Zobrazeno 1 - 10
of 68
pro vyhledávání: '"K, Fushitani"'
Autor:
R A Whiley, K. Fushitani, A. Katsuura, Akihiko Tsuji, Hideaki Nagamune, C. Ohnishi, Yoshiko Matsuda
Publikováno v:
Infection and Immunity. 64:3093-3100
A novel cytotoxin (intermedilysin) specific for human cells was identified as a cytolytic factor of Streptococcus intermedius UNS46 isolated from a human liver abscess. Intermedilysin caused human cell death with membrane blebs. Intermedilysin was pu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d2e559e321ee198e9cd589595fe0c7cb
https://doi.org/10.1128/iai.64.8.3093-3100.1996
https://doi.org/10.1128/iai.64.8.3093-3100.1996
Publikováno v:
Hemoglobin. 19:403-406
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2a86f399c9e0866316ec1897b1cdb09f
https://doi.org/10.3109/03630269509005832
https://doi.org/10.3109/03630269509005832
Autor:
Austen Riggs, K Fushitani
Publikováno v:
Journal of Biological Chemistry. 266:10275-10281
The extracellular hemoglobin of the earthworm Lumbricus terrestris has a two-tiered hexagonal structure that can be dissociated into 1/12 subunits. The Hb contains four major kinds of oxygen-binding chains, a, b, c, and d, of which a-c form a disulfi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::213c78da7119cc5dbf91a698624ad020
https://doi.org/10.1016/s0021-9258(18)99221-5
https://doi.org/10.1016/s0021-9258(18)99221-5
Publikováno v:
Anticancer research. 19(1A)
We have demonstrated a higher nuclear protein content in the hypodiploid fraction of BG-1 human ovarian cancer cells following treatment with one of the ether lipids, ET-18-OCH3. In this study, we have attempted to identify the overexpressed nuclear
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::701478ea4f5ec97cfc2eb37c663303b7
https://pubmed.ncbi.nlm.nih.gov/10226541
https://pubmed.ncbi.nlm.nih.gov/10226541
Autor:
H, Nagamune, C, Ohnishi, A, Katsuura, Y, Taoka, K, Fushitani, R A, Whiley, K, Yamashita, A, Tsuji, Y, Matsuda, T, Maeda, H, Korai, S, Kitamura
Publikováno v:
Advances in experimental medicine and biology. 418
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::8069bc80a80b4fde1daa79039e4df1c4
https://pubmed.ncbi.nlm.nih.gov/9331766
https://pubmed.ncbi.nlm.nih.gov/9331766
Publikováno v:
Hemoglobin. 19(6)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::2a696b3d2266fa932a776a2726459530
https://pubmed.ncbi.nlm.nih.gov/8718699
https://pubmed.ncbi.nlm.nih.gov/8718699
Autor:
K, Fushitani, A F, Riggs
Publikováno v:
The Journal of biological chemistry. 266(16)
The extracellular hemoglobin of the earthworm Lumbricus terrestris has a two-tiered hexagonal structure that can be dissociated into 1/12 subunits. The Hb contains four major kinds of oxygen-binding chains, a, b, c, and d, of which a-c form a disulfi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::3c29cdea200db596827049b29b4816b7
https://pubmed.ncbi.nlm.nih.gov/2037579
https://pubmed.ncbi.nlm.nih.gov/2037579
Autor:
K, Imai, K, Fushitani, G, Miyazaki, K, Ishimori, T, Kitagawa, Y, Wada, H, Morimoto, I, Morishima, D T, Shih, J, Tame
Publikováno v:
Journal of molecular biology. 218(4)
To clarify the functional role of Tyr-42(C7) alpha, which forms a hydrogen bond with Asp-99(G1) beta at the alpha 1-beta 2 interface of human deoxyhaemoglobin, we engineered two artificial mutant haemoglobins (Hb), in which Tyr-42 alpha was replaced
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::a7f8dd9b3f86ee83a671395ee835d319
https://pubmed.ncbi.nlm.nih.gov/2023248
https://pubmed.ncbi.nlm.nih.gov/2023248
Publikováno v:
Journal of Biological Chemistry. 264:5515-5521
The hemoglobin of Liophis miliaris has unusual properties. The hemoglobin is dimeric in the oxy form, and the cooperativity of O2 binding is very low, but both the Bohr effect and cooperativity are greatly enhanced in the presence of ATP (Matsuura, M
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b645535225855d047e77918658a28396
https://doi.org/10.1016/s0021-9258(18)83575-x
https://doi.org/10.1016/s0021-9258(18)83575-x
Publikováno v:
Journal of Biological Chemistry. 263:6502-6517
The extracellular hemoglobin of Lumbricus terrestris comprises four major heme-containing chains, a, b, c, and d in equal proportions. We have determined the amino acid sequences of chains a, b, and c which form a disulfide-linked trimer. Chains a, b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1c7475891368c5d0426a45ef0f8d849f
https://doi.org/10.1016/s0021-9258(18)68671-5
https://doi.org/10.1016/s0021-9258(18)68671-5