To install click the Add extension button. That's it.

The source code for the WIKI 2 extension is being checked by specialists of the Mozilla Foundation, Google, and Apple. You could also do it yourself at any point in time.

4,5
Kelly Slayton
Congratulations on this excellent venture… what a great idea!
Alexander Grigorievskiy
I use WIKI 2 every day and almost forgot how the original Wikipedia looks like.
Live Statistics
English Articles
Improved in 24 Hours
Added in 24 Hours
What we do. Every page goes through several hundred of perfecting techniques; in live mode. Quite the same Wikipedia. Just better.
.
Leo
Newton
Brights
Milds

Propionylation

From Wikipedia, the free encyclopedia

Propionylation is a post-translational modification of proteins, in which a propionyl-group is added to a lysine amino acid of a protein. Propionylation participates in crucial biological processes, including metabolic processes and cellular stress response.[1]

Lysine propionylation was first identified on histone proteins,[2] and since has also been identified on other proteins.[3] Histone propionylation is a mark of active chromatin.[4] The substrate for protein propionylation is propionyl-CoA. Propionyl-CoA in the cell is metabolised by the enzyme propionyl-CoA carboxylase. Accumulation of propionyl-CoA leads to increased protein propionylation.[5]

In patients with propionic acidemia, a rare autosomal recessive metabolic disorder, propionyl-CoA levels elevated and increased propionylation,[6] which might contribute to the pathology in these patients.[5]

References

  1. ^ Shui, Ke; Wang, Chenwei; Zhang, Xuedi; Ma, Shanshan; Li, Qinyu; Ning, Wanshan; Zhang, Weizhi; Chen, Miaomiao; Peng, Di; Hu, Hui; Fang, Zheng; Guo, Anyuan; Gao, Guanjun; Ye, Mingliang; Zhang, Luoying (2023-05-17). "Small-sample learning reveals propionylation in determining global protein homeostasis". Nature Communications. 14 (1): 2813. Bibcode:2023NatCo..14.2813S. doi:10.1038/s41467-023-38414-8. ISSN 2041-1723. PMC 10192394. PMID 37198164.
  2. ^ Chen, Y; Sprung, R; Tang, Y; Ball, H; Sangras, B; Kim, SC; Falck, JR; Peng, J; Gu, W; Zhao, Y (May 2007). "Lysine propionylation and butyrylation are novel post-translational modifications in histones". Molecular & Cellular Proteomics. 6 (5): 812–9. doi:10.1074/mcp.M700021-MCP200. PMC 2911958. PMID 17267393.
  3. ^ Cheng, Z; Tang, Y; Chen, Y; Kim, S; Liu, H; Li, SS; Gu, W; Zhao, Y (January 2009). "Molecular characterization of propionyllysines in non-histone proteins". Molecular & Cellular Proteomics. 8 (1): 45–52. doi:10.1074/mcp.M800224-MCP200. PMC 2621001. PMID 18753126.
  4. ^ Kebede, Adam F.; Nieborak, Anna; Shahidian, Lara Zorro; Le Gras, Stephanie; Richter, Florian; Gómez, Diana Aguilar; Baltissen, Marijke P.; Meszaros, Gergo; Magliarelli, Helena de Fatima; Taudt, Aaron; Margueron, Raphael (December 2017). "Histone propionylation is a mark of active chromatin". Nature Structural & Molecular Biology. 24 (12): 1048–1056. doi:10.1038/nsmb.3490. hdl:2066/207705. ISSN 1545-9985. PMID 29058708. S2CID 9788234.
  5. ^ a b Lagerwaard, Bart; Pougovkina, Olga; Bekebrede, Anna F.; Brinke, Heleen; Wanders, Ronald J.A.; Nieuwenhuizen, Arie G.; Keijer, Jaap; Boer, Vincent C. J. (2020-08-17). "Increased protein propionylation contributes to mitochondrial dysfunction in liver cells and fibroblasts, but not in myotubes". Journal of Inherited Metabolic Disease. 44 (2): 438–449. doi:10.1002/jimd.12296. ISSN 0141-8955. PMC 8049071. PMID 32740932.
  6. ^ Pougovkina, Olga; Te Brinke, Heleen; Wanders, Ronald J. A.; Houten, Sander M.; de Boer, Vincent C. J. (September 2014). "Aberrant protein acylation is a common observation in inborn errors of acyl-CoA metabolism". Journal of Inherited Metabolic Disease. 37 (5): 709–714. doi:10.1007/s10545-014-9684-9. ISSN 1573-2665. PMID 24531926. S2CID 26627794.
This page was last edited on 24 March 2024, at 11:29
Basis of this page is in Wikipedia. Text is available under the CC BY-SA 3.0 Unported License. Non-text media are available under their specified licenses. Wikipedia® is a registered trademark of the Wikimedia Foundation, Inc. WIKI 2 is an independent company and has no affiliation with Wikimedia Foundation.