@article{im_ji_lee_killens_grunden_boss_2009, title={Expression of Pyrococcus furiosus Superoxide Reductase in Arabidopsis Enhances Heat Tolerance}, volume={151}, ISSN={["1532-2548"]}, DOI={10.1104/pp.109.145409}, abstractNote={Abstract}, number={2}, journal={PLANT PHYSIOLOGY}, author={Im, Yang Ju and Ji, Mikyoung and Lee, Alice and Killens, Rushyannah and Grunden, Amy M. and Boss, Wendy F.}, year={2009}, month={Oct}, pages={893–904} }
 @article{lee_sevinsky_bundy_grunden_stephenson_2009, title={Proteomics of Pyrococcus furiosus, a Hyperthermophilic Archaeon Refractory to Traditional Methods}, volume={8}, ISSN={["1535-3907"]}, DOI={10.1021/pr801119h}, abstractNote={Pyrococcus furiosus is one of the most extensively studied hyperthermophilic archaea. Proteins from this hyperthemophile organism are extremely thermostable and are highly resistant to chemical denaturants, organic solvents and proteolytic digestion. This thermostability makes it difficult to apply traditional methods of enzymatically digesting a complex mixture of proteins, commonly a first step in peptide generation in most shotgun proteomics methods. Here, we have developed a simple shotgun proteomics approach for the global identification of the P. furiosus proteome. This methodology uses a detergent-based microwave assisted acid hydrolysis (MAAH) step coupled with an overnight trypsin digest to obtain peptides. Subsequent peptide fractionation by isoelectric focusing in immobilized pH gradients (IPG-IEF), followed by chromatographic separation with reverse phase nano-HPLC and electrospray ionization tandem mass spectrometry (ESI-MS/MS) of peptides enabled the identification of over 900 proteins representing over 44% of the proteome. In most functional classes, over 50% of the predicted proteins were identified, including a number of membrane proteins. This new sample preparation technique will enable extensive proteomics data to be obtained for this organism, thereby enabling the reconstruction of metabolic pathways and promoting a systems biology based understanding of this important extremophile.}, number={8}, journal={JOURNAL OF PROTEOME RESEARCH}, author={Lee, Alice M. and Sevinsky, Joel R. and Bundy, Jonathan L. and Grunden, Amy M. and Stephenson, James L., Jr.}, year={2009}, month={Aug}, pages={3844–3851} }
 @article{lee_seyam_hodge_oxenham_grant_2007, title={Warp breaks detection in Jacquard weaving using MEMS: System development}, volume={98}, ISSN={["0040-5000"]}, url={http://www.scopus.com/inward/record.url?eid=2-s2.0-35348829713&partnerID=MN8TOARS}, DOI={10.1080/00405000701462559}, abstractNote={Abstract Research related to warp breaks has been limited to monitoring break frequency and the reason associated with breaks in order to improve warp yarn quality. While this approach led to improvement in weaving efficiency, warp breaks still represent a major problem, especially for today's high-speed weaving machines. Researchers have been trying to develop commercial automated systems to repair warp breaks with no success. The goal of this study is to explore inexpensive methods to detect warp breaks using nontraditional technique that would pave the way to automate warp break repair. To achieve the goal, a system that can detect warp breaks using MEMS accelerometers as sensors was developed for Jacquard weaving. The MEMS accelerometers were mounted on harness cords of a Jacquard tie. MEMS output acceleration signals components in the vertical and horizontal directions were analysed using time and frequency domains. The signals were acquired while warp ends are running and at the moment of intentional breaks. The analysis led to a successful detection of warp breaks, especially using the horizontal acceleration component that is mainly due to harness cord vibration.}, number={3}, journal={JOURNAL OF THE TEXTILE INSTITUTE}, author={Lee, J. H. and Seyam, A. M. and Hodge, G. and Oxenham, W. and Grant, E.}, year={2007}, pages={275–280} }
 @article{im_ji_lee_boss_grunden_2005, title={Production of a thermostable archaeal superoxide reductase in plant cells}, volume={579}, ISSN={["1873-3468"]}, DOI={10.1016/j.febslet.2005.09.015}, abstractNote={
Pyrococcus furiosus superoxide reductase (SOR) is a thermostable archaeal enzyme that reduces superoxide without producing oxygen. When produced as a fusion protein with the green fluorescent protein in plant cells, P. furiosus SOR is located in the cytosol and nucleus. The recombinant SOR enzyme retains its function and heat stability when assayed in vitro. Importantly, expressing SOR in plant cells enhances their survival at high temperature indicating that it functions in vivo. The archaeal SOR provides a novel mechanism to reduce superoxide and demonstrates the potential for using archaeal genes to alter eukaryotic metabolism.}, number={25}, journal={FEBS LETTERS}, author={Im, YJ and Ji, MK and Lee, AM and Boss, WF and Grunden, AM}, year={2005}, month={Oct}, pages={5521–5526} }