@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 degrees 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 degrees 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 duckweedidentified in previous studies, was investigated under in vitro and field conditions. The rates of nitrogen and phosphorusuptake by the duckweed growing in the in vitro system were as high as 3.36 g m2 day1 and 0.20 g m2 day1, respectively.The highest nitrogen and phosphorus removal rates in the field duckweed system were 2.11 g m2 day1 and 0.59 g m2 day1,respectively. The highest observed duckweed growth rate was close to 29 g m2 day1 in both conditions.<br><br>Wastewater concentrations and seasonal climate conditions had direct impacts on the duckweed growth and nutrientremoval in outdoor tanks. The rate of duckweed production in diluted swine lagoon liquid increased as the dilution rateincreased. Duckweed assimilation was the dominant mechanism for nitrogen and phosphorus removal from the swine lagoonliquid when the nutrient concentration in the wastewater was low, but became less important as nutrient concentrationincreased. Reasonably high light intensity and a longer period of warm temperature could result in a higher growth rate forthe duckweed. Preacclimation of the duckweed with swine lagoon liquid could accelerate the startup of a duckweed systemto 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}, 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 Mannitol dehydrogenase (MTD) is the first enzyme in mannitol catabolism in celery (Apium graveolens L. var dulce [Mill] Pers. Cv Florida 638). Mannitol is an important photoassimilate, as well as providing plants with resistance to salt and osmotic stress. Previous work has shown that expression of the celery Mtd gene is regulated by many factors, such as hexose sugars, salt and osmotic stress, and salicylic acid. Furthermore, MTD is present in cells of sink organs, phloem cells, and mannitol-grown suspension cultures. Immunogold localization and biochemical analyses presented here demonstrate that celery MTD is localized in the cytosol and nuclei. Although the cellular density of MTD varies among different cell types, densities of nuclear and cytosolic MTD in a given cell are approximately equal. Biochemical analyses of nuclear extracts from mannitol-grown cultured cells confirmed that the nuclear-localized MTD is enzymatically active. The function(s) of nuclear-localized MTD is unknown.}, 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} }