http://compbio.biosci.uq.edu.au/mediawiki/index.php?title=N-myc_downstream-regulated_gene_2_isoform_b&feed=atom&action=historyN-myc downstream-regulated gene 2 isoform b - Revision history2024-03-28T20:26:49ZRevision history for this page on the wikiMediaWiki 1.39.6http://compbio.biosci.uq.edu.au/mediawiki/index.php?title=N-myc_downstream-regulated_gene_2_isoform_b&diff=15134&oldid=prevShang Yen: /* Reference */2009-06-16T06:25:28Z<p><span dir="auto"><span class="autocomment">Reference</span></span></p>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>==Reference==</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>==Reference==</div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>*[1]Lifeng Wang, Na Liu, Libo Yao, Fuyang Li1, Jian Zhang1,Yanchun Deng, Junye Liu, Shaoping Ji, Angang Yang, Hua Han, Yingqi <del style="font-weight: bold; text-decoration: none;"> </del></div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>*[1]Lifeng Wang, Na Liu, Libo Yao, Fuyang Li1, Jian Zhang1,Yanchun Deng, Junye Liu, Shaoping Ji, Angang Yang, Hua Han, Yingqi Zhang, Jing Zhang, Wei Han,and Xinping Liu.NDRG2 is a new HIF-1 Target Gene Necessary for Hypoxia-Induced Apoptosis in A549 cells.Cellular Physiology and Biochemistry.Cell Physiol Biochem 2008;21:239-250. </div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>Zhang, Jing Zhang, Wei Han,and Xinping Liu.NDRG2 is a new HIF-1 Target Gene Necessary for Hypoxia-Induced Apoptosis in A549 cells.Cellular Physiology and Biochemistry.Cell Physiol Biochem 2008;21:239-250. </div></td><td colspan="2" class="diff-side-added"></td></tr>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>*[2]Jian Zhang, Fuyang Li1, Xinping Liu, Lan Shen, Junye Liu, Jin Su, Wei Zhang, Yanchun Deng, Lifeng Wang, Na Liu, Wei Han, Jing Zhang, Shaoping Ji, Angang Yang, Hua Han, and Libo Yao. The Repression of Human Differentiation-related Gene NDRG2 Expression by Myc via Miz-1-dependent Interaction with the NDRG2 Core Promoter. THE JOURNAL OF BIOLOGICAL CHEMISTRY VOL. 281, NO. 51, pp. 39159–39168, December 22 2006</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>*[2]Jian Zhang, Fuyang Li1, Xinping Liu, Lan Shen, Junye Liu, Jin Su, Wei Zhang, Yanchun Deng, Lifeng Wang, Na Liu, Wei Han, Jing Zhang, Shaoping Ji, Angang Yang, Hua Han, and Libo Yao. The Repression of Human Differentiation-related Gene NDRG2 Expression by Myc via Miz-1-dependent Interaction with the NDRG2 Core Promoter. THE JOURNAL OF BIOLOGICAL CHEMISTRY VOL. 281, NO. 51, pp. 39159–39168, December 22 2006</div></td></tr>
</table>Shang Yenhttp://compbio.biosci.uq.edu.au/mediawiki/index.php?title=N-myc_downstream-regulated_gene_2_isoform_b&diff=15133&oldid=prevShang Yen: /* Reference */2009-06-16T06:25:01Z<p><span dir="auto"><span class="autocomment">Reference</span></span></p>
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<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>[1]Lifeng Wang, Na Liu, Libo Yao, Fuyang Li1, Jian Zhang1,Yanchun Deng, Junye Liu, Shaoping Ji, Angang Yang, Hua Han, Yingqi </div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;">*</ins>[1]Lifeng Wang, Na Liu, Libo Yao, Fuyang Li1, Jian Zhang1,Yanchun Deng, Junye Liu, Shaoping Ji, Angang Yang, Hua Han, Yingqi </div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>Zhang, Jing Zhang, Wei Han,and Xinping Liu.NDRG2 is a new HIF-1 Target Gene Necessary for Hypoxia-Induced Apoptosis in A549 cells.Cellular Physiology and Biochemistry.Cell Physiol Biochem 2008;21:239-250. </div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>Zhang, Jing Zhang, Wei Han,and Xinping Liu.NDRG2 is a new HIF-1 Target Gene Necessary for Hypoxia-Induced Apoptosis in A549 cells.Cellular Physiology and Biochemistry.Cell Physiol Biochem 2008;21:239-250. </div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>[2]Jian Zhang, Fuyang Li1, Xinping Liu, Lan Shen, Junye Liu, Jin Su, Wei Zhang, Yanchun Deng, Lifeng Wang, Na Liu, Wei Han, Jing Zhang, Shaoping Ji, Angang Yang, Hua Han, and Libo Yao. The Repression of Human Differentiation-related Gene NDRG2 Expression by Myc via Miz-1-dependent Interaction with the NDRG2 Core Promoter. THE JOURNAL OF BIOLOGICAL CHEMISTRY VOL. 281, NO. 51, pp. 39159–39168, December 22 2006</div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;">*</ins>[2]Jian Zhang, Fuyang Li1, Xinping Liu, Lan Shen, Junye Liu, Jin Su, Wei Zhang, Yanchun Deng, Lifeng Wang, Na Liu, Wei Han, Jing Zhang, Shaoping Ji, Angang Yang, Hua Han, and Libo Yao. The Repression of Human Differentiation-related Gene NDRG2 Expression by Myc via Miz-1-dependent Interaction with the NDRG2 Core Promoter. THE JOURNAL OF BIOLOGICAL CHEMISTRY VOL. 281, NO. 51, pp. 39159–39168, December 22 2006</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div><del style="font-weight: bold; text-decoration: none;">(</del>3<del style="font-weight: bold; text-decoration: none;">)</del>Boulkroun Sheerazed, Fay Michel, Zennaro Maria-Christina, Escoubet Brigitte*, Jaisser Frederic, Blot-Chabaud Marcel, Farman Nicolette and Courtois-Coutry Nathalie. CHARACTERIZATION OF RAT NDRG2 (N-myc Downstream-Regulated Gene 2), A NOVEL EARLY MINERALOCORTICOID-SPECIFIC INDUCED GENE. JBC Papers in Press. Published on June 18, 2002 as Manuscript M200272200</div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;">*[</ins>3<ins style="font-weight: bold; text-decoration: none;">]</ins>Boulkroun Sheerazed, Fay Michel, Zennaro Maria-Christina, Escoubet Brigitte*, Jaisser Frederic, Blot-Chabaud Marcel, Farman Nicolette and Courtois-Coutry Nathalie. CHARACTERIZATION OF RAT NDRG2 (N-myc Downstream-Regulated Gene 2), A NOVEL EARLY MINERALOCORTICOID-SPECIFIC INDUCED GENE. JBC Papers in Press. Published on June 18, 2002 as Manuscript M200272200</div></td></tr>
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<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>[4]Staller, P., Peukert, K., Kiermaier, A., Seoane, J. L. J., Karsunky, H., Moroy,T., Bartek, J., Massague, J., and Hanel, F. (2001) Nat. Cell Biol. 3, 392–399</div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;">*</ins>[4]Staller, P., Peukert, K., Kiermaier, A., Seoane, J. L. J., Karsunky, H., Moroy,T., Bartek, J., Massague, J., and Hanel, F. (2001) Nat. Cell Biol. 3, 392–399</div></td></tr>
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<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>[5]Kurdistani, S. K., Arizti, P., Reimer, C. L., Sugrue, M. M., Aaronson, S. A., and Lee, S. W. (1998) Cancer Res. 58, 4439–4444</div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;">*</ins>[5]Kurdistani, S. K., Arizti, P., Reimer, C. L., Sugrue, M. M., Aaronson, S. A., and Lee, S. W. (1998) Cancer Res. 58, 4439–4444</div></td></tr>
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<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>[6]Eilers, M., Schirm, S., and Bishop, J. M. (1991) EMBO J. 10, 133–141</div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;">*</ins>[6]Eilers, M., Schirm, S., and Bishop, J. M. (1991) EMBO J. 10, 133–141</div></td></tr>
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<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>[7]Blackwood, E. M., Kretzner, L., and Eisenman, R. N. (1992) Curr. Opin. Genet. Dev. 2, 227–235</div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;">*</ins>[7]Blackwood, E. M., Kretzner, L., and Eisenman, R. N. (1992) Curr. Opin. Genet. Dev. 2, 227–235</div></td></tr>
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<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>[8]Shachaf, C., Kopelman, A., Arvanitis, C., Karlsson, A., Beer, S., Mandl, S., Bachmann, M. H., Borowsky, A. D., Ruebner, B., <del style="font-weight: bold; text-decoration: none;"> </del>Cardiff, R. D., Yang, Q., Bishop, J. M., Contag, C. H., and Felsher, D. W. (2004) Nature 431, 1112–1117</div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;">*</ins>[8]Shachaf, C., Kopelman, A., Arvanitis, C., Karlsson, A., Beer, S., Mandl, S., Bachmann, M. H., Borowsky, A. D., Ruebner, B.,Cardiff, R. D., Yang, Q., Bishop, J. M., Contag, C. H., and Felsher, D. W. (2004) Nature 431, 1112–1117</div></td></tr>
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<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>[9]Salnikow K, Blagosklonny MV, Ryan H, Johnson R, Costa M: Carcinogenic nickel induces genes involved with hypoxic stress .Cancer Res 2000;60:38-41.</div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;">*</ins>[9]Salnikow K, Blagosklonny MV, Ryan H, Johnson R, Costa M: Carcinogenic nickel induces genes involved with hypoxic stress .Cancer Res 2000;60:38-41.</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>[10]Semenza GL: Regulation of mammalian O2 homeostasis by hypoxia-inducible factor 1.Annu Rev Cell Dev Biol 1999;15:551-578.</div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;">*</ins>[10]Semenza GL: Regulation of mammalian O2 homeostasis by hypoxia-inducible factor 1.Annu Rev Cell Dev Biol 1999;15:551-578.</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>[11]Chen B, Nelson DM, Sadovsky Y: N-myc down-regulated gene 1 modulates the response of term human trophoblasts to hypoxic injury.J Biol Chem 2006;281:2764-2772.</div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;">*</ins>[11]Chen B, Nelson DM, Sadovsky Y: N-myc down-regulated gene 1 modulates the response of term human trophoblasts to hypoxic injury.J Biol Chem 2006;281:2764-2772.</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>[12]Sowter HM, Raval RR, Moore JW, Ratcliffe PJ, Harris AL: Predominant role of hypoxia-inducible transcription factor (Hif)-1alpha versusHif-2alpha in regulation of the transcriptional response to hypoxia.Cancer Res 2003;63:6130- 6134.</div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;">*</ins>[12]Sowter HM, Raval RR, Moore JW, Ratcliffe PJ, Harris AL: Predominant role of hypoxia-inducible transcription factor (Hif)-1alpha versusHif-2alpha in regulation of the transcriptional response to hypoxia.Cancer Res 2003;63:6130- 6134.</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>[13]Zhang J, Li F, Liu X, Shen L, Liu J, Su J, Zhang W, Deng Y, Wang L, Liu N, Han W, Zhang J, Ji S, Yang A, Han H, Yao L: The <del style="font-weight: bold; text-decoration: none;"> </del>repression of human differentiation related gene NDRG2 expression by MYC via MIZ-1 dependent interaction with the NDRG2 core <del style="font-weight: bold; text-decoration: none;"> </del>promoter. J Biol Chem 2006;281:39159-39168. http://www.ncbi.nlm.nih.gov/pubmed/7885389</div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;">*</ins>[13]Zhang J, Li F, Liu X, Shen L, Liu J, Su J, Zhang W, Deng Y, Wang L, Liu N, Han W, Zhang J, Ji S, Yang A, Han H, Yao L: The repression of human differentiation related gene NDRG2 expression by MYC via MIZ-1 dependent interaction with the NDRG2 core promoter. J Biol Chem 2006;281:39159-39168. http://www.ncbi.nlm.nih.gov/pubmed/7885389</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>[14]Lehninger, Principles of Biochemistry, 4th ed. (pp 216-219)</div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;">*</ins>[14]Lehninger, Principles of Biochemistry, 4th ed. (pp 216-219)</div></td></tr>
</table>Shang Yenhttp://compbio.biosci.uq.edu.au/mediawiki/index.php?title=N-myc_downstream-regulated_gene_2_isoform_b&diff=15093&oldid=prevShang Yen: /* Results */2009-06-16T02:11:48Z<p><span dir="auto"><span class="autocomment">Results</span></span></p>
<table style="background-color: #fff; color: #202122;" data-mw="interface">
<col class="diff-marker" />
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">← Older revision</td>
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 02:11, 16 June 2009</td>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>]]</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>]]</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>The NDRG2 molecule was related to the a/b hydrolase superfamily with key <del style="font-weight: bold; text-decoration: none;">a </del>characteristic where the second B-sheet of the molecule is anti-parallel compared to the rest of the B-sheet. This proteins consists mainly of alpha 15 helices and 9 beta sheets</div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>The NDRG2 molecule was related to the a/b hydrolase superfamily with <ins style="font-weight: bold; text-decoration: none;">a </ins>key characteristic where the second B-sheet of the molecule is anti-parallel compared to the rest of the B-sheet. This proteins consists mainly of alpha 15 helices and 9 beta sheets</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>[[image:XXX1.png|centre|thumb|500px|'''Figure 2''' Figure 2. A cartoon structure of highly conserved region in NDRG2 (red) and ligands (cyan) ]]</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>[[image:XXX1.png|centre|thumb|500px|'''Figure 2''' Figure 2. A cartoon structure of highly conserved region in NDRG2 (red) and ligands (cyan) ]]</div></td></tr>
</table>Shang Yenhttp://compbio.biosci.uq.edu.au/mediawiki/index.php?title=N-myc_downstream-regulated_gene_2_isoform_b&diff=15077&oldid=prevHammerTime: /* Conclusion */2009-06-16T02:00:27Z<p><span dir="auto"><span class="autocomment">Conclusion</span></span></p>
<table style="background-color: #fff; color: #202122;" data-mw="interface">
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 02:00, 16 June 2009</td>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>==Conclusion==</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>==Conclusion==</div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>In conclusion, the NDRG 2 proteins most likely functions as a regulator of H2O2 within many organism which plays a crucial role in maintaining the stability of DNA of cells. <del style="font-weight: bold; text-decoration: none;">Furthermore, it </del>is believed <del style="font-weight: bold; text-decoration: none;">that NDRG 2 also acts </del>to <del style="font-weight: bold; text-decoration: none;">eliminate cancerous cells via apoptosis under hypoxia conditions. This is backed up by the high abundance of NDRG-2 protein in many organism, particularly complex multicellular eukaryotes where regulation at this level is crucial to ensure functionality and stability of the organisms. NDRG-2 is also highly conserved throughout many different mammals, plants, birds and insects which further strengthens this idea. Future directions for the study would require more sequence analysis to identify more homologous proteins to further strength the phylogenetic tree. </del></div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>In conclusion, the NDRG 2 proteins most likely functions as a regulator of H2O2 within many organism which plays a crucial role in maintaining the stability of DNA of cells. <ins style="font-weight: bold; text-decoration: none;">The NDRG2 function </ins>is <ins style="font-weight: bold; text-decoration: none;">also </ins>believed to <ins style="font-weight: bold; text-decoration: none;">be </ins>suppression of tumor cell by inducing the apoptosis for those are subjected to hypoxic condition, the regulation of NDRG2 expression is dependent on the Myc gene expression, which it functions in other DNA binding. The less Myc gene express the more NDRG2 express, when the Myc gene mutate to the oncoprotein then the NDRG2 expression would be no longer suppressed, mutated Myc gene results in abnormal cell differentiation and would lead to the development of tumor cell, the NDRG2 gene would be then expressed since the lower level of Myc gene expression acts as a signal that trigger the NDRG2<ins style="font-weight: bold; text-decoration: none;">. This is backed up by the high abundance of NDRG-2 protein in many organism, particularly complex multicellular eukaryotes where regulation at this level is crucial to ensure functionality and stability of the organisms. NDRG-2 is also highly conserved throughout many different mammals, plants, birds and insects which further strengthens this idea. Future directions for the study would require more sequence analysis to identify more homologous proteins to further strength the phylogenetic tree</ins>.</div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div> </div></td><td colspan="2" class="diff-side-added"></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div><del style="font-weight: bold; text-decoration: none;">The NDRG2 functions in </del>suppression of tumor cell by inducing the apoptosis for those are subjected to hypoxic condition, the regulation of NDRG2 expression is dependent on the Myc gene expression, which it functions in other DNA binding. The less Myc gene express the more NDRG2 express, when the Myc gene mutate to the oncoprotein then the NDRG2 expression would be no longer suppressed, mutated Myc gene results in abnormal cell differentiation and would lead to the development of tumor cell, the NDRG2 gene would be then expressed since the lower level of Myc gene expression acts as a signal that trigger the NDRG2.</div></td><td colspan="2" class="diff-side-added"></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>==Reference==</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>==Reference==</div></td></tr>
</table>HammerTimehttp://compbio.biosci.uq.edu.au/mediawiki/index.php?title=N-myc_downstream-regulated_gene_2_isoform_b&diff=15059&oldid=prevShang Yen: /* Conclusion */2009-06-16T01:53:22Z<p><span dir="auto"><span class="autocomment">Conclusion</span></span></p>
<table style="background-color: #fff; color: #202122;" data-mw="interface">
<col class="diff-marker" />
<col class="diff-content" />
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<tr class="diff-title" lang="en">
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">← Older revision</td>
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 01:53, 16 June 2009</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l72">Line 72:</td>
<td colspan="2" class="diff-lineno">Line 72:</td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>==Conclusion==</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>==Conclusion==</div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>In conclusion, the NDRG 2 proteins most likely functions as a regulator of H2O2 within many organism which plays a crucial role in maintaining the stability of DNA of cells. Furthermore, it is believed that NDRG 2 also acts to eliminate cancerous cells via apoptosis under hypoxia conditions. This is backed up by the high abundance of NDRG-2 protein in many organism, particularly complex multicellular eukaryotes where regulation at this level is crucial to ensure functionality and stability of the organisms. NDRG-2 is also highly conserved throughout many different mammals, plants, birds and insects which further strengthens this idea. Future directions for the study would require more sequence analysis to identify more homologous proteins to further strength the phylogenetic tree.</div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>In conclusion, the NDRG 2 proteins most likely functions as a regulator of H2O2 within many organism which plays a crucial role in maintaining the stability of DNA of cells. Furthermore, it is believed that NDRG 2 also acts to eliminate cancerous cells via apoptosis under hypoxia conditions. This is backed up by the high abundance of NDRG-2 protein in many organism, particularly complex multicellular eukaryotes where regulation at this level is crucial to ensure functionality and stability of the organisms. NDRG-2 is also highly conserved throughout many different mammals, plants, birds and insects which further strengthens this idea. Future directions for the study would require more sequence analysis to identify more homologous proteins to further strength the phylogenetic tree<ins style="font-weight: bold; text-decoration: none;">. </ins></div></td></tr>
<tr><td colspan="2" class="diff-side-deleted"></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div> </div></td></tr>
<tr><td colspan="2" class="diff-side-deleted"></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;">The NDRG2 functions in suppression of tumor cell by inducing the apoptosis for those are subjected to hypoxic condition, the regulation of NDRG2 expression is dependent on the Myc gene expression, which it functions in other DNA binding. The less Myc gene express the more NDRG2 express, when the Myc gene mutate to the oncoprotein then the NDRG2 expression would be no longer suppressed, mutated Myc gene results in abnormal cell differentiation and would lead to the development of tumor cell, the NDRG2 gene would be then expressed since the lower level of Myc gene expression acts as a signal that trigger the NDRG2</ins>.</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>==Reference==</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>==Reference==</div></td></tr>
</table>Shang Yenhttp://compbio.biosci.uq.edu.au/mediawiki/index.php?title=N-myc_downstream-regulated_gene_2_isoform_b&diff=15052&oldid=prevHammerTime: /* Conclusion */2009-06-16T01:50:55Z<p><span dir="auto"><span class="autocomment">Conclusion</span></span></p>
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 01:50, 16 June 2009</td>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>==Conclusion==</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>==Conclusion==</div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>In conclusion, the NDRG 2 proteins most likely functions as a regulator of H2O2 within many organism which plays a crucial role in maintaining the stability of DNA of cells.Furthermore, NDRG 2 also acts to eliminate cancerous cells via apoptosis under hypoxia conditions. This <del style="font-weight: bold; text-decoration: none;">explains </del>the high abundance in many organism, particularly complex multicellular eukaryotes where regulation at this level is crucial to ensure functionality and stability of the organisms.</div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>In conclusion, the NDRG 2 proteins most likely functions as a regulator of H2O2 within many organism which plays a crucial role in maintaining the stability of DNA of cells. Furthermore, <ins style="font-weight: bold; text-decoration: none;">it is believed that </ins>NDRG 2 also acts to eliminate cancerous cells via apoptosis under hypoxia conditions. This <ins style="font-weight: bold; text-decoration: none;">is backed up by </ins>the high abundance <ins style="font-weight: bold; text-decoration: none;">of NDRG-2 protein </ins>in many organism, particularly complex multicellular eukaryotes where regulation at this level is crucial to ensure functionality and stability of the organisms<ins style="font-weight: bold; text-decoration: none;">. NDRG-2 is also highly conserved throughout many different mammals, plants, birds and insects which further strengthens this idea. Future directions for the study would require more sequence analysis to identify more homologous proteins to further strength the phylogenetic tree</ins>.</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>==Reference==</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>==Reference==</div></td></tr>
</table>HammerTimehttp://compbio.biosci.uq.edu.au/mediawiki/index.php?title=N-myc_downstream-regulated_gene_2_isoform_b&diff=15035&oldid=prevYu Keng: /* Conclusion */2009-06-16T01:43:13Z<p><span dir="auto"><span class="autocomment">Conclusion</span></span></p>
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 01:43, 16 June 2009</td>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>==Conclusion==</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>==Conclusion==</div></td></tr>
<tr><td colspan="2" class="diff-side-deleted"></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;">In conclusion, the NDRG 2 proteins most likely functions as a regulator of H2O2 within many organism which plays a crucial role in maintaining the stability of DNA of cells.Furthermore, NDRG 2 also acts to eliminate cancerous cells via apoptosis under hypoxia conditions. This explains the high abundance in many organism, particularly complex multicellular eukaryotes where regulation at this level is crucial to ensure functionality and stability of the organisms.</ins></div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>==Reference==</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>==Reference==</div></td></tr>
</table>Yu Kenghttp://compbio.biosci.uq.edu.au/mediawiki/index.php?title=N-myc_downstream-regulated_gene_2_isoform_b&diff=15005&oldid=prevYu Keng: /* Discussion */2009-06-16T01:33:09Z<p><span dir="auto"><span class="autocomment">Discussion</span></span></p>
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 01:33, 16 June 2009</td>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>Function of Chloroperoxidase is to hydrolyze hydrogen peroxide as high concentrations of it have negatives effects in cells. E.g. accumulation of H2O2 In plants cells have damaging effects DNA, lipid membranes and organelles and plants rely on these enzymes to prevent accumulation of H2O2. However, presence of H2O2 also plays a role in plant defenses against pathogens. Further evidence suggests that NDRG 2 is believed to play a role in the regulation of H2O2 levels based on the overlay of human NDRG-2 protein with chlorrperoxidase from Streptomyces Lividans. This is due to low RMSD values indicating the best superimposition between both 3-d structures whihc in turn suggests that the homology of both structure may be correlated to its similarity in function.</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>Function of Chloroperoxidase is to hydrolyze hydrogen peroxide as high concentrations of it have negatives effects in cells. E.g. accumulation of H2O2 In plants cells have damaging effects DNA, lipid membranes and organelles and plants rely on these enzymes to prevent accumulation of H2O2. However, presence of H2O2 also plays a role in plant defenses against pathogens. Further evidence suggests that NDRG 2 is believed to play a role in the regulation of H2O2 levels based on the overlay of human NDRG-2 protein with chlorrperoxidase from Streptomyces Lividans. This is due to low RMSD values indicating the best superimposition between both 3-d structures whihc in turn suggests that the homology of both structure may be correlated to its similarity in function.</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>The presences of many hydrophobic residues on the surface of NDRG-2 shows that it is needed to facilitate entry pass the nuclear membrane into the nucleus. The hydrophobic region binds to hydrophobic nuclear membrane regions and via homophilic binding facilitates its endocytosis into the nucleus.Within this region consists of ligands which connects directly to the conserved region core of the protein which may also play a role in faculitating its translocation into the nucleus where this could server as a recognition signal for its translocation into the nucleus.</div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>The presences of many hydrophobic residues on the surface of NDRG-2 shows that it is needed to facilitate entry pass the nuclear membrane into the nucleus. The hydrophobic region binds to hydrophobic nuclear membrane regions and via homophilic binding facilitates its endocytosis into the nucleus.Within this region consists of ligands which connects directly to the conserved region core of the protein which may also play a role in faculitating its translocation into the nucleus where this could server as a recognition signal for its translocation into the nucleus <ins style="font-weight: bold; text-decoration: none;">[1]</ins>.</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>Based on structure of chloroperoxidase NDRG-2 protein could be active as a trimer suggesting that multiple domains is required to form a full functional molecule where the active site is formed via interaction of multiple domains.e.g formation of a catalytic triad found in protease enzyme which functions in the hydrolysis of peptide bonds due to specific amino acid residues located in the active site [<del style="font-weight: bold; text-decoration: none;">13</del>].No functions were found for organic residues (Benzoic acid and Nonaethylene glycol) present on proteins structure. Pressence of these organic residues could be due to remaining residues following crystallization of structure as no such residues were present on molecules with similar alpha/beta hydrolase molecules.</div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>Based on structure of chloroperoxidase NDRG-2 protein could be active as a trimer suggesting that multiple domains is required to form a full functional molecule where the active site is formed via interaction of multiple domains.e.g formation of a catalytic triad found in protease enzyme which functions in the hydrolysis of peptide bonds due to specific amino acid residues located in the active site [<ins style="font-weight: bold; text-decoration: none;">14</ins>].No functions were found for organic residues (Benzoic acid and Nonaethylene glycol) present on proteins structure. Pressence of these organic residues could be due to remaining residues following crystallization of structure as no such residues were present on molecules with similar alpha/beta hydrolase molecules.</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>The NDRG2 function is to down-regulate the mutated myc gene to inhibit the tumor cell proliferation. NDRG2 is a hypoxia induced gene that functions in apoptosis to kill the tumor cells, in the presence of lower level of oxygen, NDRG2 is more expressed. Hypoxia also induced the translocation of NDRG2 from cytoplasm to nucleus of tumor cells, although the nuclear localisation signal (NLS) as a nuclear import element is not identified in NDRG2 protein, but it’s speculated that NDRG2 protein has its own motif for the nuclear translocation. [1] Lifeng Wang et al showed that there was an enhanced resistance of A549 cells to hypoxia induced apoptosis if NDRG2 gene was knocked down by siRNA. It was noticeable that the ectopic expression of NDRG2 only enhanced the apoptosis of A549 cells upon hypoxia, but not under normal culture status.[1] It is unknown if the the expression of NDRG-2 gene is directly responsible for apoptosis of tumour cells or if it is a signal for the apoptosis process NDRG-2 expression is regulated by the Hypoxia-inducible factor (HIF-1) in tumor cell line under hypoxic condition, the Hypoxia responsive element (HRE-1) is one of the three HREs identified in the promoter of NDRG2 gene that bind to the HIF-1 importantly for the expression</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>The NDRG2 function is to down-regulate the mutated myc gene to inhibit the tumor cell proliferation. NDRG2 is a hypoxia induced gene that functions in apoptosis to kill the tumor cells, in the presence of lower level of oxygen, NDRG2 is more expressed. Hypoxia also induced the translocation of NDRG2 from cytoplasm to nucleus of tumor cells, although the nuclear localisation signal (NLS) as a nuclear import element is not identified in NDRG2 protein, but it’s speculated that NDRG2 protein has its own motif for the nuclear translocation. [1] Lifeng Wang et al showed that there was an enhanced resistance of A549 cells to hypoxia induced apoptosis if NDRG2 gene was knocked down by siRNA. It was noticeable that the ectopic expression of NDRG2 only enhanced the apoptosis of A549 cells upon hypoxia, but not under normal culture status.[1] It is unknown if the the expression of NDRG-2 gene is directly responsible for apoptosis of tumour cells or if it is a signal for the apoptosis process NDRG-2 expression is regulated by the Hypoxia-inducible factor (HIF-1) in tumor cell line under hypoxic condition, the Hypoxia responsive element (HRE-1) is one of the three HREs identified in the promoter of NDRG2 gene that bind to the HIF-1 importantly for the expression</div></td></tr>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>From the MSA it can be deduced that there is high conservation of NDRG-2 protein throughout many different organisms and it can be concluded that the protein plays a very important role in the biology of a cell. The most highly conserved and closely related branch was the blue branch which had the highest bootstrap values. The purple branch which contained proteins from different species of insects was more closely related to plants than the animals. This is highly interesting and could be a result of poorly optimized tree and low identity to target sequence. The addition of wider range of species including bacteria would confirm the placement of streptomyces lividans in the tree and would help to strength the overall tree.</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>From the MSA it can be deduced that there is high conservation of NDRG-2 protein throughout many different organisms and it can be concluded that the protein plays a very important role in the biology of a cell. The most highly conserved and closely related branch was the blue branch which had the highest bootstrap values. The purple branch which contained proteins from different species of insects was more closely related to plants than the animals. This is highly interesting and could be a result of poorly optimized tree and low identity to target sequence. The addition of wider range of species including bacteria would confirm the placement of streptomyces lividans in the tree and would help to strength the overall tree.</div></td></tr>
<tr><td colspan="2" class="diff-side-deleted"></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;"></ins></div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>==Conclusion==</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>==Conclusion==</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td></tr>
</table>Yu Kenghttp://compbio.biosci.uq.edu.au/mediawiki/index.php?title=N-myc_downstream-regulated_gene_2_isoform_b&diff=14995&oldid=prevYu Keng at 01:26, 16 June 20092009-06-16T01:26:33Z<p></p>
<table style="background-color: #fff; color: #202122;" data-mw="interface">
<col class="diff-marker" />
<col class="diff-content" />
<col class="diff-marker" />
<col class="diff-content" />
<tr class="diff-title" lang="en">
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">← Older revision</td>
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 01:26, 16 June 2009</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l64">Line 64:</td>
<td colspan="2" class="diff-lineno">Line 64:</td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>Based on structure of chloroperoxidase NDRG-2 protein could be active as a trimer suggesting that multiple domains is required to form a full functional molecule where the active site is formed via interaction of multiple domains.e.g formation of a catalytic triad found in protease enzyme which functions in the hydrolysis of peptide bonds due to specific amino acid residues located in the active site [13].No functions were found for organic residues (Benzoic acid and Nonaethylene glycol) present on proteins structure. Pressence of these organic residues could be due to remaining residues following crystallization of structure as no such residues were present on molecules with similar alpha/beta hydrolase molecules.</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>Based on structure of chloroperoxidase NDRG-2 protein could be active as a trimer suggesting that multiple domains is required to form a full functional molecule where the active site is formed via interaction of multiple domains.e.g formation of a catalytic triad found in protease enzyme which functions in the hydrolysis of peptide bonds due to specific amino acid residues located in the active site [13].No functions were found for organic residues (Benzoic acid and Nonaethylene glycol) present on proteins structure. Pressence of these organic residues could be due to remaining residues following crystallization of structure as no such residues were present on molecules with similar alpha/beta hydrolase molecules.</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>The NDRG2 function is to down-regulate the mutated myc gene to inhibit the tumor cell proliferation. NDRG2 is a hypoxia induced gene that functions in apoptosis to kill the tumor cells, in the presence of lower level of oxygen, NDRG2 is more expressed. Hypoxia also induced the translocation of NDRG2 from cytoplasm to <del style="font-weight: bold; text-decoration: none;">nuclear </del>of tumor cells, although the nuclear localisation signal (NLS) as a nuclear import element is not identified in NDRG2 protein, but it’s speculated that NDRG2 protein has its own motif for the nuclear translocation. [1] Lifeng Wang et al showed that there was an enhanced resistance of A549 cells to hypoxia induced apoptosis if NDRG2 gene was knocked down by siRNA. It was noticeable that the ectopic expression of NDRG2 only enhanced the apoptosis of A549 cells upon hypoxia, but not under normal culture status.[1] It is unknown if the the expression of NDRG-2 gene is directly responsible for apoptosis of tumour cells or if it is a signal for the apoptosis process NDRG-2 expression is regulated by the Hypoxia-inducible factor (HIF-1) in tumor cell line under hypoxic condition, the Hypoxia responsive element (HRE-1) is one of the three HREs identified in the promoter of NDRG2 gene that bind to the HIF-1 importantly for the expression</div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>The NDRG2 function is to down-regulate the mutated myc gene to inhibit the tumor cell proliferation. NDRG2 is a hypoxia induced gene that functions in apoptosis to kill the tumor cells, in the presence of lower level of oxygen, NDRG2 is more expressed. Hypoxia also induced the translocation of NDRG2 from cytoplasm to <ins style="font-weight: bold; text-decoration: none;">nucleus </ins>of tumor cells, although the nuclear localisation signal (NLS) as a nuclear import element is not identified in NDRG2 protein, but it’s speculated that NDRG2 protein has its own motif for the nuclear translocation. [1] Lifeng Wang et al showed that there was an enhanced resistance of A549 cells to hypoxia induced apoptosis if NDRG2 gene was knocked down by siRNA. It was noticeable that the ectopic expression of NDRG2 only enhanced the apoptosis of A549 cells upon hypoxia, but not under normal culture status.[1] It is unknown if the the expression of NDRG-2 gene is directly responsible for apoptosis of tumour cells or if it is a signal for the apoptosis process NDRG-2 expression is regulated by the Hypoxia-inducible factor (HIF-1) in tumor cell line under hypoxic condition, the Hypoxia responsive element (HRE-1) is one of the three HREs identified in the promoter of NDRG2 gene that bind to the HIF-1 importantly for the expression</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>The NDRG2 function is to down-regulate the mutated myc gene to inhibit the tumor cell proliferation. NDRG2 is a hypoxia induced gene that functions in apoptosis to kill the tumor cells, in the presence of lower level of oxygen, NDRG2 is more expressed. Hypoxia also induced the translocation of NDRG2 from cytoplasm to nuclear of tumor cells, although the nuclear localisation signal (NLS) as a nuclear import element is not identified in NDRG2 protein, but it’s speculated that NDRG2 protein has its own motif for the nuclear translocation. [1] Lifeng Wang et al showed that there was an enhanced resistance of A549 cells to hypoxia induced apoptosis if NDRG2 gene was knocked down by siRNA. It was noticeable that the ectopic expression of NDRG2 only enhanced the apoptosis of A549 cells upon hypoxia, but not under normal culture status.[1]</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>The NDRG2 function is to down-regulate the mutated myc gene to inhibit the tumor cell proliferation. NDRG2 is a hypoxia induced gene that functions in apoptosis to kill the tumor cells, in the presence of lower level of oxygen, NDRG2 is more expressed. Hypoxia also induced the translocation of NDRG2 from cytoplasm to nuclear of tumor cells, although the nuclear localisation signal (NLS) as a nuclear import element is not identified in NDRG2 protein, but it’s speculated that NDRG2 protein has its own motif for the nuclear translocation. [1] Lifeng Wang et al showed that there was an enhanced resistance of A549 cells to hypoxia induced apoptosis if NDRG2 gene was knocked down by siRNA. It was noticeable that the ectopic expression of NDRG2 only enhanced the apoptosis of A549 cells upon hypoxia, but not under normal culture status.[1]</div></td></tr>
</table>Yu Kenghttp://compbio.biosci.uq.edu.au/mediawiki/index.php?title=N-myc_downstream-regulated_gene_2_isoform_b&diff=14953&oldid=prevHammerTime at 00:58, 16 June 20092009-06-16T00:58:31Z<p></p>
<table style="background-color: #fff; color: #202122;" data-mw="interface">
<col class="diff-marker" />
<col class="diff-content" />
<col class="diff-marker" />
<col class="diff-content" />
<tr class="diff-title" lang="en">
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">← Older revision</td>
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 00:58, 16 June 2009</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l70">Line 70:</td>
<td colspan="2" class="diff-lineno">Line 70:</td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>From the MSA it can be deduced that there is high conservation of NDRG-2 protein throughout many different organisms and it can be concluded that the protein plays a very important role in the biology of a cell. The most highly conserved and closely related branch was the blue branch which had the highest bootstrap values. The purple branch which contained proteins from different species of insects was more closely related to plants than the animals. This is highly interesting and could be a result of poorly optimized tree and low identity to target sequence. The addition of wider range of species including bacteria would confirm the placement of streptomyces lividans in the tree and would help to strength the overall tree.</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>From the MSA it can be deduced that there is high conservation of NDRG-2 protein throughout many different organisms and it can be concluded that the protein plays a very important role in the biology of a cell. The most highly conserved and closely related branch was the blue branch which had the highest bootstrap values. The purple branch which contained proteins from different species of insects was more closely related to plants than the animals. This is highly interesting and could be a result of poorly optimized tree and low identity to target sequence. The addition of wider range of species including bacteria would confirm the placement of streptomyces lividans in the tree and would help to strength the overall tree.</div></td></tr>
<tr><td colspan="2" class="diff-side-deleted"></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;">==Conclusion==</ins></div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>==Reference==</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>==Reference==</div></td></tr>
</table>HammerTime