@article{yamamoto_2012, title={Values, objectivity and credibility of scientists in a contentious natural resource debate}, volume={21}, ISSN={["1361-6609"]}, DOI={10.1177/0963662510371435}, abstractNote={In contentious natural resource debates, the credibility of scientists is at risk. In this case study, citizens in contending communities and scientists in a forest management controversy constructed the scientists’ credibility differently. Shared values and views of the nature of science and objectivity were primary factors for constructing scientists’ credibility. Citizens who expected value-free, objective scientists to authenticate their knowledge were concerned about how the values of scientists on the opposite side affected research framing. Citizens who emphasized limited objectivity were less skeptical of scientists. Scientists acknowledged their values but defended their credibility in terms of professional standards, balance and resource constraints. In short, scientists’ credibility is relative because each individual has unique values and views of the nature of science and objectivity. Through a collaborative policymaking process, citizens and scientists should develop shared values and visions to reconstruct a temporary, intersubjective sense of credibility.}, number={1}, journal={PUBLIC UNDERSTANDING OF SCIENCE}, author={Yamamoto, Yuri T.}, year={2012}, month={Jan}, pages={101–125} }
 @inproceedings{sun_adney_bergmann_cheng_decker_freer_himmel_nishimura_skory_stomp_et al._2002, title={Expression of endoglucanase E1 in transgenic duckweed Lemna minor}, ISBN={1588293874}, booktitle={Biotechnology for fuels and chemicals : proceedings of the Twenty-Fourth Symposium on Biotechnology for Fuels and Chemicals, held April 28-May 1, 2002, in Gatlinburg, TN}, author={Sun, Y. and Adney, W. S. and Bergmann, B. A. and Cheng, J. and Decker, S. R. and Freer, S. and Himmel, M. E. and Nishimura, Y. and Skory, C. D. and Stomp, A.-M and et al.}, year={2002} }
 @article{yamamoto_prata_williamson_weddington_pharr_2000, title={Formation of a hexokinase complex is associated with changes in energy utilization in celery organs and cells}, volume={110}, ISSN={["0031-9317"]}, DOI={10.1034/j.1399-3054.2000.110104.x}, abstractNote={We previously presented evidence that the hexose-regulated repression of the mannitol catabolic enzyme mannitol dehydrogenase (MTD) in celery (Apium graveolens L.) may be mediated by hexokinase (EC 2.7.1.1) (HK) [Prata et al. (1997) Plant Physiol 114: 307–314]. To see if differential regulation of HK forms might be involved in the sugar-regulated repression of MTD we characterized two forms of HK with respect to their expression in various plant organs as well as in celery suspension cell cultures. We found that the vast majority of HK activity was membrane-associated, whereas fructokinase (EC 2.7.1.4) was found largely in the soluble cell fraction. Gel filtration chromatography further revealed the differential expression of two molecular size classes of HK. One HK (HK-L) chromatographed at 68 kDa, a typical size for a plant HK, while the second (HK-H) chromatographed at 280 kDa. This unique 280 kDa HK was shown to be composed of a 50 kDa HK protein, possibly complexed with other, as yet unidentified, components. The HK-L was present in all cells and organs analyzed, and thus may be a likely candidate for mediation of sugar repression. In contrast, the presence of the HK-H complex was specific to certain organs and cells grown under certain conditions. Our analyses here showed no correlation between the presence of the HK-H and MTD repression or derepression in celery cells. Instead, the HK-H complex was present exclusively in rapidly growing organs and cells, but not in non-growing celery storage tissues or in carbon-depleted celery suspension-cultured cells. Furthermore, the HK-H complex was present when Glc in the growth media was replaced with 2-deoxy Glc, a HK substrate that does not provide energy for growth and metabolism. These results imply that the HK-H complex may have a potentially unique role in the metabolism of rapidly growing celery cells, in particular, in hexose phosphorylation. We also found that mitochondria prepared from Glc-grown celery suspension-cultured cells contained substantial HK activity, and that oxygen uptake of these mitochondria was stimulated by Glc. These results are consistent with the hypothesis that mitochondrial localization of celery HK may play a role in rapid recycling of adenylate.}, number={1}, journal={PHYSIOLOGIA PLANTARUM}, author={Yamamoto, YT and Prata, RTN and Williamson, JD and Weddington, M and Pharr, DM}, year={2000}, month={Sep}, pages={28–37} }
 @article{pharr_prata_jennings_williamson_zamski_yamamoto_conkling_1999, title={Regulation of mannitol dehydrogenase: Relationship to plant growth and stress tolerance}, volume={34}, number={6}, journal={HortScience}, author={Pharr, D. M. and Prata, R. T. N. and Jennings, D. B. and Williamson, J. D. and Zamski, E. and Yamamoto, Y. T. and Conkling, M. A.}, year={1999}, pages={1027–1032} }
 @article{zamski_yamamoto_williamson_conkling_pharr_1996, title={Immunolocalization of mannitol dehydrogenase in celery plants and cells}, volume={112}, ISSN={["0032-0889"]}, DOI={10.1104/pp.112.3.931}, abstractNote={Abstract Immunolocalization of mannitol dehydrogenase (MTD) in celery (Apium graveolens L.) suspension cells and plants showed that MTD is a cytoplasmic enzyme. MTD was found in the meristems of celery root apices, in young expanding leaves, in the vascular cambium, and in the phloem, including sieve-element/companion cell complexes, parenchyma, and in the exuding phloem sap of cut petioles. Suspension cells that were grown in medium with mannitol as the sole carbon source showed a high anti-MTD cross-reaction in the cytoplasm, whereas cells that were grown in sucrose-containing medium showed little or no cross-reaction. Gel-blot analysis of proteins from vascular and nonvascular tissues of mature celery petioles showed a strong anti-MTD sera cross-reactive band, corresponding to the 40-kD molecular mass of MTD in vascular extracts, but no cross-reactive bands in nonvascular extracts. The distribution pattern of MTD within celery plants and in cell cultures that were grown on different carbon sources is consistent w ith the hypothesis that the Mtd gene may be regulated by sugar repression. Additionally, a developmental component may regulate the distribution of MTD within celery plants.}, number={3}, journal={PLANT PHYSIOLOGY}, author={Zamski, E and Yamamoto, YT and Williamson, JD and Conkling, MA and Pharr, DM}, year={1996}, month={Nov}, pages={931–938} }
 @misc{conkling_yamamoto_1995, title={Root specific gene promoter}, volume={5,459,252}, number={1995 Oct. 17}, publisher={Washington, DC: U.S. Patent and Trademark Office}, author={Conkling, M. A. and Yamamoto, Y. T.}, year={1995} }
 @article{yamamoto_taylor_acedo_cheng_conkling_1991, title={CHARACTERIZATION OF CIS-ACTING SEQUENCES REGULATING ROOT-SPECIFIC GENE-EXPRESSION IN TOBACCO}, volume={3}, ISSN={["1532-298X"]}, DOI={10.1105/tpc.3.4.371}, abstractNote={The expression of the tobacco root-specific gene TobRB7 was characterized. Gel blot hybridizations to RNA isolated from various tobacco tissues demonstrated that steady-state TobRB7 mRNA is not detected in expanded leaf, stem, or shoot apex tissue. To determine the spatial pattern of expression, in situ hybridization to root sections revealed that TobRB7 expression is localized to root meristem and immature central cylinder regions. The 5' flanking region of the gene was studied with respect to its ability to direct root-specific expression. Deletions of 5' flanking sequence were fused to the beta-glucuronidase (GUS) reporter gene and transformed into tobacco. Our data demonstrated that sequences 636 base pairs from the site of transcription initiation are sufficient to direct the root-specific GUS expression in transgenic tobacco, whereas sequences 299 base pairs from the site of transcription initiation fail to direct root-specific expression. A negative regulatory element was apparent between 813 base pairs and 636 base pairs 5' of the transcription initiation site. Histochemical localization of GUS activity in transgenic plants was consistent with in situ hybridization results: GUS activity was localized to the root meristem and central cylinder regions. GUS activity appeared 2 days post-germination in the primary root meristem. In lateral roots, GUS activity was detected from the time of initiation.}, number={4}, journal={PLANT CELL}, author={YAMAMOTO, YT and TAYLOR, CG and ACEDO, GN and CHENG, CL and CONKLING, MA}, year={1991}, month={Apr}, pages={371–382} }
 @article{yamamoto_cheng_conkling_1990, title={ROOT-SPECIFIC GENES FROM TOBACCO AND ARABIDOPSIS HOMOLOGOUS TO AN EVOLUTIONARILY CONSERVED GENE FAMILY OF MEMBRANE CHANNEL PROTEINS}, volume={18}, ISSN={["1362-4962"]}, DOI={10.1093/nar/18.24.7449}, number={24}, journal={NUCLEIC ACIDS RESEARCH}, author={YAMAMOTO, YT and CHENG, CL and CONKLING, MA}, year={1990}, month={Dec}, pages={7449–7449} }