Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Hiroyuki Wadahama"'
Autor:
Keito Nishizawa, Masao Ishimoto, Kensuke Iwasaki, Fumio Arisaka, Reiko Urade, Kyoko Takagi, Hiroyuki Wadahama, Motonori Matsusaki
Publikováno v:
Plant Physiology. 158:1395-1405
β-Conglycinin, one of the major soybean (Glycine max) seed storage proteins, is folded and assembled into trimers in the endoplasmic reticulum and accumulated into protein storage vacuoles. Prior experiments have used soybean β-conglycinin extracte
Autor:
Reiko Urade, Kensuke Iwasaki, Hiroyuki Wadahama, Masao Ishimoto, Teruo Kawada, Shinya Kamauchi
Publikováno v:
FEBS Journal. 276:4130-4141
Protein disulfide isomerase (PDI) and other PDI family proteins are members of the thioredoxin superfamily and are thought to play important roles in disulfide bond formation and isomerization in the endoplasmic reticulum (ER). The exact functions of
Autor:
Reiko Urade, Shinya Kamauchi, Keito Nishizawa, Masao Ishimoto, Kensuke Iwasaki, Hiroyuki Wadahama, Yumi Nakamoto, Teruo Kawada
Publikováno v:
FEBS Journal. 275:2644-2658
Protein disulfide isomerase family proteins play important roles in the folding of nascent polypeptides and the formation of disulfide bonds in the endoplasmic reticulum. In this study, we cloned two similar protein disulfide isomerase family genes f
Autor:
Hiroyuki Wadahama, Shinya Kamauchi, Teruo Kawada, Yumi Nakamoto, Masao Ishimoto, Keito Nishizawa, Reiko Urade
Publikováno v:
FEBS Journal. 275:399-410
The protein disulfide isomerase is known to play important roles in the folding of nascent polypeptides and in the formation of disulfide bonds in the endoplasmic reticulum (ER). In this study, we cloned a gene of a novel protein disulfide isomerase
Publikováno v:
FEBS Journal. 274:687-703
Protein disulfide isomerase family proteins are known to play important roles in the folding of nascent polypeptides and the formation of disulfide bonds in the endoplasmic reticulum. In this study, we cloned two similar protein disulfide isomerase f
Autor:
Reiko Urade, Motohiko Hirotsuka, Tatsuya Moriyama, Hiroyuki Wadahama, Mitsutaka Kohno, Yuko Mochizuki, Teruo Kawada, Motohiro Maebuchi
Publikováno v:
Journal of agricultural and food chemistry. 57(4)
In this study, HepG2 cells were treated with short peptides (7S-peptides) derived from highly purified soybean beta-conglycinin (7S), which was free from lipophilic protein, and the effect of the peptide treatment on lipid metabolism was determined.
Autor:
Shinya, Kamauchi, Hiroyuki, Wadahama, Kensuke, Iwasaki, Yumi, Nakamoto, Keito, Nishizawa, Masao, Ishimoto, Teruo, Kawada, Reiko, Urade
Publikováno v:
The FEBS journal. 275(10)
Protein disulfide isomerase family proteins play important roles in the folding of nascent polypeptides and the formation of disulfide bonds in the endoplasmic reticulum. In this study, we cloned two similar protein disulfide isomerase family genes f
Autor:
Hiroyuki, Wadahama, Shinya, Kamauchi, Yumi, Nakamoto, Keito, Nishizawa, Masao, Ishimoto, Teruo, Kawada, Reiko, Urade
Publikováno v:
The FEBS journal. 275(3)
The protein disulfide isomerase is known to play important roles in the folding of nascent polypeptides and in the formation of disulfide bonds in the endoplasmic reticulum (ER). In this study, we cloned a gene of a novel protein disulfide isomerase
Publikováno v:
The FEBS journal. 274(3)
Protein disulfide isomerase family proteins are known to play important roles in the folding of nascent polypeptides and the formation of disulfide bonds in the endoplasmic reticulum. In this study, we cloned two similar protein disulfide isomerase f