Zobrazeno 1 - 10
of 156
pro vyhledávání: '"L, Ciardelli"'
Autor:
Michael J. Nemeth, Zining Wu, Thomas M. Laue, Thomas L. Ciardelli, Byron Goldstein, Stefano F. Liparoto
Publikováno v:
Protein Science. 8:482-489
The high affinity interleukin-2 receptor is composed of three cell surface subunits, IL-2Ralpha, IL-2Rbeta, and IL-2Rgamma. Functional forms of the IL-2 receptor exist, however, that enlist only two of the three subunits. On activated T-cells, the al
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bc374fe03a4155056b56d14291545fef
https://doi.org/10.1110/ps.8.3.482
https://doi.org/10.1110/ps.8.3.482
Autor:
Thomas L. Ciardelli, Balaji M. Rao, Andrew T. Girvin, Douglas A. Lauffenburger, K. Dane Wittrup
Publikováno v:
Protein Engineering Design and Selection. 16:1081-1087
Stimulation of T-cells by IL-2 has been exploited for treatment of metastatic renal carcinoma and melanoma. However, a narrow therapeutic window delimited by negligible stimulation of T-cells at low picomolar concentrations and undesirable stimulatio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b365745f64cc2ee4bafd87e04991de1c
https://doi.org/10.1093/protein/gzg111
https://doi.org/10.1093/protein/gzg111
Autor:
Zining Wu, Thomas M. Laue, Stefano F. Liparoto, Thomas L. Ciardelli, Byron Goldstein, David G. Myszka
Publikováno v:
Biochemistry. 41:2543-2551
Interleukin-2 is the primary T cell growth factor secreted by activated T cells. IL-2 is an alpha-helical cytokine that binds to a multisubunit receptor expressed on the surface of a variety of cell types. IL-2Ralpha, IL-2Rbeta, and IL-2Rgammac recep
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2d58a6de78a9a54ccaa0f374947fa6a5
https://doi.org/10.1021/bi011692m
https://doi.org/10.1021/bi011692m
Autor:
Douglas A. Lauffenburger, Stefano F. Liparoto, Eric M. Fallon, Kathy J. Lee, Thomas L. Ciardelli
Publikováno v:
Journal of Biological Chemistry. 275:6790-6797
An interleukin-2 (IL-2) variant containing adjacent point mutations (L18M/L19S, termed 2D1) displaying binding affinity to the heterotrimeric IL-2 receptor similar to that of wild-type IL-2 (WT) had been previously found to surprisingly exhibit incre
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9171f0aa0ed095ed4851cec8406921aa
https://doi.org/10.1074/jbc.275.10.6790
https://doi.org/10.1074/jbc.275.10.6790
Publikováno v:
Journal of Molecular Recognition. 12:316-321
Surface plasmon resonance (SPR) biosensor technology has been a significant addition to the evolution and refinement of methods to study macromolecular interactions. Prior to the advent of SPR, we employed a variety of biochemical and biological tech
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::315b29b2450eb460332cce500853752d
https://doi.org/10.1002/(sici)1099-1352(199909/10)12:5<316::aid-jmr468>3.0.co
https://doi.org/10.1002/(sici)1099-1352(199909/10)12:5<316::aid-jmr468>3.0.co
Autor:
Thomas L. Ciardelli, Betty L. Lee
Publikováno v:
Biochemical and Biophysical Research Communications. 233:309-315
Interleukin-2 (IL-2) is a cytokine essential for the growth and proliferation of T-cells. The purpose of this research was to study the effects of altering the "kink" caused by Pro in an alpha-helix of the protein. The Pro-47 residue was chosen becau
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::78e3043992b0173e05f14b956f303217
https://doi.org/10.1006/bbrc.1997.6453
https://doi.org/10.1006/bbrc.1997.6453
Publikováno v:
Archives of Biochemistry and Biophysics. 339:79-84
We report the novel display of interleukin-2 (IL-2) and an IL-2 analog, D126, on the surface of filamentous bacteriophage using a phagemid vector system. A synthetic human IL-2 gene and its D126 analog were fused to the carboxyl-terminal domain of th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::65fef4d3dae59651cd47fb8a38bafc8f
https://doi.org/10.1006/abbi.1996.9853
https://doi.org/10.1006/abbi.1996.9853
Autor:
Kimberly Howland, Monthakan Ratnarathorn, John A. Sutherland, Johanna C. vanderSpek, John R. Murphy, Thomas L. Ciardelli
Publikováno v:
Journal of Biological Chemistry. 271:12145-12149
Site-directed mutagenesis was used to generate point mutations in the diphtheria toxin-related fusion protein, DAB389 interleukin-2 (IL-2). Thr-439, in the IL-2 receptor binding domain of the fusion toxin, was changed to a Pro residue. The resultant
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1d157dbade3d2e49fc810e2f4663b99a
https://doi.org/10.1074/jbc.271.21.12145
https://doi.org/10.1074/jbc.271.21.12145
Autor:
Byron Goldstein, Thomas L. Ciardelli, Zining Wu, Steven F. Eaton, Thomas M. Laue, Yoon Choi, Kirk W. Johnson
Publikováno v:
Journal of Biological Chemistry. 270:16039-16044
In this study, we report the use of coiled-coil (leucine zipper) molecular recognition for the solution assembly of stable, high affinity, heteromeric interleukin-2 receptor complexes. Co-expression of interleukin-2 receptor alpha and beta extracellu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::29dd0466dc5da4e0d24ec3a4079bfdbd
https://doi.org/10.1074/jbc.270.27.16039
https://doi.org/10.1074/jbc.270.27.16039
Publikováno v:
Journal of Biological Chemistry. 270:16045-16051
Knowledge of the kinetic binding characteristics is often critical to the development of ligand/receptor structure-activity relationships. To better understand the contribution of each of the subunits to ligand binding in the multimeric interleukin-2
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::63c5e7dfadde38495195a63c5971435f
https://doi.org/10.1074/jbc.270.27.16045
https://doi.org/10.1074/jbc.270.27.16045