Revision as of 23:07, 27 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

Besant, J.D., Das, J., Sargent, E.H., Kelley, SO. (2013) Proximal bacterial lysis and detection in nanoliter wells using electrochemistry. American Chemical Society Nano, 7(9), 8183-9.

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

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 Waste Management Conference. Tuczon, AZ. Retrieved from http://www.wmsym.org/archives/2006/pdfs/6190.pdf

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

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. Proceedings of the National Academy of Sciences of the United States of America, 82(10), 3139–43. Retrieved from http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=397730&tool=pmcentrez&rendertype=abstract

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 : 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

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. Biosensors & Bioelectronics, 26(5), 2018–24. doi:10.1016/j.bios.2010.08.079

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. Journal of Biochemistry, 139(5), 881–5. doi:10.1093/jb/mvj101

Huh, Y. S., & Kim, I. H. (2003). Purification of fusion ferritin from recombinant E. coli using two-step sonications. Biotechnology Letters, 25(12), 993–6. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/12889837

Jordan, V. C., Caplan, M. R., & Bennett, K. M. (2010). Simplified synthesis and relaxometry of magnetoferritin for magnetic resonance imaging. Magnetic Resonance in Medicine : Official Journal of the Society of Magnetic Resonance in Medicine / Society of Magnetic Resonance in Medicine, 64(5), 1260–6. doi:10.1002/mrm.22526

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

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. Proceedings of the National Academy of Sciences of the United States of America, 107(27), 12239–44. doi:10.1073/pnas.1000643107

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

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. Biochemical and Biophysical Research Communications, 298(2), 225–9. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/12387819

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. The Journal of Biological Chemistry, 269(48), 30334–9. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/7982945

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. Water Research, 42(1-2), 307–17. doi:10.1016/j.watres.2007.07.016

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

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. PloS ONE, 6(10), e25561. doi:10.1371/journal.pone.0025561

Luzzago, A., & Cesareni, G. (1989). Isolation of point mutations that affect the folding of the H chain of human ferritin in E.coli. The EMBO Journal, 8(2), 569–76. Retrieved from http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=400843&tool=pmcentrez&rendertype=abstract

Moore, J. T., Davis, S. T., & Dev, I. K. (1997). The development of beta-lactamase as a highly versatile genetic reporter for eukaryotic cells. Analytical Biochemistry, 247(2), 203–9. doi:10.1006/abio.1997.2092

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

Qureshi, S. (2007). β-Lactamase: an ideal reporter system for monitoring gene expression in live eukaryotic cells. BioTechniques, 42(1), 91–96. doi:10.2144/000112292

Remy, I., Ghaddar, G., & Michnick, S. W. (2007). Using the beta-lactamase protein-fragment complementation assay to probe dynamic protein-protein interactions. Nature Protocols, 2(9), 2302–6. doi:10.1038/nprot.2007.356

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. The Journal of Biological Chemistry, 268(17), 12744–8. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/8509409

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

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. Journal of Nanotechnology, 2012, 1–9. doi:10.1155/2012/516309

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. Proceedings of the National Academy of Sciences of the United States of America, 99(6), 3469–74. doi:10.1073/pnas.062043699

Wong, K. K. W., Douglas, T., Gider, S., Awschalom, D. D., & Mann, S. (1998). Biomimetic synthesis and characterization of magnetic proteins (magnetoferritin). Chemistry of Materials, 10(1), 279–285. doi:10.1021/cm970421o

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. (2013). 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

@@ Line 15: / Line 15: @@
 <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>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., 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>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>
+<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>
-<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>
+<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>
-<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>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>
-<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 : 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>
+<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 : 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>
 <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>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>
+<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>
-<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>
-<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>
+<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>
-<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>
+<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>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>
+<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>
+<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>
 <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>
@@ Line 44: / Line 45: @@
 <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>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>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>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>
+<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>
-<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>
+<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>
-<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>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>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>
+<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>
-<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>
+<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>
-<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>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>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>
@@ Line 62: / Line 63: @@
 <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>
+<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>
-<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>
+<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>
-<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>
+<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>
-<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>
+<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>
 <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>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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References

References