Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Teresa R. Brtva"'
Autor:
Teresa R. Brtva, Kun-Liang Guan, Jennifer K. Taylor, Tianquan Zhu, Theodore D. Barber, Claudia Figueroa, Anne B. Vojtek
Publikováno v:
The Journal of biological chemistry. 275(35)
B-Raf contains multiple Akt consensus sites located within its amino-terminal regulatory domain. One site, Ser(364), is conserved with c-Raf but two additional sites, Ser(428) and Thr(439), are unique to B-Raf. We have investigated the role of both t
Publikováno v:
Biochemical and biophysical research communications. 243(2)
Protein kinase C (PKC)-dependent activation of the Ras signal transduction cascade is essential for induction of the IL-2 promoter during stimulation of T lymphocytes via the T cell receptor (TCR). In this study, the effects of PKC-activating phorbol
Autor:
Daniel L. Altschuler, Lorenza Trabalzini, Thomas Fischer, Eduardo G. Lapetina, Gilbert C. White, Scott N. Peterson, Teresa R. Brtva, Paola Martelli, Channing J. Der
Although Ras and Rap1 share interaction with common candidate effector proteins, Rap1 lacks the transforming activity exhibited by Ras proteins. It has been speculated that Rap antagonizes Ras transformation through the formation of nonproductive com
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8c328c80acc57b4cb3b8ddf237cccaad
Autor:
Channing J. Der, Patricia A. Solski, Lawrence A. Quilliam, Suzanne M. Graham, Shayne Y. Huff, Roya Khosravi-Far, Ashley F. Overbeck, Adrienne D. Cox, Teresa R. Brtva
Publikováno v:
Molecular reproduction and development. 42(4)
Members of the Ras superfamily of proteins function as regulated GDP/GTP switches that cycle between active GTP-complexed and inactive GDP-complexed states. Guanine nucleotide exchange factors (GEFs) stimulate formation of the GTP-bound state, wherea
Autor:
Robert M. Bell, Channing J. Der, Sharon Campbell-Burk, Regina S. Terrell, Teresa R. Brtva, Jonelle K. Drugan, Sujoy Ghosh
A key event for Ras transformation involves the direct physical association between Ras and the Raf-1 kinase. This interaction promotes both Raf translocation to the plasma membrane and activation of Raf kinase activity. Although substantial experime
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f04b00f3c71b565849bb656e22491fd4