@article{watkins_newman_kuhn_maxwell_1998, title={In vitro assembly of the mouse U14 snoRNP core complex and identification of a 65-kDa box C/D-binding protein}, volume={4}, ISSN={["1469-9001"]}, DOI={10.1017/S1355838298980128}, abstractNote={The eukaryotic nucleolus contains a diverse population of small nucleolar RNAs (snoRNAs) that have been categorized into two major families based on evolutionarily conserved sequence elements. U14 snoRNA is a member of the larger, box C/D snoRNA family and possesses nucleotide box C and D consensus sequences. In previous studies, we have defined a U14 box C/D core motif that is essential for intronic U14 snoRNA processing. These studies also revealed that nuclear proteins that recognize boxes C/D are required. We have now established an in vitro U14 snoRNP assembly system to characterize protein binding. Electrophoretic mobility-shift analysis demonstrated that all the sequences and structures of the box C/D core motif required for U14 processing are also necessary for protein binding and snoRNP assembly. These required elements include a base paired 5',3' terminal stem and the phylogenetically conserved nucleotides of boxes C and D. The ability of other box C/D snoRNAs to compete for protein binding demonstrated that the box C/D core motif-binding proteins are common to this family of snoRNAs. UV crosslinking of nuclear proteins bound to the U14 core motif identified a 65-kDa mouse snoRNP protein that requires boxes C and D for binding. Two additional core motif proteins of 55 and 50 kDa were also identified by biochemical fractionation of the in vitro-assembled U14 snoRNP complex. Thus, the U14 snoRNP core complex is a multiprotein particle whose assembly requires nucleotide boxes C and D.}, number={5}, journal={RNA}, author={Watkins, NJ and Newman, DR and Kuhn, JF and Maxwell, ES}, year={1998}, month={May}, pages={582–593} }
 @article{leader_clark_boag_watters_simpson_watkins_maxwell_brown_1998, title={Processing of vertebrate box C/D small nucleolar RNAs in plant cells}, volume={253}, ISSN={["0014-2956"]}, DOI={10.1046/j.1432-1327.1998.2530154.x}, abstractNote={The recent isolation of a number of plant box C/D small nucleolar (sno)RNAs demonstrates the conservation in plants of sequence and structural elements of processed box C/D snoRNAs. Boxes C and D, and terminal inverted repeats are known to be essential for accumulation and processing in vertebrates and yeast. Processing of vertebrate box C/D snoRNAs was examined by expression of various mouse hsc70 intron 5‐U14 constructs in tobacco protoplasts. Full‐length U14 and internally deleted U14 accumulated in the plant cells. Human U3 and U8 fragments, consistent with processing to internal box C/C′ sequences, also accumulated in the plant cells. The similarity of processing behaviour of the vertebrate box C/D constructs in tobacco protoplasts and Xenopus oocytes suggests the mechanism of processing, involving recognition and association of proteins, is conserved in plants.}, number={1}, journal={EUROPEAN JOURNAL OF BIOCHEMISTRY}, author={Leader, DJ and Clark, GP and Boag, J and Watters, JA and Simpson, CG and Watkins, NJ and Maxwell, ES and Brown, JWS}, year={1998}, month={Apr}, pages={154–160} }
 @article{xia_watkins_maxwell_1997, title={Identification of specific nucleotide sequences and structural elements required for intronic U14 snorna processing}, volume={3}, number={1}, journal={RNA}, author={Xia, L. and Watkins, N. J. and Maxwell, E. S.}, year={1997}, pages={17–26} }