Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Shiho Mikawa"'
Autor:
Hitoshi Kimura, Shiho Mikawa, Chiharu Mizuguchi, Yuki Horie, Izumi Morita, Hiroyuki Oyama, Takashi Ohgita, Kazuchika Nishitsuji, Atsuko Takeuchi, Sissel Lund-Katz, Kenichi Akaji, Norihiro Kobayashi, Hiroyuki Saito
Publikováno v:
Scientific Reports, Vol 7, Iss 1, Pp 1-11 (2017)
Abstract Apolipoprotein A-I (apoA-I) undergoes a large conformational reorganization during remodeling of high-density lipoprotein (HDL) particles. To detect structural transition of apoA-I upon HDL formation, we developed novel monoclonal antibodies
Externí odkaz:
https://doaj.org/article/cd93be0f7d85464f8c4243caf236703f
Autor:
Kazuchika Nishitsuji, Yuki Horie, Sissel Lund-Katz, Chiharu Mizuguchi, Hiroyuki Oyama, Norihiro Kobayashi, Kenichi Akaji, Shiho Mikawa, Hitoshi Kimura, Izumi Morita, Atsuko Takeuchi, Takashi Ohgita, Hiroyuki Saito
Publikováno v:
Scientific Reports, Vol 7, Iss 1, Pp 1-11 (2017)
Scientific Reports
Scientific Reports
Apolipoprotein A-I (apoA-I) undergoes a large conformational reorganization during remodeling of high-density lipoprotein (HDL) particles. To detect structural transition of apoA-I upon HDL formation, we developed novel monoclonal antibodies (mAbs).
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cd2be393f36c26c409e8980212dc64b5
https://doaj.org/article/cd93be0f7d85464f8c4243caf236703f
https://doaj.org/article/cd93be0f7d85464f8c4243caf236703f
Autor:
Akira Shigenaga, Hiroyuki Saito, Naomi Sakashita, Shiho Mikawa, Teruhiko Baba, Kazuchika Nishitsuji, Akira Otaka, Kenichi Akaji, Chiharu Mizuguchi, Toshinori Shimanouchi
Publikováno v:
FEBS Letters. 590:3492-3500
Glycosaminoglycans are known to be associated with extracellular amyloid deposits of various amyloidogenic proteins. In this study, we found that the glycosaminoglycan heparin greatly accelerates the elongation step in fibril formation by the N-termi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6eb7368d64b9bec124af78039d1e73e6
https://doi.org/10.1002/1873-3468.12426
https://doi.org/10.1002/1873-3468.12426
Autor:
Norihiro Kobayashi, Kaori Kuwabara, Yoshiki Kashiwada, Hiroyuki Nakajima, Hiroyuki Saito, Shiho Mikawa, Kazuchika Nishitsuji, Kenji Uchimura, Naomi Sakashita, Hiroyuki Kawashima, Kenichi Akaji
Publikováno v:
Amyloid. 23:17-25
Apolipoprotein A-I (apoA-I) amyloidosis is either a non-hereditary form with deposits of wild-type apoA-I proteins in atherosclerotic plaques or a hereditary form with progressive accumulation of mutant apoA-I proteins in different tissues. Several s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::07c46fe7257cc606c297bd7268acc410
https://doi.org/10.3109/13506129.2015.1113167
https://doi.org/10.3109/13506129.2015.1113167
Autor:
Shiho Mikawa, Shang-Cheng Hung, Kenji Uchimura, Hiroyuki Nakajima, Naomi Sakashita, Norihiro Kobayashi, Hiroyuki Saito, Kaori Kuwabara, Kazuchika Nishitsuji, Makoto Mizuguchi
Publikováno v:
Journal of Biological Chemistry. 290:24210-24221
The single amino acid mutation G26R in human apolipoprotein A-I (apoA-I) is associated with familial amyloid polyneuropathy III. ApoA-I carrying this mutation (apoA-IIowa) forms amyloid fibrils in vitro. Heparan sulfate (HS) is a glycosaminoglycan th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5368b958ef6c19d872f9ee0822ee9912
https://doi.org/10.1074/jbc.m115.652545
https://doi.org/10.1074/jbc.m115.652545
Autor:
Akira Shigenaga, Keiichiro Okuhira, Fuka Ogata, Hiroyuki Saito, Akira Otaka, Kohei Tsuji, Toshinori Shimanouchi, Chiharu Mizuguchi, Shiho Mikawa, Teruhiko Baba
Publikováno v:
Journal of Biological Chemistry. 290:20947-20959
The N-terminal amino acid 1-83 fragment of apolipoprotein A-I (apoA-I) has a strong propensity to form amyloid fibrils at physiological neutral pH. Because apoA-I has an ability to bind to lipid membranes, we examined the effects of the lipid environ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e78950f082b642e2d4a30b5950c19036
https://doi.org/10.1074/jbc.m115.664227
https://doi.org/10.1074/jbc.m115.664227
Autor:
Hiroyuki Saito, Hirokazu Kameyama, Kazuchika Nishitsuji, Norihiro Kobayashi, Shiho Mikawa, Naomi Sakashita, Kenji Uchimura, Keiichiro Okuhira, Hiroyuki Nakajima
Publikováno v:
Scientific Reports
Scientific Reports, Nature Publishing Group, 2016, 6, pp.30391. ⟨10.1038/srep30391⟩
Scientific Reports, 2016, 6, pp.30391. ⟨10.1038/srep30391⟩
Scientific Reports, Nature Publishing Group, 2016, 6, pp.30391. ⟨10.1038/srep30391⟩
Scientific Reports, 2016, 6, pp.30391. ⟨10.1038/srep30391⟩
The single amino acid mutation G26R in human apolipoprotein A-I (apoA-IIowa) is the first mutation that was associated with familial AApoA1 amyloidosis. The N-terminal fragments (amino acid residues 1–83) of apoA-I containing this mutation deposit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6d641babe5eac51f4b422526819c2167
https://hal.univ-lille.fr/hal-03180614/document
https://hal.univ-lille.fr/hal-03180614/document
Autor:
Chiharu Mizuguchi1, Fuka Ogata1, Shiho Mikawa1, Kohei Tsuji1, Teruhiko Baba2, Akira Shigenaga1, Toshinori Shimanouchi3, Keiichiro Okuhira1, Akira Otaka1, Hiroyuki Saito1 hsaito@tokushima-u.ac.jp
Publikováno v:
Journal of Biological Chemistry. 8/21/2015, Vol. 290 Issue 34, p20947-20959. 13p.