Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Rebecca M, Wellmann"'
Autor:
Scarlett B. Ferguson, David H. Giles, Rebecca M. Wellmann, Kevin N. Dalby, Tamer S. Kaoud, Gabriel Stancu, Ranajeet Ghose, Catrina A. Chitjian, Clint D.J. Tavares
Publikováno v:
Journal of Biological Chemistry. 292:2032-2045
Eukaryotic elongation factor 2 kinase (eEF-2K), the only calmodulin (CaM)-dependent member of the unique α-kinase family, impedes protein synthesis by phosphorylating eEF-2. We recently identified Thr-348 and Ser-500 as two key autophosphorylation s
Autor:
David H. Giles, Jennifer S. Brodbelt, Kevin N. Dalby, John P. O'Brien, Mangalika Warthaka, Rebecca M. Wellmann, Clint D.J. Tavares, Scarlett B. Ferguson, Pengyu Ren, Qiantao Wang
Publikováno v:
Journal of Biological Chemistry. 289:23901-23916
Calmodulin (CaM)-dependent eukaryotic elongation factor 2 kinase (eEF-2K) impedes protein synthesis through phosphorylation of eukaryotic elongation factor 2 (eEF-2). It is subject to complex regulation by multiple upstream signaling pathways, throug
Publikováno v:
Journal of Clinical Oncology. 37:e12049-e12049
e12049 Background: Triple-negative breast cancer (TNBC) is associated with a poor prognosis when compared to hormone receptor positive breast cancers. Anthracycline-based regimens (ABRs) are mainstays of treatment for non-metastatic TNBC. However, an
Autor:
Clint D J, Tavares, David H, Giles, Gabriel, Stancu, Catrina A, Chitjian, Scarlett B, Ferguson, Rebecca M, Wellmann, Tamer S, Kaoud, Ranajeet, Ghose, Kevin N, Dalby
Publikováno v:
The Journal of biological chemistry. 292(5)
Eukaryotic elongation factor 2 kinase (eEF-2K), the only calmodulin (CaM)-dependent member of the unique α-kinase family, impedes protein synthesis by phosphorylating eEF-2. We recently identified Thr-348 and Ser-500 as two key autophosphorylation s
Autor:
Sébastien Alphonse, Ranajeet Ghose, David H. Giles, Kwangwoon Lee, Clint D.J. Tavares, Rebecca M. Wellmann, Andrea Piserchio, Kevin N. Dalby
Publikováno v:
Structure (London, England : 1993). 24(9)
Binding of Ca(2+)-loaded calmodulin (CaM) activates eukaryotic elongation factor 2 kinase (eEF-2K) that phosphorylates eEF-2, its only known cellular target, leading to a decrease in global protein synthesis. Here, using an eEF-2K-derived peptide (eE
Autor:
Jennifer S. Brodbelt, Tamer S. Kaoud, Scarlett B. Ferguson, Bulent Ozpolat, Clint D.J. Tavares, John P. O'Brien, Kevin N. Dalby, Rebecca M. Wellmann
Publikováno v:
Cancer Research. 73:2222-2222
Breast cancer is the most common malignancy in women in the Western world, with over 40,000 deaths attributed to this disease. Studies have demonstrated that breast cancer mitogens regulate the activity of eukaryotic elongation factor 2 kinase (eEF-2