Zobrazeno 1 - 9
of 9
pro vyhledávání: '"T. J. Oglesby"'
Publikováno v:
Clinical & Experimental Immunology. Feb1991, Vol. 83 Issue 2, p257-261. 5p.
Publikováno v:
The Journal of Immunology. 149:163-168
Inhibition of complement proteins D, B, C2, C1s, C1r, I, and the catalytic fragments Bb and C2a by substituted isocoumarins was investigated. 3,4-Dichloroisocoumarin, a general serine protease inhibitor, inhibited factor D, C1r, and C1s moderately wi
Publikováno v:
The Journal of Experimental Medicine
The cleavage of C3 is a critical step for complement (C) activation in the classical and alternative pathways. This reaction is controlled by the regulators of C activation protein family. Membrane cofactor protein (MCP) is a cofactor for the factor
Publikováno v:
Clinical and Experimental Immunology. 86:27-30
Publikováno v:
The Anatomical record. 246(1)
The membrane-associated proteins that regulate human complement activation are ubiquitously expressed and function cooperatively to protect cells from autologous complement damage. For classical and alternative pathways, the primary regulators at the
Publikováno v:
Journal of immunology (Baltimore, Md. : 1950). 151(2)
Human spermatozoa were analyzed for their expression of decay-accelerating factor (DAF, CD55), a glycolipid-anchored regulatory protein of the C casade. Morphologic data showed that DAF was localized at the acrosomal region of the sperm head. Analysi
SUMMARY MCP is a widely distributed regulatory glycoprotein of the complement system which binds C3b and C4b and has factor I-dependent co-factor activity. Monoclonal antibodies raised to lymphocytes (E4.3), chorionic microvilli (GB24) and an embryon
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dad890ea28ca7bbb54b78a444e0a4dd1
https://europepmc.org/articles/PMC1535256/
https://europepmc.org/articles/PMC1535256/
Publikováno v:
The Journal of Immunology. 141:926-931
We raised murine mAb against human C protein C2. The representative mAb 3A3.3 (IgG1 kappa) recognized an epitope on the C2b domain of C2, as determined by binding and inhibition of binding radioassays. The hemolytic activity of purified human C2 and
Lysis of sensitized sheep erythrocytes in human sera deficient in the second component of complement
Autor:
K L, Knutzen Steuer, L B, Sloan, T J, Oglesby, T C, Farries, M W, Nickells, P, Densen, J B, Harley, J P, Atkinson
Publikováno v:
Journal of immunology (Baltimore, Md. : 1950). 143(7)
Analysis of C-dependent lysis of sensitized SRBC by C2-deficient sera (C2D) led to the characterization of a C2 bypass pathway. Lysis in the total hemolytic C assay by C2D sera was Ca2+-dependent and required a high concentration of hemolysin to sens