Michael E. Harris, Ph.D.

Associate Professor

Center for RNA molecular Biology /
Department of Biochemistry

More Publications

Harris, M.E. and Christian, E.L. (2004).
Probing RNA Structure by Photoaffinity Crosslinking With 4-Thiourine and 6-Thioguanosine.
in Handbook of RNA Biochemistry, Wiley. Hartmann, Binderief, Shon and Westhof, eds.

Zahler, N.H. and Harris, M.E. (2004).
Site-Specific Modification of RNA.
in Handbook of RNA Biochemistry, Wiley. Hartmann, Binderief, Shon and Westhof, eds.

Anderson, V.E., Cassano, A.G. and Harris, M.E. (2004).
Nucleophile Isotope Effects
in Isotope Effects, CRC Press.

Cassano, A.G., Anderson, V.E. and Harris, M.E. (2004).
Transition states of phosphodiester bond hydrolysis: Information from heavy atom isotope effects.
Biopolymers. 73, 110-129.

Zahler, N.H., Christian, E.L. and Harris, M.E. (2003).
Recognition of the 5' leader of pre-tRNA substrates by the active site of ribonuclease P.
RNA. 9, 734-745.

Kaye, N.M., Zahler, N.H., Christian, E.L. and Harris, M.E. (2002).
Conserved helix structure contributes to functional metal ion interactions in the catalytic domain of ribonuclease P RNA.
J. Molec Biol. 324(3):429-442.

Christian, E.L., Kaye, N.M., Zahler, N.H and Harris, M.E. (2002).
Analysis of substrate recognition by the ribonucleoprotein endonuclease RNase P.
Methods 28, 307-322.

Kaye, N. M., Christian, E. L. and Harris, M. E. (2002).
NAIM and site-specific functional group modification analysis of the RNase P ribozyme: Magnesium dependent structure in the P1-P4 multi-helix junction contributes to catalysis.
Biochemistry 41, 4533-4545.

Campbell, F. E., Cassano, A. G., Anderson, V. and Harris, M. E. (2002).
Pre-steady state and stopped flow fluorescence analysis of E. coli RNase III: Insights into mechanism and conformational changes associated with binding and catalysis.
J Molec Biol. 317, 21-40.

Christian, E.L., Kaye, N.M. and Harris, M.E. (2000).
Helix P4 is a divalent metal ion binding site in the conserved core of the ribonuclease P ribozyme.
RNA. 6, 511-519.