@article{yamamoto_2012, title={Values, objectivity and credibility of scientists in a contentious natural resource debate}, volume={21}, number={1}, journal={Public Understanding of Science (Bristol, England)}, author={Yamamoto, Y. T.}, year={2012}, pages={101–125} }
 @article{sun_cheng_himmel_skory_adney_thomas_tisserat_nishimura_yamamoto_2007, title={Expression and characterization of Acidothermus cellulolyticus E1 endoglucanase in transgenic duckweed Lemna minor 8627}, volume={98}, ISSN={["0960-8524"]}, DOI={10.1016/j.biortech.2006.09.055}, abstractNote={Endoglucanase E1 from Acidothermus cellulolyticus was expressed cytosolically under control of the cauliflower mosaic virus 35S promoter in transgenic duckweed, Lemna minor 8627 without any obvious observable phenotypic effects on morphology or rate of growth. The recombinant enzyme co-migrated with the purified catalytic domain fraction of the native E1 protein on western blot analysis, revealing that the cellulose-binding domain was cleaved near or in the linker region. The duckweed-expressed enzyme was biologically active and the expression level was up to 0.24% of total soluble protein. The endoglucanase activity with carboxymethylcellulose averaged 0.2 units mg protein−1 extracted from fresh duckweed. The optimal temperature and pH for E1 enzyme activity were about 80 °C and pH 5, respectively. While extraction with HEPES (N-[2-hydroxyethyl]piperazine-N′-[2-ethanesulfonic acid]) buffer (pH 8) resulted in the highest recovery of total soluble proteins and E1 enzyme, extraction with citrate buffer (pH 4.8) at 65 °C enriched relative amounts of E1 enzyme in the extract. This study demonstrates that duckweed may offer new options for the expression of cellulolytic enzymes in transgenic plants.}, number={15}, journal={BIORESOURCE TECHNOLOGY}, author={Sun, Ye and Cheng, Jay J. and Himmel, Michael E. and Skory, Christopher D. and Adney, William S. and Thomas, Steven R. and Tisserat, Brent and Nishimura, Yufuko and Yamamoto, Yuri T.}, year={2007}, month={Nov}, pages={2866–2872} }
 @article{cheng_landesman_bergmann_classen_howard_yamamoto_2002, title={Nutrient removal from swine lagoon liquid by Lemna minor 8627}, volume={45}, DOI={10.13031/2013.9953}, abstractNote={Nitrogen and phosphorus removal from swine lagoon liquid by growing Lemna minor 8627, a promising duckweed 
identified in previous studies, was investigated under in vitro and field conditions. The rates of nitrogen and phosphorus 
uptake by the duckweed growing in the in vitro system were as high as 3.36 g m–2 day–1 and 0.20 g m–2 day–1, respectively. 
The highest nitrogen and phosphorus removal rates in the field duckweed system were 2.11 g m–2 day–1 and 0.59 g m–2 day–1, 
respectively. The highest observed duckweed growth rate was close to 29 g m–2 day–1 in both conditions. 
Wastewater concentrations and seasonal climate conditions had direct impacts on the duckweed growth and nutrient 
removal in outdoor tanks. The rate of duckweed production in diluted swine lagoon liquid increased as the dilution rate 
increased. Duckweed assimilation was the dominant mechanism for nitrogen and phosphorus removal from the swine lagoon 
liquid when the nutrient concentration in the wastewater was low, but became less important as nutrient concentration 
increased. Reasonably high light intensity and a longer period of warm temperature could result in a higher growth rate for 
the duckweed. Pre–acclimation of the duckweed with swine lagoon liquid could accelerate the start–up of a duckweed system 
to remove nutrients from the wastewater by preventing the lag phase of duckweed growth.}, number={4}, journal={Transactions of the ASAE}, author={Cheng, J. and Landesman, L. and Bergmann, Ben and Classen, J. J. and Howard, J. W. and Yamamoto, Y. T.}, year={2002}, pages={1003–1010} }
 @article{zamski_guo_yamamoto_pharr_williamson_2001, title={Analysis of celery (Apium graveolens) mannitol dehydrogenase (Mtd) promoter regulation in Arabidopsis suggests roles for MTD in key environmental and metabolic responses}, volume={47}, ISSN={["0167-4412"]}, DOI={10.1023/A:1012395121920}, abstractNote={Of the growing list of promising genes for plant improvement, some of the most versatile appear to be those involved in sugar alcohol metabolism. Mannitol, one of the best characterized sugar alcohols, is a significant photosynthetic product in many higher plants. The roles of mannitol as both a metabolite and an osmoprotectant in celery (Apium graveolens) are well documented. However, there is growing evidence that 'metabolites' can also have key roles in other environmental and developmental responses in plants. For instance, in addition to its other properties, mannitol is an antioxidant and may have significant roles in plant-pathogen interactions. The mannitol catabolic enzyme mannitol dehydrogenase (MTD) is a prime modulator of mannitol accumulation in plants. Because the complex regulation of MTD is central to the balanced integration of mannitol metabolism in celery, its study is crucial in clarifying the physiological role(s) of mannitol metabolism in environmental and metabolic responses. In this study we used transformed Arabidopsis to analyze the multiple environmental and metabolic responses of the Mtd promoter. Our data show that all previously described changes in Mtd RNA accumulation in celery cells mirrored changes in Mtd transcription in Arabidopsis. These include up-regulation by salicylic acid, hexokinase-mediated sugar down-regulation, and down-regulation by salt, osmotic stress and ABA. In contrast, the massive up-regulation of Mtd expression in the vascular tissues of salt-stressed Arabidopsis roots suggests a possible role for MTD in mannitol translocation and unloading and its interrelation with sugar metabolism.}, number={5}, journal={PLANT MOLECULAR BIOLOGY}, author={Zamski, E and Guo, WW and Yamamoto, YT and Pharr, DM and Williamson, JD}, year={2001}, pages={621–631} }
 @article{yamamoto_rajbhandari_lin_bergmann_nishimura_stomp_2001, title={Genetic transformation of duckweed Lemna gibba and Lemna minor}, volume={37}, DOI={10.1007/s11627-001-0062-6}, number={3}, journal={In Vitro Cellular & Developmental Biology. Plant}, author={Yamamoto, Y. T. and Rajbhandari, N. and Lin, X. H. and Bergmann, Ben and Nishimura, Y. and Stomp, A. M.}, year={2001}, pages={349–353} }
 @article{yamamoto_zamski_williamson_conkling_pharr_1997, title={Subcellular localization of celery mannitol dehydrogenase - A cytosolic metabolic enzyme in nuclei}, volume={115}, ISSN={["0032-0889"]}, DOI={10.1104/pp.115.4.1397}, abstractNote={Abstract}, number={4}, journal={PLANT PHYSIOLOGY}, author={Yamamoto, YT and Zamski, E and Williamson, JD and Conkling, MA and Pharr, DM}, year={1997}, month={Dec}, pages={1397–1403} }