@article{marquez_harris_kelley_brown_dawson_roberts_pace_2005, title={Structural implications of novel diversity in eucaryal RNase P RNA}, volume={11}, number={5}, journal={RNA}, author={Marquez, S. M. and Harris, J. K. and Kelley, S. T. and Brown, J. W. and Dawson, S. C. and Roberts, E. C. and Pace, N. R.}, year={2005}, pages={739–751} }
 @article{harris_haas_williams_frank_brown_2001, title={New insight into RNase P RNA structure from comparative analysis of the archaeal RNA}, volume={7}, ISSN={["1469-9001"]}, DOI={10.1017/S1355838201001777}, abstractNote={A detailed comparative analysis of archaeal RNase P RNA structure and a comparison of the resulting structural information with that of the bacterial RNA reveals that the archaeal RNase P RNAs are strikingly similar to those of Bacteria. The differences between the secondary structure models of archaeal and bacterial RNase P RNA have largely disappeared, and even variation in the sequence and structure of the RNAs are similar in extent and type. The structure of the cruciform (P7-11) has been reevaluated on the basis of a total of 321 bacterial and archaeal sequences, leading to a model for the structure of this region of the RNA that includes an extension to P11 that consistently organizes the cruciform and adjacent highly-conserved sequences.}, number={2}, journal={RNA}, author={Harris, JK and Haas, ES and Williams, D and Frank, DN and Brown, JW}, year={2001}, month={Feb}, pages={220–232} }
 @article{pannucci_haas_hall_harris_brown_1999, title={RNase P RNAs from some Archaea are catalytically active}, volume={96}, ISSN={["0027-8424"]}, DOI={10.1073/pnas.96.14.7803}, abstractNote={
            The RNA subunits of RNase Ps of Archaea and eukaryotes have been thought to depend fundamentally on protein for activity, unlike those of Bacteria that are capable of efficient catalysis in the absence of protein. Although the eukaryotic RNase P RNAs are quite different than those of Bacteria in both sequence and structure, the archaeal RNAs generally contain the sequences and structures of the bacterial, phylogenetically conserved catalytic core. A spectrum of archaeal RNase P RNAs were therefore tested for activity in a wide range of conditions. Many remain inactive in ionically extreme conditions, but catalytic activity could be detected from those of the methanobacteria, thermococci, and halobacteria. Chimeric holoenzymes, reconstituted from the
            Methanobacterium
            RNase P RNA and the
            Bacillus subtilis
            RNase P protein subunits, were functional at low ionic strength. The properties of the archaeal RNase P RNAs (high ionic-strength requirement, low affinity for substrate, and catalytic reconstitution by bacterial RNase P protein) are similar to synthetic RNase P RNAs that contain all of the catalytic core of the bacterial RNA but lack phylogenetically variable, stabilizing elements.
          }, number={14}, journal={PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA}, author={Pannucci, JA and Haas, ES and Hall, TA and Harris, JK and Brown, JW}, year={1999}, month={Jul}, pages={7803–7808} }