Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Hideyuki Ogino"'
Autor:
Noriyasu Kamei, Hideyuki Tamiwa, Mari Miyata, Yuta Haruna, Koyo Matsumura, Hideyuki Ogino, Serena Hirano, Kazuhiro Higashiyama, Mariko Takeda-Morishita
Publikováno v:
Pharmaceutics, Vol 10, Iss 4, p 182 (2018)
Cell-penetrating peptides (CPPs) have great potential to efficiently deliver drug cargos across cell membranes without cytotoxicity. Cationic arginine and hydrophobic tryptophan have been reported to be key component amino acids for cellular internal
Externí odkaz:
https://doaj.org/article/3e5feeda333b4110a6ceffaa4bd25950
Autor:
Haruka Okumura, Masahiro Kato, Serena Hirano, Yui Fujiwara, Kenji Arime, Teruyo Yuasa, Anna Nonomura, Mariko Takeda-Morishita, Sayaka Sugano, Noriyasu Kamei, Hideyuki Ogino, El-Sayed Khafagy
Publikováno v:
Journal of Controlled Release. 319:397-406
Leptin is an endogenous hormone that regulates the appetite, energy metabolism, and glucose intake in the central nervous system (CNS) and is a potential therapeutic agent for obesity. In the normal healthy condition, peripherally secreted leptin is
Autor:
Hideyuki Tamiwa, Hideyuki Ogino, Mariko Takeda-Morishita, Noriyasu Kamei, Serena Hirano, Rio Abe, Satoshi Kawano
Publikováno v:
European journal of pharmaceutics and biopharmaceutics : official journal of Arbeitsgemeinschaft fur Pharmazeutische Verfahrenstechnik e.V. 155
We previously reported that oral and intestinal absorption of insulin in rats and mice is significantly enhanced in vivo by coadministration with cell-penetrating peptides (CPPs). To evaluate the clinical use of CPPs as absorption enhancers, it is im
Autor:
Yuta Haruna, Kazuhiro Higashiyama, Mariko Takeda-Morishita, Hideyuki Tamiwa, Serena Hirano, Koyo Matsumura, Mari Miyata, Noriyasu Kamei, Hideyuki Ogino
Publikováno v:
Pharmaceutics, Vol 10, Iss 4, p 182 (2018)
Pharmaceutics
Volume 10
Issue 4
Pharmaceutics
Volume 10
Issue 4
Cell-penetrating peptides (CPPs) have great potential to efficiently deliver drug cargos across cell membranes without cytotoxicity. Cationic arginine and hydrophobic tryptophan have been reported to be key component amino acids for cellular internal