Team:Calgary/Notebook/References

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<h1>References</h1>
<h1>References</h1>
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<li>Apostolovic, B., & Klok, H.-A. (2008). pH-sensitivity of the E3/K3 heterodimeric coiled coil. <i>Biomacromolecules, 9</i>(11), 3173–80. doi:10.1021/bm800746e</li>
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<h3>Our Project</h3>
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<li>Belson, K., Fahim, K. (2007, October 6) After extensive beef recall, Topps goes out of business. <i>The New York Times</i>. Retrieved from http://www.nytimes.com/2007/10/06/us/06topps.html?pagewanted=all&_r=0</li>
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<li>CBC News. (2010, May 10) Inside Walkerton: Canada's worst ever <i>E. coli</i> contamination: the shock, the investigation and the aftermath. <i>CBC News</i></li>
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<li>Centers for Disease Control and Prevention. (2011) Enterohemorrhagic <i>Escherichia coli</i>. Retrieved from http://www.cdc.gov/ecoli/general/</li>
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<li>Chase-Topping, M., Gally, D., Low, C., Matthews, L., Woolhouse, M. (2008). Super-shedding and the link between human infection and livestock carriage of <i>Escherichia coli</i> O157. <i>Nature Reviews Microbiology</i>, 6(12):904-12. doi: 10.1038/nrmicro2029</li>
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<li> Cross, A. (2012, October 2) Most extensive beef recall in Canadian history expanded again. <i>National Post</i>.</li>
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<li>FOA/WHO (Food and Agriculture Organization of the United Nations/World Health Organization). (2011) Enterohaemorrhagic <i>Escherichia coli</i> in raw beef and beef product: approaches for the provision of scientific advice. <i>Microbial Risk Assessment Series No 18.</i> Geneva. 126pp.</li>
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<li>Food Safety News. (2012, August 27) <i>E. coli</i> outbreak linked to Australian petting zoo sickens 12. Retrieved from http://www.foodsafetynews.com/2013/08/e-coli-outbreak-at-australian-petting-zoo-sickens-12/#.Um7YCpTTXTg</li>
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<li>Hernandez, J., Prado, V., Torres, D., Waldenström, J., Haemig, P. D., Olsen, B. (2007) Enteropathogenic <i>Escherichia coli</i> (EPEC) in Antarctic fur seals <i>Arctocephalus gazella</i>. <i>Polar Biology</i>. doi:10.1007/s00300-007-0282-2</li>
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<li>Junillon, T., Vimont, A., Mosticone, D., Mallen, B., Baril, F., Rozand, C., Flandrois, J. P. (December 2012). Simplified detection of food-borne pathogens: an in situ high affinity capture and staining concept. <i>Journal of Microbial Methods</i> 91(3), 501-505. doi: 10.1016/j.mimet.2012.09.015</li>
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<li>Mermin, J. H., Griffin, P. M. (1999) Invited commentary: public health: outbreaks of <i>Escherichia coli</i> O157:H7 infections in Japan. <i>American Journal of Epidemiology.</i>  150(8), 797-803.</li>
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<li>Okeke, I. (2009). Diarrheagenic <i>Escherichia coli</i> in sub-Saharan Africa: status, uncertainties and necessities. <i>The Journal Of Infection In Developing Countries</i>, 3(11), 817-842. doi:10.3855/jidc.586</li>
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<li>Russo, T. A., Johnson, J. R. (2003) Medical and economic impact of extraintestinal infections due to <i>Escherichia coli</i>: focus on an increasingly important endemic problem. <i>Microbes and Infection.</i> 5(5), 449-456.</li>
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<li>World Health Organization. (2011) <i>Outbreak of E. coli O104:h4 infection: update 30</i>. Retrieved from http://www.euro.who.int/en/health-topics/disease-prevention/food-safety/news/news/2011/07/outbreaks-of-e.-coli-o104h4-infection-update-30</li>
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<li>Beurdeley, M., Bietz, F., Li, J., Thomas, S., Stoddard, T., Juillerat, A., … Silva, G. H. (2013). Compact designer TALENs for efficient genome engineering. <i>Nature communications, 4</i>, 1762. doi:10.1038/ncomms2782</li>
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<h3>Detector</h3>
<li>Boch, J., Scholze, H., Schornack, S., Landgraf, A., Hahn, S., Kay, S., … Bonas, U. (2009). Breaking the code of DNA binding specificity of TAL-type III effectors. <i>Science (New York, N.Y.), 326</i>(5959), 1509–12. doi:10.1126/science.1178811</li>
<li>Boch, J., Scholze, H., Schornack, S., Landgraf, A., Hahn, S., Kay, S., … Bonas, U. (2009). Breaking the code of DNA binding specificity of TAL-type III effectors. <i>Science (New York, N.Y.), 326</i>(5959), 1509–12. doi:10.1126/science.1178811</li>
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<li>Bogdanove, A. J., Schornack, S., & Lahaye, T. (2010). TAL effectors: finding plant genes for disease and defense. <i>Current opinion in plant biology, 13</i>(4), 394–401. doi:10.1016/j.pbi.2010.04.010</li>
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<li>Bogdanove, A. J., Schornack, S., & Lahaye, T. (2010). TAL effectors: finding plant genes for disease and defense. <i>Current Opinion in Plant Biology, 13</i>(4), 394–401. doi:10.1016/j.pbi.2010.04.010</li>
<li>Bogdanove, A. J., & Voytas, D. F. (2011). TAL effectors: customizable proteins for DNA targeting. <i>Science (New York, N.Y.), 333</i>6051), 1843–6. doi:10.1126/science.1204094</li>
<li>Bogdanove, A. J., & Voytas, D. F. (2011). TAL effectors: customizable proteins for DNA targeting. <i>Science (New York, N.Y.), 333</i>6051), 1843–6. doi:10.1126/science.1204094</li>
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<li>Bushart, S., Bradbury, D., Elder, G., Duffield, J., Pascual, I., & Ratcliffe, N. (2006). The Development of Magnetic Molecules for the Selective Removal of Contaminents. In <i>Waste Management Conference</i>. Tuczon, AZ. Retrieved from http://www.wmsym.org/archives/2006/pdfs/6190.pdf </li>
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<li>Cong, L., Zhou, R., Kuo, Y., Cunniff, M., & Zhang, F. (2013). Comprehensive interrogation of natural TALE DNA-binding modules and transcriptional repressor domains. <i>Nature Communications</i>. doi:10.1038/ncomms1962.Comprehensive</li>
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<li>Cong, L., Zhou, R., Kuo, Y., Cunniff, M., & Zhang, F. (2013). Comprehensive interrogation of natural TALE DNA-binding modules and transcriptional repressor domains. <i>Nature communications</i>. doi:10.1038/ncomms1962.Comprehensive</li>
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<li>Meckler, J.F., Bhakta, M.S., Kim, M.S., Ovadia, R., Habrian, C.H., Zykovich, A., ... Baldwin, E.P. (2013). Quantitative analysis of TALE-DNA interactions suggests polarity effects. <i>Nucleic Acids Research</i>, 41(7), 4118–28. doi:10.1093/nar/gkt085</li>
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<li>De Lange, O., Schreiber, T., Schandry, N., Radeck, J., Braun, K. H., Koszinowski, J., … Lahaye, T. (2013). Breaking the DNA-binding code of Ralstonia solanacearum TAL effectors provides new possibilities to generate plant resistance genes against bacterial wilt disease. <i>The New phytologist, 199</i>(3), 773–86. doi:10.1111/nph.12324</li>
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<li>Mussolino, C., & Cathomen, T. (2012). TALE nucleases: tailored genome engineering made easy. <i>Current Opinion in Biotechnology, 23</i>(5), 644–50. doi:10.1016/j.copbio.2012.01.013</li>
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<li>Dörner, M. H., Salfeld, J., Will, H., Leibold, E. A., Vass, J. K., & Munro, H. N. (1985). Structure of human ferritin light subunit messenger RNA: comparison with heavy subunit message and functional implications. <i>Proceedings of the National Academy of Sciences of the United States of America</i>, 82(10), 3139–43. Retrieved from http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=397730&tool=pmcentrez&rendertype=abstract</li>
 
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<li>Ford, A. G. C., Harrison, P. M., Rice, D. W., Smith, J. M. A., Treffry, A., White, J. L., & Yariv, J. (2013). Ferritin : Design and Formation of an Iron-Storage Molecule Source : Philosophical Transactions of the Royal Society of London . Series B , Biological Sciences , Vol . 304 , No . 1121 , Mineral Phases in Biology ( Feb . 13 , 1984 ), pp . 551-565 Published by : The Royal Society Stable URL : http://www.jstor.org/stable/2396121 . IRON OXIDES ,, 304(1121), 551–565.</li>
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<h3>Prussian Blue</h3>
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<li>Ford, A. G. C., Harrison, P. M., Rice, D. W., Smith, J. M. A., Treffry, A., White, J. L., & Yariv, J. (1984). Ferritin : design and formation of an iron-storage molecule source . <i>Philosophical Transactions of the Royal Society of London Series B, Biological Sciences</i>, 304(1121), 551-65. Retrieved from http://www.jstor.org/stable/2396121</li>
<li>Harrison, P.-M., & Arosio, P. (1996). The ferritins: molecular properties, iron storage function and cellular regulation. <i>Biochimica et Biophysica Acta, 1275</i>(3), 161-203. doi:10.1016/0005-2728(96)00022-9</li>
<li>Harrison, P.-M., & Arosio, P. (1996). The ferritins: molecular properties, iron storage function and cellular regulation. <i>Biochimica et Biophysica Acta, 1275</i>(3), 161-203. doi:10.1016/0005-2728(96)00022-9</li>
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<li>He, Y., Zhang, S., Zhang, X., Baloda, M., Gurung, A. S., Xu, H., … Liu, G. (2011). Ultrasensitive nucleic acid biosensor based on enzyme-gold nanoparticle dual label and lateral flow strip biosensor.<i> Biosensors & bioelectronics</i>, 26(5), 2018–24. doi:10.1016/j.bios.2010.08.079</li>
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<li>Lawson, D. M., Artymiuk, P. J., Yewdall, S. J., Smith, J. M., Livingstone, J. C., Treffry, A., Luzzago, A., Levi, S., Arosio, P., Cesareni, G. (1991). Solving the structure of human H ferritin by genetically engineering intermolecular crystal contacts. <i>Nature, 349</i>(6309), 541–4. doi:10.1038/349541a0</li>
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<li>Ingrassia, R., Gerardi, G., Biasiotto, G., & Arosio, P. (2006). Mutations of ferritin H chain C-terminus produced by nucleotide insertions have altered stability and functional properties. <i>Journal of biochemistry</i>, 139(5), 881–5. doi:10.1093/jb/mvj101</li>
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<li>Huh, Y. S., & Kim, I. H. (2003). Purification of fusion ferritin from recombinant E. coli using two-step sonications. <i>Biotechnology letters</i>, 25(12), 993–6. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/12889837</li>
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<li>Munro, H.N. (1990). Iron regulation of ferritin gene expression. <i>Journal of Cellular Biochemistry</i> 44(2), 107-115.</li>
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<li>Zhang, W., Zhang, Y., Chen, Y., Li, S., Gu, N., Hu, S., Sun, Y., Chen, X., & Li, Q. (2013). Prussian blue modified ferritin as peroxidase mimetics and its applications in biological detection, <i>Journal of Nanoscience and Nanotechnology, 12</i>, 1–8. doi:10.1166/jnn.2012.6871</li>
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<li>Zhang, X.-Q., Gong, S.-W., Zhang, Y., Yang, T., Wang, C.-Y., & Gu, N. (2010). Prussian blue modified iron oxide magnetic nanoparticles and their high peroxidase-like activity. <i>Journal of Materials Chemistry, 20</i>(24), 5110. doi:10.1039/c0jm00174k</li>
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<li>Jordan, V. C., Caplan, M. R., & Bennett, K. M. (2010). Simplified synthesis and relaxometry of magnetoferritin for magnetic resonance imaging. <i>Magnetic resonance in medicine : official journal of the Society of Magnetic Resonance in Medicine / Society of Magnetic Resonance in Medicine</i>, 64(5), 1260–6. doi:10.1002/mrm.22526</li>
 
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<li>Kim, S.-E., Ahn, K.-Y., Park, J.-S., Kim, K. R., Lee, K. E., Han, S.-S., & Lee, J. (2011). Fluorescent ferritin nanoparticles and application to the aptamer sensor. <i>Analytical chemistry, 83</i>(15), 5834–43. doi:10.1021/ac200657s</li>
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<h3>Beta-Lactamase</h3>
<li>Kong, Y., Yao, H., Ren, H., Subbian, S., Cirillo, S. L. G., Sacchettini, J. C., … Cirillo, J. D. (2010). Imaging tuberculosis with endogenous beta-lactamase reporter enzyme fluorescence in live mice. <i>Proceedings of the National Academy of Sciences of the United States of America, 107</i>(27), 12239–44. doi:10.1073/pnas.1000643107</li>
<li>Kong, Y., Yao, H., Ren, H., Subbian, S., Cirillo, S. L. G., Sacchettini, J. C., … Cirillo, J. D. (2010). Imaging tuberculosis with endogenous beta-lactamase reporter enzyme fluorescence in live mice. <i>Proceedings of the National Academy of Sciences of the United States of America, 107</i>(27), 12239–44. doi:10.1073/pnas.1000643107</li>
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<li>Lawson, D. M., Artymiuk, P. J., Yewdall, S. J., Smith, J. M., Livingstone, J. C., Treffry, A., Luzzago, A., Levi, S., Arosio, P., Cesareni, G. (1991). Solving the structure of human H ferritin by genetically engineering intermolecular crystal contacts. <i>Nature, 349</i>(6309), 541–4. doi:10.1038/349541a0</li>
+
<li>Moore, J.T., Davis, S.T., & Dev, I.K. (1997). The development of beta-lactamase as a highly versatile genetic reporter for eukaryotic cells. <i>Analytical Biochemistry, 247</i>(2), 203–9. doi:10.1006/abio.1997.2092</li>
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<li>Lee, J., Kim, S. W., Kim, Y. H., & Ahn, J. Y. (2002). Active human ferritin H/L-hybrid and sequence effect on folding efficiency in Escherichia coli. <i>Biochemical and biophysical research communications</i>, 298(2), 225–9. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/12387819</li>
+
<li>Qureshi, S. (2007). β-Lactamase: an ideal reporter system for monitoring gene expression in live eukaryotic cells. <i>BioTechniques, 42</i>(1), 91–96. doi:10.2144/000112292</li>
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<li>Levi, S., Corsi, B., Rovida, E., Cozzi, A., Santambrogio, P., Albertini, A., & Arosio, P. (1994). Construction of a ferroxidase center in human ferritin L-chain. <i>The Journal of biological chemistry</i>, 269(48), 30334–9. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/7982945</li>
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<li>Remy, I., Ghaddar, G., & Michnick, S. W. (2007). Using the beta-lactamase protein-fragment complementation assay to probe dynamic protein-protein interactions. <i>Nature Protocols, 2</i>(9), 2302–6. doi:10.1038/nprot.2007.356</li>
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<li>Li, D., Yang, M., Hu, J., Zhang, Y., Chang, H., & Jin, F. (2008). Determination of penicillin G and its degradation products in a penicillin production wastewater treatment plant and the receiving river. <i>Water research, 42</i>(1-2), 307–17. doi:10.1016/j.watres.2007.07.016</li>
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<li>Wehrman, T., Kleaveland, B., Her, J.-H., Balint, R. F., & Blau, H. M. (2002). Protein-protein interactions monitored in mammalian cells via complementation of beta -lactamase enzyme fragments. <i>Proceedings of the National Academy of Sciences of the United States of America, 99</i>(6), 3469–74. doi:10.1073/pnas.062043699</li>
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<li>Litowski, J. R., & Hodges, R. S. (2002). Designing heterodimeric two-stranded alpha-helical coiled-coils. Effects of hydrophobicity and alpha-helical propensity on protein folding, stability, and specificity. <i>The Journal of biological chemistry, 277</i>(40), 37272–9. doi:10.1074/jbc.M204257200</li>
 
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<li>Lohsse, A., Ullrich, S., Katzmann, E., Borg, S., Wanner, G., Richter, M., … Schüler, D. (2011). Functional analysis of the magnetosome island in Magnetospirillum gryphiswaldense: the mamAB operon is sufficient for magnetite biomineralization. <i>PloS one</i>, 6(10), e25561. doi:10.1371/journal.pone.0025561</li>
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<h3>Linker</h3>
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<li>Luzzago, A., & Cesareni, G. (1989). Isolation of point mutations that affect the folding of the H chain of human ferritin in E.coli. <i>The EMBO journal</i>, 8(2), 569–76. Retrieved from http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=400843&tool=pmcentrez&rendertype=abstract</li>
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<li>Huh, Y. S., & Kim, I. H. (2003). Purification of fusion ferritin from recombinant <i>E. coli</i> using two-step sonications. <i>Biotechnology Letters</i>, 25(12), 993–6. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/12889837</li>
-
<li>Moore, J. T., Davis, S. T., & Dev, I. K. (1997). The development of beta-lactamase as a highly versatile genetic reporter for eukaryotic cells. <i>Analytical biochemistry, 247</i>(2), 203–9. doi:10.1006/abio.1997.2092</li>
+
<li>Litowski, J. R., & Hodges, R. S. (2002). Designing heterodimeric two-stranded alpha-helical coiled-coils. Effects of hydrophobicity and alpha-helical propensity on protein folding, stability, and specificity. <i>The Journal of Biological Chemistry, 277</i>(40), 37272–9. doi:10.1074/jbc.M204257200</li>
-
<li>Mussolino, C., & Cathomen, T. (2012). TALE nucleases: tailored genome engineering made easy. <i>Current opinion in biotechnology, 23</i>(5), 644–50. doi:10.1016/j.copbio.2012.01.013</li>
+
<li>Zhang, X.-Q., Gong, S.-W., Zhang, Y., Yang, T., Wang, C.-Y., & Gu, N. (2010). Prussian blue modified iron oxide magnetic nanoparticles and their high peroxidase-like activity. <i>Journal of Materials Chemistry, 20</i>(24), 5110. doi:10.1039/c0jm00174k</li>
-
<li>Qureshi, S. (2007). β-Lactamase: an ideal reporter system for monitoring gene expression in live eukaryotic cells. <i>BioTechniques, 42</i>(1), 91–96. doi:10.2144/000112292</li>
 
-
<li>Remy, I., Ghaddar, G., & Michnick, S. W. (2007). Using the beta-lactamase protein-fragment complementation assay to probe dynamic protein-protein interactions. <i>Nature protocols, 2</i>(9), 2302–6. doi:10.1038/nprot.2007.356</li>
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<h3>Journals and Parts Pages on the Registry of Standard Biological Parts</h3>
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<li>Santambrogio, P., Levi, S., Cozzi, A., Rovida, E., Albertini, A., & Arosio, P. (1993). Production and characterization of recombinant heteropolymers of human ferritin H and L chains.<i> The Journal of biological chemistry</i>, 268(17), 12744–8. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/8509409</li>
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<li>Apostolovic, B., & Klok, H.-A. (2008). pH-sensitivity of the E3/K3 heterodimeric coiled coil. <i>Biomacromolecules, 9</i>(11), 3173–80. doi:10.1021/bm800746e</li>
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<li>Streubel, J., Blücher, C., Landgraf, A., & Boch, J. (2012). TAL effector RVD specificities and efficiencies. <i>Nature biotechnology, 30</i>(7), 593–5. doi:10.1038/nbt.2304</li>
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<li>Arthur, T.M., Keen, J.E., Bosilevac, J.M, Brichta-Harhay, D.M., Kalchayanand, N., Shackelford, S.D., … Koohmaraie, M. (2009). Longitudinal study of <i>Escherichia coli</i> O157:H7 in a beef cattle feedlot and role of high-level shedders in hide contamination. <i>Applied and Environmental Microbiology</i>, 75(20), 6515-23. doi: 10.1128/AEM.00081-09</li>
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<li>Watt, G. D., Kim, J.-W., Zhang, B., Miller, T., Harb, J. N., Davis, R. C., & Choi, S. H. (2012). A Protein-Based Ferritin Bio-Nanobattery. <i>Journal of Nanotechnology</i>, 2012, 1–9. doi:10.1155/2012/516309</li>
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<li>Beurdeley, M., Bietz, F., Li, J., Thomas, S., Stoddard, T., Juillerat, A., … Silva, G. H. (2013). Compact designer TALENs for efficient genome engineering. <i>Nature Communications, 4</i>, 1762. doi:10.1038/ncomms2782</li>
-
<li>Wehrman, T., Kleaveland, B., Her, J.-H., Balint, R. F., & Blau, H. M. (2002). Protein-protein interactions monitored in mammalian cells via complementation of beta -lactamase enzyme fragments. <i>Proceedings of the National Academy of Sciences of the United States of America, 99</i>(6), 3469–74. doi:10.1073/pnas.062043699</li>
+
<li>Besant, J.D., Das, J., Sargent, E.H., Kelley, SO. (2013) Proximal bacterial lysis and detection in nanoliter wells using electrochemistry. <i>American Chemical Society Nano</i>, 7(9), 8183-9.</li>
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<li>Wong, K. K. W., Douglas, T., Gider, S., Awschalom, D. D., & Mann, S. (1998). Biomimetic Synthesis and Characterization of Magnetic Proteins (Magnetoferritin). <i>Chemistry of Materials</i>, 10(1), 279–285. doi:10.1021/cm970421o</li>
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<li>Blais, B.W., Gauthier, M., Descheênes, M., & Huszczynski G. (2012). Polyester cloth-based hybridization array system for identification of enterohemorrhagic <i>Escherichia coli</i> serogroups O26, O45, O103, O111, O121, O145, and O157. <i>Journal of Food Protection,</i> 75(9), 1691-7. doi: 10.4315/0362-028X.JFP-12-116</li>
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<li>Zhang, X.-Q., Gong, S.-W., Zhang, Y., Yang, T., Wang, C.-Y., & Gu, N. (2010). Prussian blue modified iron oxide magnetic nanoparticles and their high peroxidase-like activity. <i>Journal of Materials Chemistry, 20</i>(24), 5110. doi:10.1039/c0jm00174k</li>
+
<li>Bushart, S., Bradbury, D., Elder, G., Duffield, J., Pascual, I., & Ratcliffe, N. (2006). The development of magnetic molecules for the selective removal of contaminants. In <i>Waste Management Conference</i>. Tuczon, AZ. Retrieved from http://www.wmsym.org/archives/2006/pdfs/6190.pdf </li>
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<li>Carvalho, R. H., Lemos, F., Lemos, M. A., Vojinović, V., Fonseca, L. P., & Cabral, J. M. S. (2006). Kinetic modelling of phenol co-oxidation using horseradish peroxidase. <i>Bioprocess and Biosystems Engineering</i>, 29(2), 99–108. doi:10.1007/s00449-006-0057-0</li>
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<li>Cermak, T., Doyle, E.L., Christian, M., Wang, L., Zhang, Y.,Schmidt, C., … Voytas, D.F. (2011). Efficient design and assembly of custom TALEN and other TAL effector-based constructs for DNA targeting. <i>Nucleic Acids Research</i>, 39(12), e82.</li>
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<li>Chase-Topping, M., Gally, D., Low, C., Matthews, L., Woolhouse, M. (2008). Super-shedding and the link between human infection and livestock carriage of <i>Escherichia coli</i> O157. <i>Nature Reviews Microbiology</i>, 6(12):904-12. doi: 10.1038/nrmicro2029</li>
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<li>Cornish-Bowden, A. (2012). <i>Fundamentals of Enzyme Kinetics</i> (4th ed.). Weinheim, Germany: Wiley-Blackwell.</li>
 +
 
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<li>De Lange, O., Schreiber, T., Schandry, N., Radeck, J., Braun, K. H., Koszinowski, J., … Lahaye, T. (2013). Breaking the DNA-binding code of Ralstonia solanacearum TAL effectors provides new possibilities to generate plant resistance genes against bacterial wilt disease. <i>The New Phytologist, 199</i>(3), 773–86. doi:10.1111/nph.12324</li>
 +
 
 +
<li>Dörner, M. H., Salfeld, J., Will, H., Leibold, E. A., Vass, J. K., & Munro, H. N. (1985). Structure of human ferritin light subunit messenger RNA: comparison with heavy subunit message and functional implications. <i>Proceedings of the National Academy of Sciences of the United States of America</i>, 82(10), 3139–43. Retrieved from http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=397730&tool=pmcentrez&rendertype=abstract</li>
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<li>Engler, C., Kandzia, R., & Marillonnet, S. (2008). A one pot, one step, precision cloning method with high throughput capability. <i>PLoS ONE</i>, 3(11), e3647. doi: 10.1371/journal.pone.0003647</li>
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<li>Feng, P., & Lampel, K.A. (1994). Genetic analysis of <i>uidA</i> expression in enterohaemorrhagic <i>Escherichia coli</i> serotype O157:H7. <i>Microbiology</i>, 140, 2101-2107.</li>
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<li>Fortin, N.Y., Mulchandani, A., & Chen, W. (2001). Use of real-time polymerase chain reaction and molecular beacons for the detection of <i>Escherichia coli</i> O157:H7. <i>Analytical Biochemistry</i> , 289(2), 281-8.</li>
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<li>Gibson, D.G., Young, L., Chuang, R.Y., Venter, J.C., Hutchison, C.A. 3rd, Smith, H.O. (2009). Enzymatic assembly of DNA molecules up to several hundred kilobases. <i>Nature Methods</i>, 6(5), 343-5. doi: 10.1038/nmeth.1318</li>
 +
 
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Latest revision as of 02:48, 29 October 2013

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Our Project

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