Zobrazeno 1 - 10
of 19
pro vyhledávání: '"Elena S. Stavridi"'
Autor:
Soheila Emamzadah, Thanos D. Halazonetis, Jeffery G. Saven, Tom J. Petty, Lorenzo Costantino, Irina Petkova, Elena S. Stavridi, Eric Vauthey
Publikováno v:
The EMBO Journal. 30:2167-2176
The p53 tumour suppressor gene, the most frequently mutated gene in human cancer, encodes a transcription factor that contains sequence-specific DNA binding and homo-tetramerization domains. Interestingly, the affinities of p53 for specific and non-s
Autor:
Richard A. DiTullio, Emily A. Sheston, Yentram Huyen, Hestia S. Mellert, Thanos D. Halazonetis, Elena S. Stavridi, Omar Zgheib, Panayotis Zacharatos, Vassilis G. Gorgoulis, Tom J. Petty
Publikováno v:
Nature. 432:406-411
The mechanisms by which eukaryotic cells sense DNA double-strand breaks (DSBs) in order to initiate checkpoint responses are poorly understood. 53BP1 is a conserved checkpoint protein with properties of a DNA DSB sensor. Here, we solved the structure
Autor:
Thanos D. Halazonetis, W. Brent Derry, Joel H. Rothman, Elena S. Stavridi, Nikola P. Pavletich, Yentram Huyen, Philip D. Jeffrey
Publikováno v:
Structure. 12:1237-1243
The DNA binding domains of human p53 and Cep-1, its C. elegans ortholog, recognize essentially identical DNA sequences despite poor sequence similarity. We solved the three-dimensional structure of the Cep-1 DNA binding domain in the absence of DNA a
Publikováno v:
Genes & Development. 18:241-244
The p53 tumor suppressor is one of the central players in the response of cells to various forms of stress. Clearly, the main form of stress that activates p53 is genotoxic stress in the form of DNA double-strand breaks (DSBs) or stalled DNA replicat
Autor:
Nikola P. Pavletich, John Bothos, Steve E Stayrook, Philip D. Jeffrey, Yentram Huyen, Kimberly G. Harris, Peter-Mark Verwoerd, Francis C. Luca, Elena S. Stavridi
Publikováno v:
Structure. 11(9):1163-1170
The Mob protein family comprises a group of highly conserved eukaryotic proteins whose founding member functions in the mitotic exit network. At the molecular level, Mob proteins act as kinase-activating subunits. We cloned a human Mob1 family member
Autor:
Nikola P. Pavletich, Philip D. Jeffrey, Thanos D. Halazonetis, Yentram Huyen, Daniel M. Scolnick, Ivy R. Loreto, Elena S. Stavridi
Publikováno v:
Structure. 10:891-899
The Chfr mitotic checkpoint protein is frequently inactivated in human cancer. We determined the three-dimensional structure of its FHA domain in its native form and in complex with tungstate, an analog of phosphate. The structures revealed a β sand
Publikováno v:
Journal of Cellular Physiology. 190:365-374
Although p53 responses after DNA damage have been investigated extensively, p53 responses after heat shock, which exerts cytotoxic action by mechanisms other than direct induction of DNA damage, are less well characterized. We investigated, therefore
Autor:
Asra Malikzay, Richard A. DiTullio, Nabil H. Chehab, L.B. Schultz, Thanos D. Halazonetis, Elena S. Stavridi
Publikováno v:
Cold Spring Harbor Symposia on Quantitative Biology. 65:489-498
Publikováno v:
Protein Science. 8:1773-1779
The tumor suppressor function of the wild-type p53 protein is transdominantly inhibited by tumor-derived mutant p53 proteins. Such transdominant inhibition limits the prospects for gene therapy approaches that aim to introduce wild-type p53 into canc
Publikováno v:
Nature Cell Biology. 7:648-650
The Nbs1 protein participates in the cell-cycle checkpoint response to DNA double-strand breaks (DSBs), but its precise mode of action — especially in relation to the checkpoint kinase Atm — has been debated. New mouse models suggest that Nbs1 is