http://52.214.119.220/wiki/index.php?action=history&feed=atom&title=User%3AAnthony_Milto%2FSandbox_1User:Anthony Milto/Sandbox 1 - Revision history2026-04-14T07:52:03ZRevision history for this page on the wikiMediaWiki 1.11.2http://52.214.119.220/wiki/index.php?title=User:Anthony_Milto/Sandbox_1&diff=2496864&oldid=prevAnthony Milto at 21:57, 28 October 20152015-10-28T21:57:56Z<p></p>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>==DNA Interaction ==</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>==DNA Interaction ==</div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div>MyoD, along with most other bHLH proteins, recognizes the <del style="color: red; font-weight: bold; text-decoration: none;">concensus </del>DNA sequence CAN NTG, where N can be any base. This sequence is known as the E-box and is bound by MyoD's <scene name='71/714943/Br_dna_interaction/4'>basic region</scene> (basic residues pictured in blue, acidic in red) in DNA's major groove. MyoD's basic region residues indirectly establish selectivity for specific E-box sequences by influencing the conformation in which the basic region binds DNA. There are <scene name='71/714943/Dna_interacting_aas/1'>four residues</scene> responsible for the DNA interaction that provides MyoD's myogenic effect: Arg111, Ala114, Thr115, and Lys124. The <del style="color: red; font-weight: bold; text-decoration: none;">former three </del>residues <del style="color: red; font-weight: bold; text-decoration: none;">directly contact </del>the <del style="color: red; font-weight: bold; text-decoration: none;">bases </del>in DNA's major groove<del style="color: red; font-weight: bold; text-decoration: none;">, while the latter likely interacts </del>with the <del style="color: red; font-weight: bold; text-decoration: none;">backbone phosphate groups </del><ref>Kophengnavong, T., Michnowicz, J. E., & Blackwell, T. K. Establishment of Distinct MyoD, E2A, and Twist DNA Binding Specificities by Different Basic Region-DNA Conformations. Molecular and Cellular Biology, '''2000''', 20. 261–272.</ref>.</div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>MyoD, along with most other bHLH proteins, recognizes the <ins style="color: red; font-weight: bold; text-decoration: none;">consensus </ins>DNA sequence CAN NTG, where N can be any base. This sequence is known as the <ins style="color: red; font-weight: bold; text-decoration: none;"><scene name='71/714943/</ins>E-box<ins style="color: red; font-weight: bold; text-decoration: none;">/2'>E-box</scene> </ins>and is bound by MyoD's <scene name='71/714943/Br_dna_interaction/4'>basic region</scene> (basic residues pictured in blue, acidic in red) in DNA's major groove. MyoD's basic region residues indirectly establish selectivity for specific E-box sequences by influencing the conformation in which the basic region binds DNA. There are <scene name='71/714943/Dna_interacting_aas/1'>four residues</scene> responsible for the DNA interaction that provides MyoD's myogenic effect: Arg111, Ala114, Thr115, and Lys124. The <ins style="color: red; font-weight: bold; text-decoration: none;">lysine and arginine </ins>residues <ins style="color: red; font-weight: bold; text-decoration: none;">are situated near </ins>the <ins style="color: red; font-weight: bold; text-decoration: none;">backbone of the DNA and interact with the backbone phosphate groups and create a type of phosphate clamp, while the alanine and threonine are </ins>in DNA's major groove <ins style="color: red; font-weight: bold; text-decoration: none;">and interact </ins>with the <ins style="color: red; font-weight: bold; text-decoration: none;">DNA's bases </ins><ref>Kophengnavong, T., Michnowicz, J. E., & Blackwell, T. K. Establishment of Distinct MyoD, E2A, and Twist DNA Binding Specificities by Different Basic Region-DNA Conformations. Molecular and Cellular Biology, '''2000''', 20. 261–272.</ref>. </div></td></tr>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>== Regulation ==</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>== Regulation ==</div></td></tr>
</table>Anthony Miltohttp://52.214.119.220/wiki/index.php?title=User:Anthony_Milto/Sandbox_1&diff=2496863&oldid=prevAnthony Milto at 21:49, 28 October 20152015-10-28T21:49:19Z<p></p>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>==Structure==</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>==Structure==</div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div>MyoD has a basic region at its amino-terminal end, which functions in binding the transcription factor to a region of the DNA known as the E-box. At the carboxyl-terminal end is MyoD's <scene name='71/714943/Hlh/2'>HLH domain</scene>. The HLH domain functions in <scene name='71/714943/Hlh_interaction_segment/<del style="color: red; font-weight: bold; text-decoration: none;">4</del>'>protein-protein interactions</scene> and forms homodimeric and heterodimeric complexes through a combination of hydrophobic interactions and hydrogen bonding (hydrophobic residues in gray, hydrogen bonding in purple) <ref>DOI: 10.1186/gb-2004-5-6-226</ref>.MyoD also contains an acidic activation domain. The activity of this activation domain has been observed to increase drastically upon deletion of residues in other parts of the protein. This suggests that the acidic activation domain is buried within the protein in vivo and can be activated by subtle changes in structure <ref>Weintraub, H., Dwarki, V. J., Verma, I., Davis, R., Hollenberg, S., Snider, L., Lassar, A., Tapscott, S. J. Muscle-specific transcriptional activation</div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>MyoD has a basic region at its amino-terminal end, which functions in binding the transcription factor to a region of the DNA known as the E-box. At the carboxyl-terminal end is MyoD's <scene name='71/714943/Hlh/2'>HLH domain</scene>. The HLH domain functions in <scene name='71/714943/Hlh_interaction_segment/<ins style="color: red; font-weight: bold; text-decoration: none;">5</ins>'>protein-protein interactions</scene> and forms homodimeric and heterodimeric complexes through a combination of hydrophobic interactions and hydrogen bonding (hydrophobic residues in gray, hydrogen bonding in purple) <ref>DOI: 10.1186/gb-2004-5-6-226</ref>.MyoD also contains an acidic activation domain. The activity of this activation domain has been observed to increase drastically upon deletion of residues in other parts of the protein. This suggests that the acidic activation domain is buried within the protein in vivo and can be activated by subtle changes in structure <ref>Weintraub, H., Dwarki, V. J., Verma, I., Davis, R., Hollenberg, S., Snider, L., Lassar, A., Tapscott, S. J. Muscle-specific transcriptional activation</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>by MyoD. Genes & Dev. '''1991'''. 5. 1377-1386 </ref>.</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>by MyoD. Genes & Dev. '''1991'''. 5. 1377-1386 </ref>.</div></td></tr>
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</table>Anthony Miltohttp://52.214.119.220/wiki/index.php?title=User:Anthony_Milto/Sandbox_1&diff=2496862&oldid=prevAnthony Milto at 21:47, 28 October 20152015-10-28T21:47:50Z<p></p>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>==Structure==</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>==Structure==</div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div>MyoD has a basic region at its amino-terminal end, which functions in binding the transcription factor to a region of the DNA known as the E-box. At the carboxyl-terminal end is MyoD's <scene name='71/714943/Hlh/2'>HLH domain</scene>. The HLH domain functions in <scene name='71/714943/Hlh_interaction_segment/<del style="color: red; font-weight: bold; text-decoration: none;">3</del>'>protein-protein interactions</scene> and forms homodimeric and heterodimeric complexes through a combination of hydrophobic interactions and hydrogen bonding (hydrophobic residues in gray, hydrogen bonding in purple) <ref>DOI: 10.1186/gb-2004-5-6-226</ref>.MyoD also contains an acidic activation domain. The activity of this activation domain has been observed to increase drastically upon deletion of residues in other parts of the protein. This suggests that the acidic activation domain is buried within the protein in vivo and can be activated by subtle changes in structure <ref>Weintraub, H., Dwarki, V. J., Verma, I., Davis, R., Hollenberg, S., Snider, L., Lassar, A., Tapscott, S. J. Muscle-specific transcriptional activation</div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>MyoD has a basic region at its amino-terminal end, which functions in binding the transcription factor to a region of the DNA known as the E-box. At the carboxyl-terminal end is MyoD's <scene name='71/714943/Hlh/2'>HLH domain</scene>. The HLH domain functions in <scene name='71/714943/Hlh_interaction_segment/<ins style="color: red; font-weight: bold; text-decoration: none;">4</ins>'>protein-protein interactions</scene> and forms homodimeric and heterodimeric complexes through a combination of hydrophobic interactions and hydrogen bonding (hydrophobic residues in gray, hydrogen bonding in purple) <ref>DOI: 10.1186/gb-2004-5-6-226</ref>.MyoD also contains an acidic activation domain. The activity of this activation domain has been observed to increase drastically upon deletion of residues in other parts of the protein. This suggests that the acidic activation domain is buried within the protein in vivo and can be activated by subtle changes in structure <ref>Weintraub, H., Dwarki, V. J., Verma, I., Davis, R., Hollenberg, S., Snider, L., Lassar, A., Tapscott, S. J. Muscle-specific transcriptional activation</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>by MyoD. Genes & Dev. '''1991'''. 5. 1377-1386 </ref>.</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>by MyoD. Genes & Dev. '''1991'''. 5. 1377-1386 </ref>.</div></td></tr>
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</table>Anthony Miltohttp://52.214.119.220/wiki/index.php?title=User:Anthony_Milto/Sandbox_1&diff=2496861&oldid=prevAnthony Milto at 21:45, 28 October 20152015-10-28T21:45:03Z<p></p>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>==Structure==</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>==Structure==</div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div>MyoD has a basic region at its amino-terminal end, which functions in binding the transcription factor to a region of the DNA known as the E-box. At the carboxyl-terminal end is MyoD's <scene name='71/714943/Hlh/2'>HLH domain</scene>. The HLH domain functions in <scene name='71/714943/Hlh_interaction_segment/<del style="color: red; font-weight: bold; text-decoration: none;">2</del>'>protein-protein interactions</scene> and forms homodimeric and heterodimeric complexes through a combination of hydrophobic interactions and hydrogen bonding (hydrophobic residues in gray, hydrogen bonding in purple) <ref>DOI: 10.1186/gb-2004-5-6-226</ref>.MyoD also contains an acidic activation domain. The activity of this activation domain has been observed to increase drastically upon deletion of residues in other parts of the protein. This suggests that the acidic activation domain is buried within the protein in vivo and can be activated by subtle changes in structure <ref>Weintraub, H., Dwarki, V. J., Verma, I., Davis, R., Hollenberg, S., Snider, L., Lassar, A., Tapscott, S. J. Muscle-specific transcriptional activation</div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>MyoD has a basic region at its amino-terminal end, which functions in binding the transcription factor to a region of the DNA known as the E-box. At the carboxyl-terminal end is MyoD's <scene name='71/714943/Hlh/2'>HLH domain</scene>. The HLH domain functions in <scene name='71/714943/Hlh_interaction_segment/<ins style="color: red; font-weight: bold; text-decoration: none;">3</ins>'>protein-protein interactions</scene> and forms homodimeric and heterodimeric complexes through a combination of hydrophobic interactions and hydrogen bonding (hydrophobic residues in gray, hydrogen bonding in purple) <ref>DOI: 10.1186/gb-2004-5-6-226</ref>.MyoD also contains an acidic activation domain. The activity of this activation domain has been observed to increase drastically upon deletion of residues in other parts of the protein. This suggests that the acidic activation domain is buried within the protein in vivo and can be activated by subtle changes in structure <ref>Weintraub, H., Dwarki, V. J., Verma, I., Davis, R., Hollenberg, S., Snider, L., Lassar, A., Tapscott, S. J. Muscle-specific transcriptional activation</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>by MyoD. Genes & Dev. '''1991'''. 5. 1377-1386 </ref>.</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>by MyoD. Genes & Dev. '''1991'''. 5. 1377-1386 </ref>.</div></td></tr>
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</table>Anthony Miltohttp://52.214.119.220/wiki/index.php?title=User:Anthony_Milto/Sandbox_1&diff=2496860&oldid=prevAnthony Milto at 21:41, 28 October 20152015-10-28T21:41:02Z<p></p>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>==Structure==</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>==Structure==</div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div>MyoD has a basic region at its amino-terminal end, which functions in binding the transcription factor to a region of the DNA known as the E-box. At the carboxyl-terminal end is MyoD's <scene name='71/714943/Hlh/2'>HLH domain</scene>. The HLH domain functions in <scene name='71/714943/<del style="color: red; font-weight: bold; text-decoration: none;">Hlh_interaction</del>/<del style="color: red; font-weight: bold; text-decoration: none;">1</del>'>protein-protein interactions</scene> and forms homodimeric and heterodimeric complexes <ref>DOI: 10.1186/gb-2004-5-6-226</ref>.MyoD also contains an acidic activation domain. The activity of this activation domain has been observed to increase drastically upon deletion of residues in other parts of the protein. This suggests that the acidic activation domain is buried within the protein in vivo and can be activated by subtle changes in structure <ref>Weintraub, H., Dwarki, V. J., Verma, I., Davis, R., Hollenberg, S., Snider, L., Lassar, A., Tapscott, S. J. Muscle-specific transcriptional activation</div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>MyoD has a basic region at its amino-terminal end, which functions in binding the transcription factor to a region of the DNA known as the E-box. At the carboxyl-terminal end is MyoD's <scene name='71/714943/Hlh/2'>HLH domain</scene>. The HLH domain functions in <scene name='71/714943/<ins style="color: red; font-weight: bold; text-decoration: none;">Hlh_interaction_segment</ins>/<ins style="color: red; font-weight: bold; text-decoration: none;">2</ins>'>protein-protein interactions</scene> and forms homodimeric and heterodimeric complexes <ins style="color: red; font-weight: bold; text-decoration: none;">through a combination of hydrophobic interactions and hydrogen bonding (hydrophobic residues in gray, hydrogen bonding in purple) </ins><ref>DOI: 10.1186/gb-2004-5-6-226</ref>.MyoD also contains an acidic activation domain. The activity of this activation domain has been observed to increase drastically upon deletion of residues in other parts of the protein. This suggests that the acidic activation domain is buried within the protein in vivo and can be activated by subtle changes in structure <ref>Weintraub, H., Dwarki, V. J., Verma, I., Davis, R., Hollenberg, S., Snider, L., Lassar, A., Tapscott, S. J. Muscle-specific transcriptional activation</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>by MyoD. Genes & Dev. '''1991'''. 5. 1377-1386 </ref>.</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>by MyoD. Genes & Dev. '''1991'''. 5. 1377-1386 </ref>.</div></td></tr>
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</table>Anthony Miltohttp://52.214.119.220/wiki/index.php?title=User:Anthony_Milto/Sandbox_1&diff=2496858&oldid=prevAnthony Milto at 21:06, 28 October 20152015-10-28T21:06:54Z<p></p>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>==MyoD==</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>==MyoD==</div></td></tr>
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<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div><StructureSection load=<del style="color: red; font-weight: bold; text-decoration: none;">''71/714943/Myod_bhlh_domain/1</del>'' size='340' side='right' caption='Crystal Structure of MyoD Homodimer bHLH Domain' scene=''></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div><StructureSection load='' size='340' side='right' caption='Crystal Structure of MyoD Homodimer bHLH Domain' scene='<ins style="color: red; font-weight: bold; text-decoration: none;">71/714943/Myod_bhlh_domain/1</ins>'></div></td></tr>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>==Function and Classification==</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>==Function and Classification==</div></td></tr>
</table>Anthony Miltohttp://52.214.119.220/wiki/index.php?title=User:Anthony_Milto/Sandbox_1&diff=2496857&oldid=prevAnthony Milto at 20:30, 28 October 20152015-10-28T20:30:34Z<p></p>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>==MyoD==</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>==MyoD==</div></td></tr>
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<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div><StructureSection load='<del style="color: red; font-weight: bold; text-decoration: none;"><scene name=</del>'71/714943/Myod_bhlh_domain/1'<del style="color: red; font-weight: bold; text-decoration: none;">></del>' size='340' side='right' caption='Crystal Structure of MyoD Homodimer bHLH Domain' scene=''></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div><StructureSection load=''71/714943/Myod_bhlh_domain/1'' size='340' side='right' caption='Crystal Structure of MyoD Homodimer bHLH Domain' scene=''></div></td></tr>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>==Function and Classification==</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>==Function and Classification==</div></td></tr>
</table>Anthony Miltohttp://52.214.119.220/wiki/index.php?title=User:Anthony_Milto/Sandbox_1&diff=2496856&oldid=prevAnthony Milto at 20:29, 28 October 20152015-10-28T20:29:51Z<p></p>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>==Function and Classification==</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>==Function and Classification==</div></td></tr>
</table>Anthony Miltohttp://52.214.119.220/wiki/index.php?title=User:Anthony_Milto/Sandbox_1&diff=2496855&oldid=prevAnthony Milto at 20:27, 28 October 20152015-10-28T20:27:08Z<p></p>
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<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div><StructureSection load='<del style="color: red; font-weight: bold; text-decoration: none;">1mdy</del>' size='340' side='right' caption='Crystal Structure of MyoD Homodimer bHLH Domain' scene=''></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div><StructureSection load='<ins style="color: red; font-weight: bold; text-decoration: none;">71/714943/Myod_bhlh_domain/1</ins>' size='340' side='right' caption='Crystal Structure of MyoD Homodimer bHLH Domain' scene=''></div></td></tr>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>==Function and Classification==</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>==Function and Classification==</div></td></tr>
</table>Anthony Miltohttp://52.214.119.220/wiki/index.php?title=User:Anthony_Milto/Sandbox_1&diff=2496854&oldid=prevAnthony Milto at 20:21, 28 October 20152015-10-28T20:21:56Z<p></p>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>==Structure==</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>==Structure==</div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div>MyoD has a basic region at its amino-terminal end, which functions in binding the transcription factor to a region of the DNA known as the E-box. At the carboxyl-terminal end is MyoD's <scene name='71/714943/Hlh/<del style="color: red; font-weight: bold; text-decoration: none;">1</del>'>HLH domain</scene>. The HLH domain functions in <scene name='71/714943/Hlh_interaction/1'>protein-protein interactions</scene> and forms homodimeric and heterodimeric complexes <ref>DOI: 10.1186/gb-2004-5-6-226</ref>.MyoD also contains an acidic activation domain. The activity of this activation domain has been observed to increase drastically upon deletion of residues in other parts of the protein. This suggests that the acidic activation domain is buried within the protein in vivo and can be activated by subtle changes in structure <ref>Weintraub, H., Dwarki, V. J., Verma, I., Davis, R., Hollenberg, S., Snider, L., Lassar, A., Tapscott, S. J. Muscle-specific transcriptional activation</div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>MyoD has a basic region at its amino-terminal end, which functions in binding the transcription factor to a region of the DNA known as the E-box. At the carboxyl-terminal end is MyoD's <scene name='71/714943/Hlh/<ins style="color: red; font-weight: bold; text-decoration: none;">2</ins>'>HLH domain</scene>. The HLH domain functions in <scene name='71/714943/Hlh_interaction/1'>protein-protein interactions</scene> and forms homodimeric and heterodimeric complexes <ref>DOI: 10.1186/gb-2004-5-6-226</ref>.MyoD also contains an acidic activation domain. The activity of this activation domain has been observed to increase drastically upon deletion of residues in other parts of the protein. This suggests that the acidic activation domain is buried within the protein in vivo and can be activated by subtle changes in structure <ref>Weintraub, H., Dwarki, V. J., Verma, I., Davis, R., Hollenberg, S., Snider, L., Lassar, A., Tapscott, S. J. Muscle-specific transcriptional activation</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>by MyoD. Genes & Dev. '''1991'''. 5. 1377-1386 </ref>.</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>by MyoD. Genes & Dev. '''1991'''. 5. 1377-1386 </ref>.</div></td></tr>
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</table>Anthony Milto