Sandbox Reserved 1656

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==== Function ====
==== Function ====
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Deubiquitinases or Deubiquitinating enzymes (DUBs) are key enzymes belonging to the vast group of proteases, allowing the degradation of ubiquitin of proteins. These enzymes are thus implicated in the regulation of protein degradation. Indeed, when a protein is going to be degraded, an enzymatic cascade will add a poly-ubiquitin fragment to the protein. This mechanism is called ubiquitination.[https://fr.wikipedia.org/wiki/Ubiquitination] Following this step, mono or poly-ubiquitin is removed from the protein which has been degraded, by deubiquitinase.
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Deubiquitinases or Deubiquitinating enzymes (DUBs) are key enzymes belonging to the vast group of proteases, allowing the degradation of ubiquitin of proteins. These enzymes are thus implicated in the regulation of protein degradation. Indeed, when a protein is going to be degraded, an enzymatic cascade will add a poly-ubiquitin fragment to the protein. This mechanism is called ubiquitination.[https://fr.wikipedia.org/wiki/Ubiquitination] Following this step, mono or poly-ubiquitin is removed from the protein which has been degraded, by deubiquitinase. <ref>PMID:9409543</ref>
==== Families ====
==== Families ====

Revision as of 10:49, 9 January 2021

This Sandbox is Reserved from 26/11/2020, through 26/11/2021 for use in the course "Structural Biology" taught by Bruno Kieffer at the University of Strasbourg, ESBS. This reservation includes Sandbox Reserved 1643 through Sandbox Reserved 1664.
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Deubiquitinase

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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. ↑ Wilkinson KD. Regulation of ubiquitin-dependent processes by deubiquitinating enzymes. FASEB J. 1997 Dec;11(14):1245-56. PMID:9409543
  4. ↑ Amerik AY, Hochstrasser M. Mechanism and function of deubiquitinating enzymes. Biochim Biophys Acta. 2004 Nov 29;1695(1-3):189-207. doi:, 10.1016/j.bbamcr.2004.10.003. PMID:15571815 doi:http://dx.doi.org/10.1016/j.bbamcr.2004.10.003
  5. ↑ Johnston SC, Larsen CN, Cook WJ, Wilkinson KD, Hill CP. Crystal structure of a deubiquitinating enzyme (human UCH-L3) at 1.8 A resolution. EMBO J. 1997 Jul 1;16(13):3787-96. PMID:9233788 doi:http://dx.doi.org/10.1093/emboj/16.13.3787
  6. ↑ Hamner JB. Applying the Roy adaptation model to the CCU. Crit Care Nurse. 1989 Mar;9(3):51-61. PMID:2582804
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