Matthew J. Harley, Ph.D.
Affiliations: | 2004 | Johns Hopkins University, Baltimore, MD |
Area:
Biochemistry, Molecular BiologyGoogle:
"Matthew Harley"Parents
Sign in to add mentor| Joel F. Schildbach | grad student | 2004 | Johns Hopkins | |
| (The determination of functional amino acid residues for F TraI relaxase activity and specificity.) | ||||
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Publications
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| Larkin C, Haft RJ, Harley MJ, et al. (2007) Roles of active site residues and the HUH motif of the F plasmid TraI relaxase. The Journal of Biological Chemistry. 282: 33707-13 |
| Larkin C, Datta S, Harley MJ, et al. (2005) Inter- and intramolecular determinants of the specificity of single-stranded DNA binding and cleavage by the F factor relaxase Structure. 13: 1533-1544 |
| Harley MJ, Schildbach JF. (2003) Swapping single-stranded DNA sequence specificities of relaxases from conjugative plasmids F and R100. Proceedings of the National Academy of Sciences of the United States of America. 100: 11243-8 |
| Street LM, Harley MJ, Stern JC, et al. (2003) Subdomain organization and catalytic residues of the F factor TraI relaxase domain. Biochimica Et Biophysica Acta. 1646: 86-99 |
| Harley MJ, Toptygin D, Troxler T, et al. (2002) R150A mutant of F TraI relaxase domain: reduced affinity and specificity for single-stranded DNA and altered fluorescence anisotropy of a bound labeled oligonucleotide. Biochemistry. 41: 6460-8 |
| Hammond GL, Underhill DA, Smith CL, et al. (1987) The cDNA-deduced primary structure of human sex hormone-binding globulin and location of its steroid-binding domain. Febs Letters. 215: 100-4 |
| Hammond GL, Smith CL, Goping IS, et al. (1987) Primary structure of human corticosteroid binding globulin, deduced from hepatic and pulmonary cDNAs, exhibits homology with serine protease inhibitors. Proceedings of the National Academy of Sciences of the United States of America. 84: 5153-7 |