Zobrazeno 1 - 10
of 17
pro vyhledávání: '"E L Barsumian"'
Autor:
M, Suemura, H, Kikutani, K, Sugiyama, N, Uchibayashi, M, Aitani, T, Kuritani, E L, Barsumian, A, Yamatodani, T, Kishimoto
Publikováno v:
Allergy proceedings : the official journal of regional and state allergy societies. 12(3)
The significance of sFc epsilon RII in IgE-mediated allergic disease was examined. sFc epsilon RII in serum was found to decrease following clinical improvement, suggesting sFc epsilon RII in serum may be an indicator of allergic diseases. Significan
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::6f8c26cc11100d5db962f1ae95921c5d
https://pubmed.ncbi.nlm.nih.gov/1716601
https://pubmed.ncbi.nlm.nih.gov/1716601
Autor:
N Uchibayashi, H Kikutani, E L Barsumian, R Hauptmann, F J Schneider, R Schwendenwein, W Sommergruber, W Spevak, I Maurer-Fogy, M Suemura
Publikováno v:
The Journal of Immunology. 142:3901-3908
We have undertaken the production of recombinant soluble Fc epsilon receptor II (Fc epsilon RII) as a secretory protein, but not as a cleavage product of membrane-bound receptor. Several plasmid constructs containing soluble receptor sequence were pr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::09d5448a308c0d7fac1e99317eb9aaef
https://doi.org/10.4049/jimmunol.142.11.3901
https://doi.org/10.4049/jimmunol.142.11.3901
Publikováno v:
Infection and Immunity. 14:767-775
Streptococcal pyrogenic exotoxin (SPE) isolated from culture filtrates of strain NY-5 (type 10), and separated from other extracellular by differential solubility in ethanol and acetate-buffered saline, has previously been shown to exhibit a wide ran
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a67675e853d47d950ab169171b60a535
https://doi.org/10.1128/iai.14.3.767-775.1976
https://doi.org/10.1128/iai.14.3.767-775.1976
Autor:
M Suemura, H Kikutani, E L Barsumian, Y Hattori, S Kishimoto, R Sato, A Maeda, H Nakamura, H Owaki, R R Hardy
Publikováno v:
The Journal of Immunology. 137:1214-1220
Three monoclonal antibodies, 1-7 (gamma 2b), 3-5 (gamma 1), and 8-30 (mu), specific to Fc epsilon receptors (Fc epsilon R) on human B cells were established. The two monoclonals (1-7 and 8-30) could inhibit the binding of IgE to Fc epsilon R in roset
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ae818837073696a509aeaf9cf1d017b0
https://doi.org/10.4049/jimmunol.137.4.1214
https://doi.org/10.4049/jimmunol.137.4.1214
A B cell-specific differentiation antigen, CD23, is a receptor for IgE (Fc epsilon R) on lymphocytes
Autor:
K Yukawa, H Kikutani, H Owaki, K Yamasaki, A Yokota, H Nakamura, E L Barsumian, R R Hardy, M Suemura, T Kishimoto
Publikováno v:
The Journal of Immunology. 138:2576-2580
Two independent L cell transformants expressing human lymphocyte Fc epsilon R were established by using cellular DNA from RPMI 8866 cells. The surface expression of the receptor was confirmed on the basis of the binding of a panel of anti-Fc epsilon
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b4a6c7518ee139e0b79dfed599577536
https://doi.org/10.4049/jimmunol.138.8.2576
https://doi.org/10.4049/jimmunol.138.8.2576
Publikováno v:
The Journal of Immunology. 127:1318-1322
A cell-associated lectin activity that mediates lactose-inhibitable adherence of Actinomyces viscosus T14V has been localized to a specific population of fimbriae by the use of monoclonal antibodies. Nine monoclonal antibodies were produced that reac
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9e0260b0bff4a501a4eef2b82a7e02f7
https://doi.org/10.4049/jimmunol.127.4.1318
https://doi.org/10.4049/jimmunol.127.4.1318
Publikováno v:
Infection and Immunity. 22:681-688
Group A streptococcal pyrogenic exotoxin (SPE) types A, B, and C induced lymphocyte proliferation both specifically and nonspecifically, and the responses showed characteristics associated with both types of stimulation. Guinea pig lymphocytes from a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::074700c991d6e247d87a3b023412e804
https://doi.org/10.1128/iai.22.3.681-688.1978
https://doi.org/10.1128/iai.22.3.681-688.1978
Autor:
M, Suemura, H, Kikutani, E L, Barsumian, Y, Hattori, S, Kishimoto, R, Sato, A, Maeda, H, Nakamura, H, Owaki, R R, Hardy
Publikováno v:
Journal of immunology (Baltimore, Md. : 1950). 137(4)
Three monoclonal antibodies, 1-7 (gamma 2b), 3-5 (gamma 1), and 8-30 (mu), specific to Fc epsilon receptors (Fc epsilon R) on human B cells were established. The two monoclonals (1-7 and 8-30) could inhibit the binding of IgE to Fc epsilon R in roset
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::66303f3408c3ece3277d17fab5c2078f
https://pubmed.ncbi.nlm.nih.gov/2426355
https://pubmed.ncbi.nlm.nih.gov/2426355
A B cell-specific differentiation antigen, CD23, is a receptor for IgE (Fc epsilon R) on lymphocytes
Autor:
K, Yukawa, H, Kikutani, H, Owaki, K, Yamasaki, A, Yokota, H, Nakamura, E L, Barsumian, R R, Hardy, M, Suemura, T, Kishimoto
Publikováno v:
Journal of immunology (Baltimore, Md. : 1950). 138(8)
Two independent L cell transformants expressing human lymphocyte Fc epsilon R were established by using cellular DNA from RPMI 8866 cells. The surface expression of the receptor was confirmed on the basis of the binding of a panel of anti-Fc epsilon
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::0a36573dd6f4b6b3d934c2476354e5ea
https://pubmed.ncbi.nlm.nih.gov/2951441
https://pubmed.ncbi.nlm.nih.gov/2951441
Publikováno v:
Infection and immunity. 20(2)
Streptococcal pyrogenic exotoxin type B purified from culture filtrates of either the NY-5 or T-19 strain of group A streptococcus was found to be heterogeneous in charge. Three protein fractions with isoelectric points of 8.0, 8.4, and 9.0 were isol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2e88f1e995f16c3516254a15e385dcca
https://pubmed.ncbi.nlm.nih.gov/352946
https://pubmed.ncbi.nlm.nih.gov/352946