@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} }