@misc{boston_bass_obrian_1996, title={DNA encoding a ribosome inactivating protein}, volume={5552140}, publisher={Washington, DC: U.S. Patent and Trademark Office}, author={Boston, R. S. and Bass, H. W. and OBrian, G. R.}, year={1996} }
 @article{bass_obrian_boston_1995, title={CLONING AND SEQUENCING OF A 2ND RIBOSOME-INACTIVATING PROTEIN GENE FROM MAIZE (ZEA-MAYS L)}, volume={107}, ISSN={["0032-0889"]}, DOI={10.1104/pp.107.2.661}, abstractNote={Toxic proteins are among the wide array of antibiotic compounds produced by plants. Some of the most potent plant toxins belong to a class of translational inhibitors called RIPs (Stirpe et al., 1992). RIPs act as N-glycosidases to remove a specific adenine from the large rRNA, thereby irreversibly inactivating the ribosome. A maize Rip gene encodes a highly expressed seed-specific RIP (also called b-32 or proRIP) that accumulates under the control of the transcriptional activator, Opaque-2, as a nontoxic, singlechain zymogen (Soave et al., 1981; Walsh et al., 1991; Bass et al., 1992). During germination the RIP is proteolytically cleaved to an active form with two noncovalently linked chains of 8 and 16 kD (Walsh et al., 1991). A genomic library was screened with a cDNA clone for the seed RIP. This led to the isolation of a genomic clone for a second, nonallelic Rip gene from maize. The sequence of a 963-bp segment within this clone is described in Table I. This region includes an ORF that predicts a 31-kD polypeptide with 73% amino acid identity with maize seed proRIP. Among the residues shared are the five active site cleft residues found in a11 plant RIPs for which data are available (Bass et al., 1992). Genomic Southern analysis and recombinant inbred restriction fragment length polymorphism mapping results are consistent with a two-member Rip gene family. One member corresponds to the seed-specific Rip gene, which has been previously mapped by segregation analysis of allelic protein isoforms to chromosome 8L (Soave et al., 1981). The Rip gene described here corresponds to a second member that can be placed on chromosome 7L (Bass et al., 1990). The existence of multiple RIPs, and in some cases organ-specific isoforms, has also been observed in severa1 other plant species (Stirpe et al., 1992). We propose that the seed-specific Rip gene be designated Rip3:l for the first member of the maize Rip multigene family and that the gene described here be designated Rip3:2 (Mundy et al., 1994). Alignment of the deduced amino acid sequences of the two maize RIPs reveals little similarity in the regions cor-}, number={2}, journal={PLANT PHYSIOLOGY}, author={BASS, HW and OBRIAN, GR and BOSTON, RS}, year={1995}, month={Feb}, pages={661–662} }
 @article{bass_goode_greene_boston_1994, title={CONTROL OF RIBOSOME-INACTIVATING PROTEIN (RIP) RNA LEVELS DURING MAIZE SEED DEVELOPMENT}, volume={101}, ISSN={["0168-9452"]}, DOI={10.1016/0168-9452(94)90161-9}, abstractNote={The maize RIP1 gene encodes proRIP, the zymogen form of a ribosome-inactivating protein that accumulates to high levels in endosperm. ProRIP is synthesized coordinately with the major storage proteins and requires a functional allele of the transcriptional activator, Opaque-2 (O2)3 for maximal accumulation. RIP1 gene expression was characterized by developmental RNA gel blot analysis. RIP1 RNA was first detected at 10 days after pollination (DAP), and increased in abundance to reach maximal levels at mid-maturation of the kernel. In four W64A maize lines with independently-derived opaque-2 (o2) alleles, RIP1 RNA still accumulated in a developmentally specific pattern, but showed qualitative and quantitative changes from normal. RNA gel blots reprobed with an O2-specific probe provided evidence for coordinate accumulation of RIP1 and O2 RNAs throughout normal kernel development. The pleiotropic endosperm mutations brittle-1 (bt1), brittle-2 (bt2), shrunken-2 (sh2), sugary-2 (su2), Mucronate (Mc), Defective endosperm-B30 (De∗-B30), and floury-2 (fl2), affected RIP1 and O2 RNA accumulation to varying degrees. None of these mutations, however, resulted in RIP1 RNA reductions comparable to that seen in W64Ao2. When coupled with o2, bt1 and bt2 mutations showed synergistic interactions in their effects of reducing RIP1 RNA levels. Thus, RIP1 gene expression and relative RNA levels are controlled by multiple factors including O2, and o2-independent component(s), genetic background, and the presence of other pleiotropic mutations.}, number={1}, journal={PLANT SCIENCE}, author={BASS, HW and GOODE, JH and GREENE, TW and BOSTON, RS}, year={1994}, pages={17–30} }
 @misc{boston_bass_obrian_1994, title={DNA encoding a ribosome inactivating protein}, volume={5332808}, publisher={Washington, DC: U.S. Patent and Trademark Office}, author={Boston, R. S. and Bass, H. W. and OBrian, G. R.}, year={1994} }
 @article{bass_webster_obrian_roberts_boston_1992, title={A MAIZE RIBOSOME-INACTIVATING PROTEIN IS CONTROLLED BY THE TRANSCRIPTIONAL ACTIVATOR OPAQUE-2}, volume={4}, ISSN={["1040-4651"]}, DOI={10.1105/tpc.4.2.225}, abstractNote={Although synthesis of the cytosolic maize albumin b-32 had been shown to be controlled by the Opaque-2 regulatory locus, its function was unknown. We show here that b-32 is a member of the large and widely distributed class of toxic plant proteins with ribosome-inactivating activity. These ribosome-inactivating proteins (RIPs) are RNA N-glycosidases that remove a single base from a conserved 28S rRNA loop required for elongation factor 1 alpha binding. Cell-free in vitro translation extracts were used to show that both maize and wheat ribosomes were resistant to molar excesses of b-32 but not to the dicotyledonous RIP gelonin. We extracted RIP activity from kernels during seed maturation and germination. The amount of RIP activity increased during germination, although the amount of b-32 protein remained fairly constant. Expression of a maize RIP gene under the control of an endosperm-specific transcriptional regulatory may be an important clue prompting investigation of the biological basis for RIP expression in seeds of other plants.}, number={2}, journal={PLANT CELL}, author={BASS, HW and WEBSTER, C and OBRIAN, GR and ROBERTS, JKM and BOSTON, RS}, year={1992}, month={Feb}, pages={225–234} }
 @article{bass_sisco_murray_boston_1990, title={Probes for the b-32 protein hybridize to loci on 7L and 8L}, number={64}, journal={Maize Genetics Cooperation Newsletter}, author={Bass, H. W. and Sisco, P. H. and Murray, D. L. and Boston, R. S.}, year={1990}, pages={97} }