@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}, 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}, abstractNote={TobRB7 is a cDNA isolated from a cDNA library constructed of tobacco root mRNA (1). It had been shown to be expressed specifically in roots, to be transcriptionally regulated, and to be encoded by a small gene family (1). The TobRB7-5A (a fulllength TobRB7 cDNA) nucleotide sequence data will appear in EMBL, Genbank, and DDBJ Nucleotide Sequence Databases under the accession number X54855. The deduced TobRB7 amino acid (250 amino acids, Mr=25,233) sequence initiated at the first ATG of the sequence. This putative initiation site agrees with the consensus sequence surrounding eucaryotic initiation sites (Kozac's rules) (2), is preceded by two in-frame termination codons and thus is the likely initiation codon. To examine the amino acid sequence of a TobRB7 homologue from another plant species, a cDNA library constructed of mRNA isolated from Arabidopsis roots was screened at low stringency. A full length counterpart of TobRB7, designated AtRB7, was isolated. The AtRB7 nucleotide sequence data will appear in EMBL, GenBank, and DDBJ Nucleotide Sequence Databases under the accession number X54854. The predicted TobRB7 and AtRB7 proteins exhibit high similarity to a number of protein sequences believed to function as membrane channels, including the mammalian lens fiber major intrinsic protein (MTP26) (3), a soybean peribacteriod membrane nodulin (Nod26) (4, 5), a membrane pore type protein of E. coli, the glycerol facilitator (glpF) (6), the Drosophila neurogenic protein big brain (bib) (7), and a tonoplast protein of soybean seed storage vacuoles (TIP) (8) (Fig. 1). Regions in which at least 3 of the 7 sequences exhibited amino acid identity are shaded.}, number={24}, journal={NUCLEIC ACIDS RESEARCH}, author={YAMAMOTO, YT and CHENG, CL and CONKLING, MA}, year={1990}, month={Dec}, pages={7449–7449} }