the presence and absence of phosphate. The core formed in the presence of phosphate contained phosphate in amounts comparable to the iron content. The size distribution of the core was a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c49ace353be64dbc05c0ae014fa2bb90
https://doi.org/10.1007/s00775-022-01952-5
https://doi.org/10.1007/s00775-022-01952-5
Autor:
Masamichi Ikeguchi, Eriko Aoki
Publikováno v:
Biophysical Reviews. 11:303-309
Haemophilus influenzae adhesin (Hia) belongs to the trimeric autotransporter family, and it mediates the adherence of these bacteria to the epithelial cells of host organisms. Hia is composed of the passenger domain, which is a virulence factor, and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::44c36d8925e277be16d785df2510a267
https://doi.org/10.1007/s12551-019-00535-0
https://doi.org/10.1007/s12551-019-00535-0
Autor:
Daisuke Sato, Masamichi Ikeguchi
Publikováno v:
Biophysical Reviews. 11:449-455
The assembly reaction of Escherichia coli ferritin A (EcFtnA) was studied using time-resolved small-angle X-ray scattering (SAXS). EcFtnA forms a cage-like structure that consists of 24 identical subunits and dissociates into dimers at acidic pH. The
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f0362a6dd7f21f6bca5ff300eb718d44
https://doi.org/10.1007/s12551-019-00538-x
https://doi.org/10.1007/s12551-019-00538-x
Autor:
Yuta Okada, Kazuo Fujiwara, Takuma Fukumura, Masamichi Ikeguchi, Daisuke Sato, Takumi Kuwata, Tomoki Yamamoto
Publikováno v:
Biochemistry. 58:2318-2325
Neuroferritinopathy is a rare, adult-onset, dominantly inherited movement disorder caused by mutations in the ferritin gene. A ferritin light-chain variant related to neuroferritinopathy, in which alanine 96 is replaced with threonine (A96T), was exp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0c1570ac3f62fff86121f044e7743c5c
https://doi.org/10.1021/acs.biochem.8b01068
https://doi.org/10.1021/acs.biochem.8b01068
Publikováno v:
Protein Expression and Purification. 145:19-24
To obtain a high yield of the transmembrane domain of Haemophilus influenzae adhesin (HiaTD) in Escherichia coli, we attempted to express the HiaTD with and without a signal sequence using a T7 expression system. The expression level of HiaTD after i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5bbbe44f95415e53936dbd8edd240fa0
https://doi.org/10.1016/j.pep.2017.12.009
https://doi.org/10.1016/j.pep.2017.12.009
Publikováno v:
Biochemistry. 56:2139-2148
Haemophilus influenzae adhesin (Hia) belongs to the trimeric autotransporter family and mediates the adherence of these bacteria to the epithelial cells of host organisms. Hia contains a passenger and a transmembrane domain. The transmembrane domain
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7681b31510718d268281dd67228a60ce
https://doi.org/10.1021/acs.biochem.6b01130
https://doi.org/10.1021/acs.biochem.6b01130
Autor:
Hideaki Ohtomo, Atsushi Kurobe, Daisuke Sato, Masamichi Ikeguchi, Kazuo Fujiwara, Yoshiteru Yamada, Takaaki Hikima
Publikováno v:
Biochemistry. 55:287-293
The assembly reaction of Escherichia coli ferritin A (EcFtnA) was studied using time-resolved small-angle X-ray scattering (TR-SAXS). EcFtnA forms a cagelike structure that consists of 24 identical subunits and dissociates into dimers at acidic pH. T
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5647667c4b467a2d6275140cfcc8bbbe
https://doi.org/10.1021/acs.biochem.5b01152
https://doi.org/10.1021/acs.biochem.5b01152
Autor:
Masamichi Ikeguchi, Ayumi Sunato, Kazuo Fujiwara, Atsushi Kurobe, Mio Ohtomo, Hiroshi Kihara, Hideaki Ohtomo, Daisuke Sato, Yoshitaka Matsumura
Publikováno v:
Biochemistry. 54:6243-6251
Ferritin A from Escherichia coli (EcFtnA) is 24-meric protein, which forms spherical cagelike structures called nanocages. The nanocage structure is stabilized by the interface around 4-, 3-, and 2-fold symmetric axes. The subunit structure of EcFtnA
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dc977991a7310a0a7109a6aa51fc7f9d
https://doi.org/10.1021/acs.biochem.5b00723
https://doi.org/10.1021/acs.biochem.5b00723
Publikováno v:
Biochemistry. 53:3858-3866
Many studies have shown that during the early stages of the folding of a protein, chain collapse and secondary structure formation lead to a partially folded intermediate. Thus, direct observation of these early folding events is crucial if we are to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a22e1270cd15137ee1ad811286fbeaf5
https://doi.org/10.1021/bi5003647
https://doi.org/10.1021/bi5003647