@article{alejos-gonzalez_qu_zhou_saravitz_shurtleff_xie_2011, title={Characterization of development and artemisinin biosynthesis in self-pollinated Artemisia annua plants}, volume={234}, ISSN={["1432-2048"]}, DOI={10.1007/s00425-011-1430-z}, number={4}, journal={PLANTA}, author={Alejos-Gonzalez, Fatima and Qu, Guosheng and Zhou, Li-Li and Saravitz, Carole H. and Shurtleff, Janet L. and Xie, De-Yu}, year={2011}, month={Oct}, pages={685–697} }
 @article{qu_nues_watkins_maxwell_2011, title={The Spatial-Functional Coupling of Box C/D and C '/D ' RNPs Is an Evolutionarily Conserved Feature of the Eukaryotic Box C/D snoRNP Nucleotide Modification Complex}, volume={31}, ISSN={["1098-5549"]}, DOI={10.1128/mcb.00918-10}, abstractNote={Box C/D ribonucleoprotein particles guide the 2'-O-ribose methylation of target nucleotides in both archaeal and eukaryotic RNAs. These complexes contain two functional centers, assembled around the C/D and C'/D' motifs in the box C/D RNA. The C/D and C'/D' RNPs of the archaeal snoRNA-like RNP (sRNP) are spatially and functionally coupled. Here, we show that similar coupling also occurs in eukaryotic box C/D snoRNPs. The C/D RNP guided 2'-O-methylation when the C'/D' motif was either mutated or ablated. In contrast, the C'/D' RNP was inactive as an independent complex. Additional experiments demonstrated that the internal C'/D' RNP is spatially coupled to the terminal box C/D complex. Pulldown experiments also indicated that all four core proteins are independently recruited to the box C/D and C'/D' motifs. Therefore, the spatial-functional coupling of box C/D and C'/D' RNPs is an evolutionarily conserved feature of both archaeal and eukaryotic box C/D RNP complexes.}, number={2}, journal={MOLECULAR AND CELLULAR BIOLOGY}, author={Qu, Guosheng and Nues, Rob W. and Watkins, Nicholas J. and Maxwell, E. Stuart}, year={2011}, month={Jan}, pages={365–374} }
 @article{gagnon_zhang_qu_biswas_suryadi_brown_maxwell_2010, title={Signature amino acids enable the archaeal L7Ae box C/D RNP core protein to recognize and bind the K-loop RNA motif}, volume={16}, ISSN={["1469-9001"]}, DOI={10.1261/rna.1692310}, abstractNote={The archaeal L7Ae and eukaryotic 15.5kD protein homologs are members of the L7Ae/15.5kD protein family that characteristically recognize K-turn motifs found in both archaeal and eukaryotic RNAs. In Archaea, the L7Ae protein uniquely binds the K-loop motif found in box C/D and H/ACA sRNAs, whereas the eukaryotic 15.5kD homolog is unable to recognize this variant K-turn RNA. Comparative sequence and structural analyses, coupled with amino acid replacement experiments, have demonstrated that five amino acids enable the archaeal L7Ae core protein to recognize and bind the K-loop motif. These signature residues are highly conserved in the archaeal L7Ae and eukaryotic 15.5kD homologs, but differ between the two domains of life. Interestingly, loss of K-loop binding by archaeal L7Ae does not disrupt C'/D' RNP formation or RNA-guided nucleotide modification. L7Ae is still incorporated into the C'/D' RNP despite its inability to bind the K-loop, thus indicating the importance of protein-protein interactions for RNP assembly and function. Finally, these five signature amino acids are distinct for each of the L7Ae/L30 family members, suggesting an evolutionary continuum of these RNA-binding proteins for recognition of the various K-turn motifs contained in their cognate RNAs.}, number={1}, journal={RNA}, author={Gagnon, Keith T. and Zhang, Xinxin and Qu, Guosheng and Biswas, Shyamasri and Suryadi, Jimmy and Brown, Bernard A., II and Maxwell, E. Stuart}, year={2010}, month={Jan}, pages={79–90} }