Zobrazeno 1 - 8
of 8
pro vyhledávání: '"K. E. Truitt"'
Publikováno v:
The Journal of Immunology. 158:4688-4695
Perturbation of several distinct T cell molecules, including the CD3/TCR complex, CD7, and CD28, activates phosphatidylinositol 3-kinase (PI3-K), but a clear consensus on the role of PI3-K in T cell activation has yet to emerge. We report here that C
Publikováno v:
The Journal of Immunology. 156:4539-4541
Although under certain conditions an association with phosphatidylinositol 3'-kinase (PI3-K) appears to be critical for CD28 signaling, mutation of the PI3-K binding site (Tyr 170) does not alter the costimulatory ability of murine CD28 (mCD28) in Ju
Publikováno v:
Journal of immunology (Baltimore, Md. : 1950). 161(10)
The accessory molecule CD28 delivers a costimulus that acts in concert with TCR signals to promote T cell activation. Activation of Jun-N-terminal kinases (JNK) requires simultaneous stimulation of the TCR and CD28 and, therefore, likely plays an imp
Publikováno v:
Journal of immunology (Baltimore, Md. : 1950). 158(10)
Perturbation of several distinct T cell molecules, including the CD3/TCR complex, CD7, and CD28, activates phosphatidylinositol 3-kinase (PI3-K), but a clear consensus on the role of PI3-K in T cell activation has yet to emerge. We report here that C
Publikováno v:
Journal of immunology (Baltimore, Md. : 1950). 156(12)
Although under certain conditions an association with phosphatidylinositol 3'-kinase (PI3-K) appears to be critical for CD28 signaling, mutation of the PI3-K binding site (Tyr 170) does not alter the costimulatory ability of murine CD28 (mCD28) in Ju
Publikováno v:
Journal of immunology (Baltimore, Md. : 1950). 155(10)
CD28, a cell-surface molecule expressed by T cells, delivers costimulatory signals during the activation of T cells by Ag. Stimulation of CD28 induces its association with phosphatidylinositol 3'-kinase (PI3-K), raising the possibility that PI3-K pla
Publikováno v:
The Journal of biological chemistry. 269(8)
Interleukin-2 (IL-2) signaling results in tyrosine phosphorylation of the 75-kDa IL-2 receptor (IL-2R) beta chain and the activation of phosphatidylinositol 3'-kinase (PI3-K). Herein, we demonstrate that the 85-kDa (p85) regulatory subunit of PI3-K p
Autor:
Robert J. Linhardt, C. W. Abell, R. M. Denney, B. W. Altrock, R. Auerbach, S. D. Bernal, R. E. Canfield, P. H. Ehrlich, W. R. Moyle, T. S. Chan, T. W. Chang, N. T. Chang, J. A. Cidlowski, M. D. Viceps, R. J. Cote, D. M. Morrissey, A. N. Houghton, E. J. Beattie, H. F. Oettgen, L. J. Old, C. M. Croce, R. S. Cubicciotti, A. E. Karu, R. M. Krauss, J. S. Cullor, A. Deutsch, H. Brandwein, H. Platt, D. M. Hunter, A. Dubitsky, S. M. Durham, F. A. Dolbeare, J. W. Gray, G. R. Dreesman, C. E. Kendall, J. C. Egrie, A. R. Frackelton, H. N. Eisen, A. H. Ross, S. Gay, G. Geirnaert, J. E. Geltosky, E. H. Goldberg, E. Goldwasser, C. Kavinsky, T. L. Weiss, H. G. Gratzner, B. Hampar, M. Zweig, S. D. Showalter, H. H. Handley, M. C. Glassy, Y. Hagiwara, H. Hagiwara, C. M. Huang, S. N. Cohen, J. V. Hughes, E. M. Scolnick, J. E. Tomassini, R. Jefferis, J. Steensgaard, H. S. Kaplan, N. N. H. Teng, K. S. Earn, R. F. Calvo, L. Kass, J. R. Kettman, M. V. Norgard, M. B. Khazaeli, W. H. Beierwaltes, B. G. England, P. C. Kung, G. Goldstein, L. Lanier, J. Phillips, N. L. Warner, J. W. Larrick, A. R. Raubitschek, K. E. Truitt, H. Lazarus, J. F. Schwaber, J. Lewicki, C. Lewis, J. V. Olander, W. R. Tolbert, E. L. Milford, C. B. Carpenter, J. M. Paradysz, D. F. Mosher, J. L. Mulshine, J. D. Minna, K. A. Murray, D. M. Neville, R. J. Youle, M. Nicolson, I. Pastan, M. C. Willingham, D. J. Fitzgerald, A. Pucci, A. M. Smithyman, M. B. Slade, P. W. French, G. Wijffels, C. S. Pukel, K. O. Lloyd, L. R. Travassos, W. G. Dippold, R. P. Reckel, J. L. Harris, R. Wellerson, S. M. Shaw, P. M. Kaplan, E. L. Reinherz, S. F. Schlossman, S. C. Mener, J. Sakamoto, C. C. Cordon, E. Friedman, C. L. Finstad, W. E. Enker, M. R. Melamed, J. F. Oettgen, P. J. Scannon, L. E. Spitler, H. M. Lee, R. T. Kawahata, R. P. Mischak, J. Schlom, D. Colcher, M. Nuti, P. H. Hand, F. Austin, G. D. Shockman, D. E. Jackson, W. Wong, Z. Steplewski, H. Koprowski, M. Herlyn, M. Strand, I. S. Trowbridge, D. L. Urdal, C. J. March, S. K. Dower, J. R. Wands, V. R. Zurawski, C. A. White, R. Dulbecco, W. R. Allen, E. C. Arnold, M. Flasher, H. H. Freedman, T. D. Heath, P. Shek, D. Papahadjopoulos, M. Ikeda, S. Sakamoto, K. Suzuki, M. Kuboyama, Y. Harada, A. Kawashiri, E. Takahashi, H. S. Lee, S. Margel, R. C. Nowinski, A. S. Hoffman, J. W. Peterson, K. B. Platt, D. E. Reed, F. X. Real, M. J. Mattes, P. O. Livingston, A. Rembaum, R. C. K. Yen, R. Rosenstein, B. Schneider
Publikováno v:
Applied Biochemistry and Biotechnology. 15:53-80
Antibodies in both their free and immobilized state have been the object of considerable industrial and academic interest. A variety of methods are used for preparing and immobilizing antibodies. Applications for monoclonal antibodies include the pre