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A. K. McClendon, Ph.D.

Affiliations: 
2006 Vanderbilt University, Nashville, TN 
Area:
Biochemistry
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"A. McClendon"
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Neil Osheroff grad student 2006 Vanderbilt
 (Human topoisomerases and DNA geometry: Putting a positive twist on enzyme action.)

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Publications

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Dean JL, McClendon AK, Knudsen ES. (2012) Modification of the DNA damage response by therapeutic CDK4/6 inhibition. The Journal of Biological Chemistry. 287: 29075-87
McClendon AK, Dean JL, Ertel A, et al. (2010) Differential impact of tumor suppressor pathways on DNA damage response and therapy-induced transformation in a mouse primary cell model. Plos One. 5: e8558
McClendon AK, Gentry AC, Dickey JS, et al. (2008) Bimodal recognition of DNA geometry by human topoisomerase II alpha: preferential relaxation of positively supercoiled DNA requires elements in the C-terminal domain. Biochemistry. 47: 13169-78
Braden WA, McClendon AK, Knudsen ES. (2008) Cyclin-dependent kinase 4/6 activity is a critical determinant of pre-replication complex assembly. Oncogene. 27: 7083-93
Frøhlich RF, Veigaard C, Andersen FF, et al. (2007) Tryptophane-205 of human topoisomerase I is essential for camptothecin inhibition of negative but not positive supercoil removal. Nucleic Acids Research. 35: 6170-80
McClendon AK, Osheroff N. (2007) DNA topoisomerase II, genotoxicity, and cancer. Mutation Research. 623: 83-97
McClendon AK, Dickey JS, Osheroff N. (2006) Ability of viral topoisomerase II to discern the handedness of supercoiled DNA: bimodal recognition of DNA geometry by type II enzymes. Biochemistry. 45: 11674-80
McClendon AK, Osheroff N. (2006) The geometry of DNA supercoils modulates topoisomerase-mediated DNA cleavage and enzyme response to anticancer drugs. Biochemistry. 45: 3040-50
McClendon AK, Rodriguez AC, Osheroff N. (2005) Human topoisomerase IIalpha rapidly relaxes positively supercoiled DNA: implications for enzyme action ahead of replication forks. The Journal of Biological Chemistry. 280: 39337-45
Sappal DS, McClendon AK, Fleming JA, et al. (2004) Biological characterization of MLN944: a potent DNA binding agent. Molecular Cancer Therapeutics. 3: 47-58
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