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Brandon Ason, Ph.D. - Publications

Affiliations: 
2003 University of Wisconsin, Madison, Madison, WI 
Area:
Biochemical genetics; studies on the molecular mechanism of transposition
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6 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2005 Ason B, Knauss DJ, Balke AM, Merkel G, Skalka AM, Reznikoff WS. Targeting Tn5 transposase identifies human immunodeficiency virus type 1 inhibitors. Antimicrobial Agents and Chemotherapy. 49: 2035-43. PMID 15855529 DOI: 10.1128/Aac.49.5.2035-2043.2005  0.422
2004 Ason B, Reznikoff WS. A high-throughput assay for Tn5 Tnp-induced DNA cleavage. Nucleic Acids Research. 32: e83. PMID 15201394 DOI: 10.1093/Nar/Gnh080  0.564
2004 Ason B, Reznikoff WS. DNA sequence bias during Tn5 transposition. Journal of Molecular Biology. 335: 1213-25. PMID 14729338 DOI: 10.1016/J.Jmb.2003.11.039  0.549
2003 Ason B, Handayani R, Williams CR, Bertram JG, Hingorani MM, O'Donnell M, Goodman MF, Bloom LB. Mechanism of loading the Escherichia coli DNA polymerase III beta sliding clamp on DNA. Bona fide primer/templates preferentially trigger the gamma complex to hydrolyze ATP and load the clamp. The Journal of Biological Chemistry. 278: 10033-40. PMID 12519754 DOI: 10.1074/Jbc.M211741200  0.439
2002 Ason B, Reznikoff WS. Mutational analysis of the base flipping event found in Tn5 transposition. The Journal of Biological Chemistry. 277: 11284-91. PMID 11805107 DOI: 10.1074/Jbc.M111119200  0.538
2000 Ason B, Bertram JG, Hingorani MM, Beechem JM, O'Donnell M, Goodman MF, Bloom LB. A model for Escherichia coli DNA polymerase III holoenzyme assembly at primer/template ends. DNA triggers a change in binding specificity of the gamma complex clamp loader. The Journal of Biological Chemistry. 275: 3006-15. PMID 10644772 DOI: 10.1074/Jbc.275.4.3006  0.429
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