Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Mitsushi Tsujimura"'
Autor:
Yukiko Inoue, Seizaburo Kashiwagi, Atae Utsunomiya, Eijiro Kojima, Mitsushi Tsujimura, Hiroshi Shiraki, Koichi Ohshima, Yasuko Sagara
Publikováno v:
Cancer Science. 98:240-245
Human T-cell lymphotropic virus type 1 (HTLV-1) is an etiologic agent of adult T-cell leukemia/lymphoma (ATL). HTLV-1 is spread by cell-to-cell transmission via the gp46-197 region, Asp197 to Leu216, on the envelope protein gp46. In the present study
Autor:
Hiroshi Shiraki, Eijiro Kojima, Mitsushi Tsujimura, Yukiko Inoue, Seizaburo Kashiwagi, Yasuko Sagara
Publikováno v:
Cancer Science. 95:835-839
We previously showed that 71-kDa heat shock cognate protein (HSC70) functions as a cellular receptor for gp46 protein via the gp46-197 region, corresponding to Asp197 to Leu216 of human T-cell lymphotropic virus type 1 (HTLV-1), leading to cell-to-ce
Autor:
Teizo Fujita, L. A. Mclintock, Mitsushi Tsujimura, C. Koch, Marc Turner, Tessa L. Holyoake, I. M. Franklin, N. E. Jordanides, Hiroshi Shiraki, Mhairi Copland, K. Stewart, E. K. Allan, D. C. Kilpatrick, Misao Matsushita
Publikováno v:
Clinical and Experimental Immunology. 134:279-284
SUMMARY Chemotherapy causes neutropenia and an increased susceptibility to infection. Recent reports indicate that mannan-binding lectin (MBL) insufficiency is associated with an increased duration of febrile neutropenia and incidence of serious infe
Autor:
Teizo Fujita, Misao Matsushita, Mitsushi Tsujimura, Naotaka Hamasaki, Mikio Kuraya, Hiroshi Shiraki
Publikováno v:
The Journal of Immunology. 168:3502-3506
Ficolins are a group of proteins which consist of a collagen-like domain and a fibrinogen-like domain. In human serum, there are two types of ficolins named L-ficolin/P35 and H-ficolin (Hakata Ag), both of which have lectin activity. We recently demo
Autor:
Mitsushi Tsujimura, Yasuko Sagara, Koichi Murakami, Yoshiaki Maeda, Hiroshi Shiraki, Kazuo Okochi, Takashi Miyazaki, Chuzo Ishida
Publikováno v:
Clinical Diagnostic Laboratory Immunology. 8:454-459
Although a serum thermolabile β-2 macroglycoprotein (TMG) may play a role in host defense as a lectin, little is known of its related physiological functions, mainly due to a lack of appropriate methods for tracing the functions of TMG. We identifie
Autor:
Misao, Matsushita, David, Kilpatrick, Hiroshi, Shiraki, Yu, Liu, Koichiro, Tateishi, Mitsushi, Tsujimura, Yuichi, Endo, Teizo, Fujita
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 1100
Ficolins constitute a group of lectins involved in innate immunity. L-Ficolin, H-ficolin, and M-ficolin are present in human serum. The human ficolins differ in carbohydrate-binding specificity, but they have in common the ability to recognize the ac
Autor:
Mitsushi Tsujimura, Teizo Fujita, Yu Liu, Hiroshi Shiraki, Misao Matsushita, Koichiro Tateishi, David C. Kilpatrick, Yuichi Endo
Publikováno v:
The Complement System ISBN: 9781627037235
Ficolins constitute a group of lectins involved in innate immunity. L-Ficolin, H-ficolin, and M-ficolin are present in human serum. The human ficolins differ in carbohydrate-binding specificity, but they have in common the ability to recognize the ac
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e27aacbb4be9b71875bada11f1d97b3e
https://doi.org/10.1007/978-1-62703-724-2_12
https://doi.org/10.1007/978-1-62703-724-2_12
Autor:
Kenichi Yoshikawa, Mitiko Go, Mitsushi Tsujimura, Tosiyuki Noguti, Tadao Horiuchi, Hideo Koga, Takanori Yasukochi
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1122:41-44
During investigations of the structural character of a mutant P-450cam where Glu-286 is replaced with lysine, we obtained evidence of a hydrogen bond network between helix K and the heme group via helix L of P-450cam. This mutant protein loses the ab
Autor:
Yasuko Sagara, Yoshiaki Maeda, Mitsushi Tsujimura, Takashi Miyazaki, Hiroshi Shiraki, Eijiro Kojima, Kazuo Okochi
Publikováno v:
Clinica chimica acta; international journal of clinical chemistry. 325(1-2)
Background : Hakata antigen (Hakata) is a novel serum glycoprotein that consists of collagen- and fibrinogen-like domains, similar to ficolin/p35. Our research suggested that serum Hakata may be a target of a polysaccharide (PSA) produced by Aerococc
Publikováno v:
Vox sanguinis. 69(3)
Using an immunodiffusion assay, we tested all of the blood units donated at the Fukuoka Red Cross Blood Center from June 1991 to July 1994 for B19 antigen. Over this 3-year trial period, we detected 16 viremic cases out of approximately 560,000 blood