Team:Calgary/Sandbox/Notebook/References

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<h1>References</h1>
<h1>References</h1>
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<p>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</p>
+
<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>
-
<p>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</p>
+
<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>
-
<p>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</p>
+
<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>
-
<p>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</p>
+
<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>
-
<p>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</p>
+
<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>
-
<p>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</p>
+
<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>
-
<p>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</p>
+
<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>
-
<p>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.</p>
+
<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>
-
<p>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</p>
+
<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>
-
<p>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</p>
+
<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>
-
<p>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</p>
+
<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>
-
<p>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</p>
+
<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>
-
<p>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</p>
+
<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>
-
<p>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</p>
+
<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>
-
<p>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</p>
+
<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>
-
<p>Zhang, W., Zhang, Y., Chen, Y., Li, S., Gu, N., Hu, S., Sun, Y., Chen, X., & Li, Q. (2012). 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</p>
+
<li>Zhang, W., Zhang, Y., Chen, Y., Li, S., Gu, N., Hu, S., Sun, Y., Chen, X., & Li, Q. (2012). 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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Latest revision as of 23:04, 22 September 2013

References

  • Apostolovic, B., & Klok, H.-A. (2008). pH-sensitivity of the E3/K3 heterodimeric coiled coil. Biomacromolecules, 9(11), 3173–80. doi:10.1021/bm800746e
  • Beurdeley, M., Bietz, F., Li, J., Thomas, S., Stoddard, T., Juillerat, A., … Silva, G. H. (2013). Compact designer TALENs for efficient genome engineering. Nature communications, 4, 1762. doi:10.1038/ncomms2782
  • 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. Science (New York, N.Y.), 326(5959), 1509–12. doi:10.1126/science.1178811
  • Bogdanove, A. J., Schornack, S., & Lahaye, T. (2010). TAL effectors: finding plant genes for disease and defense. Current opinion in plant biology, 13(4), 394–401. doi:10.1016/j.pbi.2010.04.010
  • Bogdanove, A. J., & Voytas, D. F. (2011). TAL effectors: customizable proteins for DNA targeting. Science (New York, N.Y.), 3336051), 1843–6. doi:10.1126/science.1204094
  • Cong, L., Zhou, R., Kuo, Y., Cunniff, M., & Zhang, F. (2013). Comprehensive interrogation of natural TALE DNA-binding modules and transcriptional repressor domains. Nature communications. doi:10.1038/ncomms1962.Comprehensive
  • 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. The New phytologist, 199(3), 773–86. doi:10.1111/nph.12324
  • 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.
  • Harrison, P.-M., & Arosio, P. (1996). The ferritins: molecular properties, iron storage function and cellular regulation. Biochimica et Biophysica Acta, 1275(3), 161-203. doi:10.1016/0005-2728(96)00022-9
  • 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. Analytical chemistry, 83(15), 5834–43. doi:10.1021/ac200657s
  • 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. The Journal of biological chemistry, 277(40), 37272–9. doi:10.1074/jbc.M204257200
  • 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. Nature, 349(6309), 541–4. doi:10.1038/349541a0
  • Mussolino, C., & Cathomen, T. (2012). TALE nucleases: tailored genome engineering made easy. Current opinion in biotechnology, 23(5), 644–50. doi:10.1016/j.copbio.2012.01.013
  • Streubel, J., Blücher, C., Landgraf, A., & Boch, J. (2012). TAL effector RVD specificities and efficiencies. Nature biotechnology, 30(7), 593–5. doi:10.1038/nbt.2304
  • 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. Journal of Materials Chemistry, 20(24), 5110. doi:10.1039/c0jm00174k
  • Zhang, W., Zhang, Y., Chen, Y., Li, S., Gu, N., Hu, S., Sun, Y., Chen, X., & Li, Q. (2012). Prussian Blue Modified Ferritin as Peroxidase Mimetics and Its Applications in Biological Detection, Journal of nanoscience and nanotechnology, 12, 1–8. doi:10.1166/jnn.2012.6871

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