Maria Diakonova
Affiliations: | Biology (Cell-Molecular Biology) | The University of Toledo |
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Cell BiologyGoogle:
"Maria Diakonova"
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Publications
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| Shahi A, Kahle J, Hopkins C, et al. (2022) The SH2 domain and kinase activity of JAK2 target JAK2 to centrosome and regulate cell growth and centrosome amplification. Plos One. 17: e0261098 |
| Hammer A, Diakonova M. (2016) Prolactin-induced PAK1 tyrosyl phosphorylation promotes FAK dephosphorylation, breast cancer cell motility, invasion and metastasis. Bmc Cell Biology. 17: 31 |
| Oladimeji P, Diakonova M. (2016) PAK1 translocates into nucleus in response to prolactin but not to estrogen. Biochemical and Biophysical Research Communications |
| Oladimeji P, Skerl R, Rusch C, et al. (2016) Synergistic activation of ERα by estrogen and prolactin in breast cancer cells requires tyrosyl phosphorylation of PAK1. Cancer Research |
| Oladimeji P, Kubohara Y, Kikuchi H, et al. (2015) A Derivative of Differentiation-Inducing Factor-3 Inhibits PAK1 Activity and Breast Cancer Cell Proliferation. International Journal of Cancer and Clinical Research. 2: 1-6 |
| Hammer A, Laghate S, Diakonova M. (2015) Src tyrosyl phosphorylates cortactin in response to prolactin. Biochemical and Biophysical Research Communications. 463: 644-9 |
| Hammer A, Diakonova M. (2015) Tyrosyl phosphorylated serine-threonine kinase PAK1 is a novel regulator of prolactin-dependent breast cancer cell motility and invasion. Advances in Experimental Medicine and Biology. 846: 97-137 |
| Hammer A, Oladimeji P, De Las Casas LE, et al. (2015) Phosphorylation of tyrosine 285 of PAK1 facilitates βPIX/GIT1 binding and adhesion turnover. Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology. 29: 943-59 |
| Jay J, Hammer A, Nestor-Kalinoski A, et al. (2015) JAK2 tyrosine kinase phosphorylates and is negatively regulated by centrosomal protein Ninein. Molecular and Cellular Biology. 35: 111-31 |
| Rider L, Oladimeji P, Diakonova M. (2013) PAK1 regulates breast cancer cell invasion through secretion of matrix metalloproteinases in response to prolactin and three-dimensional collagen IV. Molecular Endocrinology (Baltimore, Md.). 27: 1048-64 |