Sandbox Reserved 1092

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==5JI1 : Myostatin (GDF8)==
==5JI1 : Myostatin (GDF8)==
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<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
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<StructureSection load='5JI1' size='340' side='right' caption='Caption for this structure' scene=''>
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This is a default text for your page '''Serine Protease'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
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This is a default text for your page '''Myostatin'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
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== Function ==
== Function ==
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== Structure/ Structural highlights ==
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== Structure==
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This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
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</StructureSection>
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If myostatin action is inhibited, researchers have noticed that muscular mass increases <ref name="edumont"/><ref name="patho"/>.Indeed, myostatin and particularly its inhibition can be a solution to cure muscle atrophy disease: let’s focus on the example of OPMD <ref> PMID:31066242</ref>, oculopharyngeal muscular dystrophy: This disease involves that the muscles affected show increased fibrosis and atrophy.This is a late-onset disease, affecting 1 people over 80000. It is characterized by dysphagia and ptosis but also limb weakness when the disease is at a very advanced stage. Researcher have noticed that the inhibition of myostatin, increased the muscle quantity and so it help to reduce the symptoms of OPMD.
If myostatin action is inhibited, researchers have noticed that muscular mass increases <ref name="edumont"/><ref name="patho"/>.Indeed, myostatin and particularly its inhibition can be a solution to cure muscle atrophy disease: let’s focus on the example of OPMD <ref> PMID:31066242</ref>, oculopharyngeal muscular dystrophy: This disease involves that the muscles affected show increased fibrosis and atrophy.This is a late-onset disease, affecting 1 people over 80000. It is characterized by dysphagia and ptosis but also limb weakness when the disease is at a very advanced stage. Researcher have noticed that the inhibition of myostatin, increased the muscle quantity and so it help to reduce the symptoms of OPMD.
In this case, a monoclonal antibiotic is injected to mice during 10 weeks and the results show that muscle strength and muscle fiber diameter increased and the expression of the markers of muscle fibrosis reduced. However, myostatin does not cure the disease because there was no change in intranuclear inclusion density which is a characteristic of OPMD spread, so, it only treats the symptom.
In this case, a monoclonal antibiotic is injected to mice during 10 weeks and the results show that muscle strength and muscle fiber diameter increased and the expression of the markers of muscle fibrosis reduced. However, myostatin does not cure the disease because there was no change in intranuclear inclusion density which is a characteristic of OPMD spread, so, it only treats the symptom.
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In other cases, it is also possible to introduce follistatin [[Category:Follistatin]] <ref> PMID:19644449</ref> to block myostatin because they will form a complex and so it will stop myostatin actions.
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In other cases, it is also possible to introduce follistatin <ref> PMID:19644449</ref> to block myostatin because they will form a complex and so it will stop myostatin actions.
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{{Serine_Protease}}
 
== Relevance ==
== Relevance ==
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==Structural highlights ==
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This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
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</StructureSection>
== References ==
== References ==
<references/>
<references/>

Revision as of 17:40, 11 January 2020

This Sandbox is Reserved from 25/11/2019, through 30/9/2020 for use in the course "Structural Biology" taught by Bruno Kieffer at the University of Strasbourg, ESBS. This reservation includes Sandbox Reserved 1091 through Sandbox Reserved 1115.
To get started:
  • Click the edit this page tab at the top. Save the page after each step, then edit it again.
  • show the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page.
  • Add a description of your scene. Use the buttons above the wikitext box for bold, italics, links, headlines, etc.

More help: Help:Editing

5JI1 : Myostatin (GDF8)

Caption for this structure

Drag the structure with the mouse to rotate

References

  1. Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
  2. Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
  3. 3.0 3.1 Université de Montpellier. Physiologie et médecien fondamentale du coeur et des muscles : myostatine. [1]
  4. 4.0 4.1 4.2 Carnac G, Vernus B, Bonnieu A. Myostatin in the pathophysiology of skeletal muscle. Curr Genomics. 2007 Nov;8(7):415-22. doi: 10.2174/138920207783591672. PMID:19412331 doi:http://dx.doi.org/10.2174/138920207783591672
  5. Jeffrey L. Corden,David Tollervey. Cell Biology, Chapter 36 Motor Proteins.2017 DOI:10.1016/B978-0-323-34126-4.00036-0
  6. 6.0 6.1 6.2 Sharma, M., McFarlane, C., Kambadur, R., Kukreti, H., Bonala, S. and Srinivasan, S. (2015), Myostatin: Expanding horizons. IUBMB Life, 67: 589-600. [ https://doi.org/10.1002/iub.1392 DOI:10.1002/iub.1392]
  7. Harish P, Malerba A, Lu-Nguyen N, Forrest L, Cappellari O, Roth F, Trollet C, Popplewell L, Dickson G. Inhibition of myostatin improves muscle atrophy in oculopharyngeal muscular dystrophy (OPMD). J Cachexia Sarcopenia Muscle. 2019 Oct;10(5):1016-1026. doi: 10.1002/jcsm.12438. , Epub 2019 May 7. PMID:31066242 doi:http://dx.doi.org/10.1002/jcsm.12438
  8. Cash JN, Rejon CA, McPherron AC, Bernard DJ, Thompson TB. The structure of myostatin:follistatin 288: insights into receptor utilization and heparin binding. EMBO J. 2009 Sep 2;28(17):2662-76. Epub 2009 Jul 30. PMID:19644449 doi:10.1038/emboj.2009.205
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