Zobrazeno 1 - 10
of 59
pro vyhledávání: '"Hideki Yanagi"'
Autor:
Akihiko Kondo, Naotake Okumura, Yoichi Kurokawa, Hideki Fukuda, Jiro Kohda, Hideki Yanagi, Kazuyo Nishihara, Takashi Yura, Yasunori Endo
Publikováno v:
Biochemical Engineering Journal. 10:39-45
Since two classes of folding accessory proteins, molecular chaperones and foldases, prevent the misfolding of newly synthesized polypeptides in the cell, their coexpression could be expected to improve the productivity of soluble and active recombina
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0c957a453c3647ec852708d05b4e8967
https://doi.org/10.1016/s1369-703x(01)00154-1
https://doi.org/10.1016/s1369-703x(01)00154-1
Publikováno v:
Journal of Veterinary Medical Science. 64:177-180
Expression of 150 kda oxygen-regulated protein, ORP150, was examined in the atheromatous lesions on aortic valves in high-fat diet fed mice. Immunohistochemical staining revealed that ORP150 was expressed on the surface of plaque and was co-localized
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a901713ab174f95375961ed3d0764858
https://doi.org/10.1292/jvms.64.177
https://doi.org/10.1292/jvms.64.177
Autor:
Kentaro Ozawa, Tomohiro Kobayashi, David M. Stern, Masaru Okabe, Satoshi Ogawa, Osamu Hori, Yasuko Kitao, Tetsumori Yamashima, Mayuki Miyazaki, Michio Tamatani, Hideki Yanagi, Masahito Ikawa
Publikováno v:
Journal of Clinical Investigation. 108:1439-1450
金沢大学医薬保健研究域医学系
A series of events initiated by glutamate-receptor interaction perturbs cellular homeostasis resulting in elevation of intracellular free calcium and cell death. Cells subject to such environmental chan
A series of events initiated by glutamate-receptor interaction perturbs cellular homeostasis resulting in elevation of intracellular free calcium and cell death. Cells subject to such environmental chan
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6dc358646f98c016e84e84881a05ea37
https://doi.org/10.1172/jci12978
https://doi.org/10.1172/jci12978
Publikováno v:
Journal of Bacteriology. 183:5302-5310
RpoH ( Escherichia coli ς 32 and its homologs) is the central regulator of the heat shock response in gram-negative proteobacteria. Here we studied salient regulatory features of RpoH in Agrobacterium tumefaciens by examining its synthesis, stabilit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7a0d92ee6105d9a67a9a3cbcd6c02d9f
https://doi.org/10.1128/jb.183.18.5302-5310.2001
https://doi.org/10.1128/jb.183.18.5302-5310.2001
Publikováno v:
European Journal of Biochemistry. 268:4664-4673
The chaperonin-containing t-complex polypeptide 1 (CCT) is a cytosolic molecular chaperone composed of eight subunits that assists in the folding of actin, tubulin and other cytosolic proteins. We show here that the content of particular subunits of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::25b09015341df4cd1cdaf08e86982c6c
https://doi.org/10.1046/j.1432-1327.2001.02393.x
https://doi.org/10.1046/j.1432-1327.2001.02393.x
Publikováno v:
Journal of Biological Chemistry. 276:14393-14399
Production of eukaryotic proteins with multiple disulfide bonds in the Escherichia coli periplasm often encounters difficulty in obtaining soluble products with native structure. Human nerve growth factor beta (NGF) contains three disulfide bonds bet
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e8a555972bbcebdf37a307fecd690e11
https://doi.org/10.1074/jbc.m100132200
https://doi.org/10.1074/jbc.m100132200
Autor:
Manabu Taniguchi, David M. Stern, Hiroyuki Nishimura, Yoshitane Tsukamoto, Atsushi Yamaguchi, Satoshi Ogawa, Masaya Tohyama, Tomohiro Matsuyama, Yong Ho Che, Michio Tamatani, Hideki Yanagi, Noriaki Mitsuda, Kentaro Ozawa, Atsuko Yamashita, Masaru Okabe, Osamu Hori
Publikováno v:
Nature Medicine. 7:317-323
Oxygen-regulated protein 150 kD (ORP150) is a novel endoplasmic-reticulum-associated chaperone induced by hypoxia/ischemia. Although ORP150 was sparingly upregulated in neurons from human brain undergoing ischemic stress, there was robust induction i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::02a4d7064544e27c9690970844dc53c2
https://doi.org/10.1038/85463
https://doi.org/10.1038/85463
Autor:
Masashi Kurimoto, Hideki Yanagi, Hiroshi Kubota, Takashi Yura, Tsunetaka Ohta, Tohru Kayano, Shin-ichi Yokota
Publikováno v:
Biochemical and Biophysical Research Communications. 279:712-717
The chaperonin containing t-complex polypeptide 1 (CCT) is a heterooligomeric molecular chaperone that assists in the folding of actin, tubulin, and other cytosolic proteins. We show here that degradation of CCT in mammalian cells is inhibited by a p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::42d7242cdd0d5397af021387e4045234
https://doi.org/10.1006/bbrc.2000.4011
https://doi.org/10.1006/bbrc.2000.4011
Publikováno v:
Journal of Biochemistry. 128:529-538
150 kDa oxygen-regulated protein (ORP150) is one of the endoplasmic reticulum (ER)-resident stress proteins. We have cloned and sequenced the entire human ORP150 gene covering over 15-kb. Analyses of transcription initiation sites and transcriptional
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::459342117bbd7dd48a7cb017127b2298
https://doi.org/10.1093/oxfordjournals.jbchem.a022783
https://doi.org/10.1093/oxfordjournals.jbchem.a022783
Autor:
Osamu Hori, Yoshio Bando, Masaya Tohyama, Kentaro Ozawa, Michio Tamatani, Hideki Yanagi, Satoshi Ogawa, Keisuke Kuwabara, Atsushi Yamauchi
Publikováno v:
American Journal of Physiology-Cell Physiology. 278:C1172-C1182
To assess the participation of the 150-kDa oxygen-regulated protein (ORP150) in protein transport, its function in Madin-Darby canine kidney (MDCK) cells was studied. Exposure of MDCK cells to hypoxia resulted in an increase of ORP150 antigen and inc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::09f64a537dc1240ddfd55733e79eedcf
https://doi.org/10.1152/ajpcell.2000.278.6.c1172
https://doi.org/10.1152/ajpcell.2000.278.6.c1172