Sean M. Post, Ph.D.
Affiliations: | 2003 | The University of Texas Health Science Center at San Antonio, San Antonio, TX, United States |
Area:
Cell Biology, Molecular Biology, OncologyGoogle:
"Sean Post"Parents
Sign in to add mentorEva Y. P. Lee | grad student | 2003 | UT Health San Antonio | |
(The role of ATR-mediated phosphorylation of human Rad17 in the DNA damage and replication checkpoints.) |
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Publications
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Post SM, Ma H, Malaney P, et al. (2021) AXL/MERTK inhibitor ONO-7475 potently synergizes with venetoclax and overcomes venetoclax resistance to kill -ITD acute myeloid leukemia. Haematologica |
Post SM, Andreeff M, DiNardo C, et al. (2021) TAM kinases as regulators of cell death. Biochimica Et Biophysica Acta. Molecular Cell Research. 1868: 118992 |
Ruvolo PP, Ruvolo VR, Burks JK, et al. (2018) Role of MSC-derived galectin 3 in the AML microenvironment. Biochimica Et Biophysica Acta |
Ruvolo PP, Ma H, Ruvolo VR, et al. (2017) Anexelekto /MER Tyrosine Kinase inhibitor ONO-7475 growth arrests and kills FMS-Like Tyrosine Kinase 3-Internal Tandem Duplication Mutant Acute Myeloid Leukemia cells by diverse mechanisms. Haematologica |
Jackson JG, Post SM, Lozano G. (2011) Regulation of tissue- and stimulus-specific cell fate decisions by p53 in vivo. The Journal of Pathology. 223: 127-36 |
Martinez LA, Goluszko E, Chen HZ, et al. (2010) E2F3 is a mediator of DNA damage-induced apoptosis. Molecular and Cellular Biology. 30: 524-36 |
Song W, Levin DS, Varkey J, et al. (2007) A conserved physical and functional interaction between the cell cycle checkpoint clamp loader and DNA ligase I of eukaryotes. The Journal of Biological Chemistry. 282: 22721-30 |
Post SM, Lee EY. (2004) Detection of kinase and phosphatase activities. Methods in Molecular Biology (Clifton, N.J.). 241: 285-97 |
Motycka TA, Bessho T, Post SM, et al. (2004) Physical and functional interaction between the XPF/ERCC1 endonuclease and hRad52. The Journal of Biological Chemistry. 279: 13634-9 |
Post SM, Tomkinson AE, Lee EY. (2003) The human checkpoint Rad protein Rad17 is chromatin-associated throughout the cell cycle, localizes to DNA replication sites, and interacts with DNA polymerase epsilon. Nucleic Acids Research. 31: 5568-75 |