Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Clint D J, Tavares"'
Autor:
Tamer S. Kaoud, William H. Johnson, Nancy D. Ebelt, Andrea Piserchio, Diana Zamora-Olivares, Sabrina X. Van Ravenstein, Jacey R. Pridgen, Ramakrishna Edupuganti, Rachel Sammons, Micael Cano, Mangalika Warthaka, Matthew Harger, Clint D. J. Tavares, Jihyun Park, Mohamed F. Radwan, Pengyu Ren, Eric V. Anslyn, Kenneth Y. Tsai, Ranajeet Ghose, Kevin N. Dalby
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-15 (2019)
The ERK signalling pathway is activated in many cancers, however ERK1 and ERK2 are difficult to target pharmacologically. Here, the authors identify a small molecule inhibitor that binds covalently to the D-recruitment site of ERK and induces cell de
Externí odkaz:
https://doaj.org/article/a5398760f41b41118e32f8afccdebe49
Publikováno v:
Frontiers in Molecular Biosciences, Vol 2 (2015)
A-484954 is a known eEF2K inhibitor with submicromolar IC50 potency. However, the binding mechanism and the crystal structure of the kinase remains unknown. Here, we employ a homology eEF2K model, docking and alchemical free energy simulations to pro
Externí odkaz:
https://doaj.org/article/eb9e186484c84465969163fd604c5922
Autor:
Ibrahim Tekedereli, S Neslihan Alpay, Clint D J Tavares, Zehra E Cobanoglu, Tamer S Kaoud, Ibrahim Sahin, Anil K Sood, Gabriel Lopez-Berestein, Kevin N Dalby, Bulent Ozpolat
Publikováno v:
PLoS ONE, Vol 7, Iss 7, p e41171 (2012)
Eukaryotic elongation factor 2 kinase (eEF-2K), through its phosphorylation of elongation factor 2 (eEF2), provides a mechanism by which cells can control the rate of the elongation phase of protein synthesis. The activity of eEF-2K is increased in r
Externí odkaz:
https://doaj.org/article/7b1050ea3c5247ddb961e153def8c789
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
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 1360
Protein kinases have emerged as an important class of therapeutic targets, as they are known to be involved in pathological pathways linked to numerous human disorders. Major efforts to discover kinase inhibitors in both academia and pharmaceutical c