Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Ikuko, OKAZAKI"'
Autor:
Ikuko, Okazaki, Department of Environmental Management, School of International Environmental Management, KIBI International University
Publikováno v:
吉備国際大学研究紀要. 国際環境経営学部 = Journal of Kibi International University, School of International Environmental Management. 20:27-36
Autor:
Ikuko, OKAZAKI, Department of Environmental Risk Management, School of Policy Management, Kibi International University
Publikováno v:
吉備国際大学政策マネジメント学部研究紀要 = Journal of Kibi International University School of Policy Management. 4:1-9
Autor:
Ikuko, Okazaki, Department of Environmental Risk Management, School of Policy Management, Kibi International University
Publikováno v:
吉備国際大学政策マネジメント学部研究紀要 = Journal of Kibi International University School of Policy Management. 3:59-68
Autor:
Shigeyuki Kon, Takashi Fujii, Chiemi Kimura, Junko Morimoto, Nobuo Seki, Nobuchika Yamamoto, Ikuko Okazaki, Fumihiko Sakai, Toshimitsu Uede, Harumi Yamazaki
Publikováno v:
Journal of Clinical Investigation. 112:181-188
It has been shown that osteopontin (OPN) plays a pivotal role in the pathogenesis of rheumatoid arthritis (RA). However, the molecular mechanism of OPN action is yet to be elucidated. Splenic monocytes obtained from arthritic mice exhibited a signifi
Autor:
Motoyoshi Nomizu, Yasuo Kitagawa, Nobuharu Suzuki, Hironobu Yamashita, Norio Nishi, Atsushi Utani, Ikuko Okazaki, Hiroshi Shinkai, Hiroshi Matsuura
Publikováno v:
Journal of Biological Chemistry. 277:37070-37078
Laminins are a family of trimeric extracellular matrix proteins consisting of alpha, beta, and gamma chains. So far five different laminin alpha chains have been identified. The laminin alpha 4 chain, which is present in laminin-8/9, is expressed in
Autor:
Yoko Yamamoto, Shinsaku Nakagawa, Masahiko Sasaki, Haruhiko Kamata, Koichi Kawasaki, Tadanori Mayumi, Mitsuko Maeda, Ikuko Okazaki, Keiko Hojo, Motoyoshi Nomizu, Yuichi Susuki
Publikováno v:
Chemical and Pharmaceutical Bulletin. 50:1229-1232
A bivalent poly(ethylene glycol) or PEG hybrid of fibronectin-related peptides was prepared. An active site peptide (RGD) and its synergistic site peptide (PHSRN) of fibronectin were conjugated with an amino acid-type PEG (aaPEG) to form PHSRN-aaPEG-
Autor:
Yoko Wakabayashi, Kozue Kato, Yuichi Kadoya, Norio Nishi, Masanori Yamada, Taku Sato, Motoyoshi Nomizu, Ikuko Okazaki, Mayumi Mochizuki, Nobuo Sakairi
Publikováno v:
FASEB journal : official publication of the Federation of American Societies for Experimental Biology. 17(8)
Laminin, a major component of the basement membrane, has diverse biological activities. Recently, we identified various biologically active sequences on laminin-1 by using a large set of synthetic peptides. Chitosan, a polysaccharide, is biodegradabl
Autor:
Shingo Kasai, Peter K. Nielsen, Motoyoshi Nomizu, Ikuko Okazaki, Masayoshi Makino, Yoshihiko Yamada, Norio Nishi, Benjamin S. Weeks, Akira Otaka, Maria Bougaeva
Publikováno v:
Experimental cell research. 277(1)
The laminins consist of at least 11 polypeptides (5 alpha-chains, 3 beta-chains, and 3 gamma-chains) specific to basement membranes. Here we investigate the biological activity associated with the G domain of the newly identified laminin alpha5-chain
Autor:
Keiko Hojo, Koichi Kawasaki, Tadanori Mayumi, Shinsaku Nakagawa, Haruhiko Kamada, Yuichi Susuki, Motoyoshi Nomizu, Ikuko Okazaki, Yoko Yamamoto, Mitsuko Maeda
Publikováno v:
Bioorganicmedicinal chemistry letters. 11(11)
Fibronectin contains the active sequence Arg-Gly-Asp (RGD), along with its synergic site Pro-His-Ser-Arg-Asn (PHSRN). However, the PHSRN peptide does not show synergic activity when it is mixed with the RGD peptide, indicating that a spatial array be
Autor:
Motoyoshii Nomizu, Hitoshi Mori, Ikuko Okazaki, Konrad Beck, Hirotake Yamaguchi, Hironobu Yamashita, Yasuo Kitagawa
Publikováno v:
The Journal of biological chemistry. 275(38)
G domains of the mouse laminin alpha 1 and alpha 4 chains consisting of its five subdomains LG1-LG5 were overexpressed in Chinese hamster ovary cells and purified by heparin chromatography. alpha 1LG1-LG5 and alpha 4LG1-LG5 eluted at NaCl concentrati