MLP - Revision history

https://proteopedia.org/index.php?action=history&feed=atom&title=MLP MLP - Revision history 2026-10-04T23:00:52Z Revision history for this page on the wiki MediaWiki 1.43.8 https://proteopedia.org/index.php?title=MLP&diff=1534337&oldid=prev Nikos Pinotsis: Replacing page with 'http://www.proteopedia.org/wiki/index.php/Group:MUZIC:MLP' 2012-09-13T15:49:41Z

<p>Replacing page with 'http://www.proteopedia.org/wiki/index.php/Group:MUZIC:MLP'</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 15:49, 13 September 2012</td> </tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l1">Line 1:</td> <td colspan="2" class="diff-lineno">Line 1:</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;">Three members of Cysteine rich proteins (CRPs) have been identified in vertebrates</del>. <del style="font-weight: bold; text-decoration: none;">CRP3 is localized in Z and M-lines in striated muscles and also called '''Muscle LIM protein''' (MLP)</del>. <del style="font-weight: bold; text-decoration: none;">All three proteins are associated with the actin cytoskeleton and play similar functions in different muscle varieties</del>. <del style="font-weight: bold; text-decoration: none;">CRPs 1-3 contain 192-194 residues and consist of two LIM domains with the adjacent flexible glycine reach linker region. Each LIM domain comprises two Zn-binding motifs CCHC and CCCC and represents structural and presumably functional independent unit. LIM domains have been intensively characterized using NMR. The solution structures exist for human </del>MLP <del style="font-weight: bold; text-decoration: none;">and other vertebrate CRPs family members. The interactions of MLP with α-actinin, telethonin (T-Cap), βI-spectrin, N-RAP (Nebulin-related-anchoring protein) and cofilin2 (CFL2) have been shown, suggesting its essential role as a scaffold protein in the sarcomere. Potential role of MLP in myogenesis has been reported through the complex formation with muscle helix-loop-helix transcription factors MyoD, MRF4 and myogenin. The mutations of MLP are found in cardiac myopathies.</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><ins style="font-weight: bold; text-decoration: none;">http://www</ins>.<ins style="font-weight: bold; text-decoration: none;">proteopedia</ins>.<ins style="font-weight: bold; text-decoration: none;">org/wiki/index</ins>.<ins style="font-weight: bold; text-decoration: none;">php/Group:MUZIC:</ins>MLP</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><del style="font-weight: bold; text-decoration: none;">[[ref]]</del></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> </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;"><Structure load='2o10' size='200' frame='true' align='right' caption='NMR structure of human muscle LIM protein 3 with Zn+2 ions, [[2o10]]' scene='Insert optional scene name here' /></del></div></td><td colspan="2" class="diff-side-added"></td></tr> </table>

Nikos Pinotsis https://proteopedia.org/index.php?title=MLP&diff=1512821&oldid=prev Michal Harel at 12:19, 7 August 2012 2012-08-07T12:19:10Z

<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 12:19, 7 August 2012</td> </tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l1">Line 1:</td> <td colspan="2" class="diff-lineno">Line 1:</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>Three members of Cysteine rich proteins (CRPs) have been identified in vertebrates. CRP3 is localized in Z and M-lines in striated muscles and also called Muscle LIM protein (MLP). All three proteins are associated with the actin cytoskeleton and play similar functions in different muscle varieties. CRPs 1-3 contain 192-194 residues and consist of two LIM domains with the adjacent flexible glycine reach linker region. Each LIM domain comprises two Zn-binding motifs CCHC and CCCC and represents structural and presumably functional independent unit. LIM domains have been intensively characterized using NMR. The solution structures exist for human MLP and other vertebrate CRPs family members. The interactions of MLP with α-actinin, telethonin (T-Cap), βI-spectrin, N-RAP (Nebulin-related-anchoring protein) and cofilin2 (CFL2) have been shown, suggesting its essential role as a scaffold protein in the sarcomere. Potential role of MLP in myogenesis has been reported through the complex formation with muscle helix-loop-helix transcription factors MyoD, MRF4 and myogenin. The mutations of MLP are found in cardiac myopathies.</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>Three members of Cysteine rich proteins (CRPs) have been identified in vertebrates. CRP3 is localized in Z and M-lines in striated muscles and also called <ins style="font-weight: bold; text-decoration: none;">'''</ins>Muscle LIM protein<ins style="font-weight: bold; text-decoration: none;">''' </ins>(MLP). All three proteins are associated with the actin cytoskeleton and play similar functions in different muscle varieties. CRPs 1-3 contain 192-194 residues and consist of two LIM domains with the adjacent flexible glycine reach linker region. Each LIM domain comprises two Zn-binding motifs CCHC and CCCC and represents structural and presumably functional independent unit. LIM domains have been intensively characterized using NMR. The solution structures exist for human MLP and other vertebrate CRPs family members. The interactions of MLP with α-actinin, telethonin (T-Cap), βI-spectrin, N-RAP (Nebulin-related-anchoring protein) and cofilin2 (CFL2) have been shown, suggesting its essential role as a scaffold protein in the sarcomere. Potential role of MLP in myogenesis has been reported through the complex formation with muscle helix-loop-helix transcription factors MyoD, MRF4 and myogenin. The mutations of MLP are found in cardiac myopathies.</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>[[ref]]</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>[[ref]]</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><Structure load='2o10' size='200' frame='true' align='right' caption='<del style="font-weight: bold; text-decoration: none;">Insert caption here</del>' scene='Insert optional scene name here' /></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><Structure load='2o10' size='200' frame='true' align='right' caption='<ins style="font-weight: bold; text-decoration: none;">NMR structure of human muscle LIM protein 3 with Zn+2 ions, [[2o10]]</ins>' scene='Insert optional scene name here' /></div></td></tr> </table>

Michal Harel https://proteopedia.org/index.php?title=MLP&diff=1265751&oldid=prev Nikos Pinotsis at 14:35, 4 July 2011 2011-07-04T14:35:03Z

<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 14:35, 4 July 2011</td> </tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l2">Line 2:</td> <td colspan="2" class="diff-lineno">Line 2:</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>[[ref]]</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>[[ref]]</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><Structure load='2o10' size='<del style="font-weight: bold; text-decoration: none;">500</del>' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /></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><Structure load='2o10' size='<ins style="font-weight: bold; text-decoration: none;">200</ins>' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /></div></td></tr> </table>

Nikos Pinotsis https://proteopedia.org/index.php?title=MLP&diff=1261450&oldid=prev Nikos Pinotsis at 13:13, 23 June 2011 2011-06-23T13:13:57Z

<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 13:13, 23 June 2011</td> </tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l1">Line 1:</td> <td colspan="2" class="diff-lineno">Line 1:</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>Three members of Cysteine rich proteins (CRPs) have been identified in vertebrates. CRP3 is localized in Z and M-lines in striated muscles and also called Muscle LIM protein (MLP). All three proteins are associated with the actin cytoskeleton and play similar functions in different muscle varieties. CRPs 1-3 contain 192-194 residues and consist of two LIM domains with the adjacent flexible glycine reach linker region. Each LIM domain comprises two Zn-binding motifs CCHC and CCCC and represents structural and presumably functional independent unit. LIM domains have been intensively characterized using NMR. The solution structures exist for human MLP and other vertebrate CRPs family members. The interactions of MLP with α-actinin, telethonin (T-Cap), βI-spectrin, N-RAP (Nebulin-related-anchoring protein) and cofilin2 (CFL2) have been shown, suggesting its essential role as a scaffold protein in the sarcomere. Potential role of MLP in myogenesis has been reported through the complex formation with muscle helix-loop-helix transcription factors MyoD, MRF4 and myogenin. The mutations of MLP are found in cardiac myopathies.</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>Three members of Cysteine rich proteins (CRPs) have been identified in vertebrates. CRP3 is localized in Z and M-lines in striated muscles and also called Muscle LIM protein (MLP). All three proteins are associated with the actin cytoskeleton and play similar functions in different muscle varieties. CRPs 1-3 contain 192-194 residues and consist of two LIM domains with the adjacent flexible glycine reach linker region. Each LIM domain comprises two Zn-binding motifs CCHC and CCCC and represents structural and presumably functional independent unit. LIM domains have been intensively characterized using NMR. The solution structures exist for human MLP and other vertebrate CRPs family members. The interactions of MLP with α-actinin, telethonin (T-Cap), βI-spectrin, N-RAP (Nebulin-related-anchoring protein) and cofilin2 (CFL2) have been shown, suggesting its essential role as a scaffold protein in the sarcomere. Potential role of MLP in myogenesis has been reported through the complex formation with muscle helix-loop-helix transcription factors MyoD, MRF4 and myogenin. The mutations of MLP are found in cardiac myopathies.</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 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;">[[ref]]</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><Structure load='2o10' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /></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><Structure load='2o10' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /></div></td></tr> </table>

Nikos Pinotsis https://proteopedia.org/index.php?title=MLP&diff=1261436&oldid=prev Nikos Pinotsis at 12:54, 23 June 2011 2011-06-23T12:54:11Z

<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 12:54, 23 June 2011</td> </tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l1">Line 1:</td> <td colspan="2" class="diff-lineno">Line 1:</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>Three members of Cysteine rich proteins (CRPs) have been identified in vertebrates. CRP3 is localized in Z and M-lines in striated muscles and also called Muscle LIM protein (MLP). All three proteins are associated with the actin cytoskeleton and play similar functions in different muscle varieties. CRPs 1-3 contain 192-194 residues and consist of two LIM domains with the adjacent flexible glycine reach linker region. Each LIM domain comprises two Zn-binding motifs CCHC and CCCC and represents structural and presumably functional independent unit. LIM domains have been intensively characterized using NMR. The solution structures exist for human MLP and other vertebrate CRPs family members. The interactions of MLP with α-actinin, telethonin (T-Cap), βI-spectrin, N-RAP (Nebulin-related-anchoring protein) and cofilin2 (CFL2) have been shown, suggesting its essential role as a scaffold protein in the sarcomere. Potential role of MLP in myogenesis has been reported through the complex formation with muscle helix-loop-helix transcription factors MyoD, MRF4 and myogenin. The mutations of MLP are found in cardiac myopathies.</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>Three members of Cysteine rich proteins (CRPs) have been identified in vertebrates. CRP3 is localized in Z and M-lines in striated muscles and also called Muscle LIM protein (MLP). All three proteins are associated with the actin cytoskeleton and play similar functions in different muscle varieties. CRPs 1-3 contain 192-194 residues and consist of two LIM domains with the adjacent flexible glycine reach linker region. Each LIM domain comprises two Zn-binding motifs CCHC and CCCC and represents structural and presumably functional independent unit. LIM domains have been intensively characterized using NMR. The solution structures exist for human MLP and other vertebrate CRPs family members. The interactions of MLP with α-actinin, telethonin (T-Cap), βI-spectrin, N-RAP (Nebulin-related-anchoring protein) and cofilin2 (CFL2) have been shown, suggesting its essential role as a scaffold protein in the sarcomere. Potential role of MLP in myogenesis has been reported through the complex formation with muscle helix-loop-helix transcription factors MyoD, MRF4 and myogenin. The mutations of MLP are found in cardiac myopathies.</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><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> </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;"><Structure load='2o10' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /</ins>></div></td></tr> </table>

Nikos Pinotsis https://proteopedia.org/index.php?title=MLP&diff=1261433&oldid=prev Nikos Pinotsis: New page: <!-- Three members of Cysteine rich proteins (CRPs) have been identified in vertebrates. CRP3 is localized in Z and M-lines in striated muscles and also called Muscle LIM protein (MLP). Al... 2011-06-23T12:52:40Z

<p>New page: </div>

Nikos Pinotsis