User:Jocelyn Munson/sandbox

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Summary of characteristics of target article

Our article should contain enough content so that sections and subsections are necessary, but excessive detailing is kept to a minimum. It should be written at a level that's easy for most readers to understand. The article must be written in a neutral and balanced way. It should contain reliable references and additional content such as tables, pictures, and diagrams. Plagiarism is not allowed.

Practice citations

p21, a protein that halts the cell cycle, is downregulated by histone deacetylase. Halting the cell cycle prevents the proliferation of tumors.[1] Therefore, p21 has potential in preventing the spread of cancer.[1] [2] Histone deacetylase inhibitors upregulate p21 expression. Histone deacetylase inhibitors have been shown to be possible pancreatic cancer treatments.[2]

Practice references

  1. ^ a b Fang, JY (2002 Jun). "Effects of histone acetylation and DNA methylation on p21( WAF1) regulation". World Journal of Gastroenterology : WJG. 8 (3): 400–5. doi:10.3748/wjg.v8.i3.400. PMC 4656409. PMID 12046058. {{cite journal}}: Check date values in: |date= (help); Unknown parameter |coauthors= ignored (|author= suggested) (help)CS1 maint: unflagged free DOI (link)
  2. ^ a b Wang, G (2012). "Class I and class II histone deacetylases are potential therapeutic targets for treating pancreatic cancer". PLOS ONE. 7 (12): e52095. doi:10.1371/journal.pone.0052095. PMC 3522644. PMID 23251689. {{cite journal}}: Unknown parameter |coauthors= ignored (|author= suggested) (help)

Possible references for PIAS article

Articles

Unit 5 references[1][2][3][4][5]

Additional article references[6][7][8][9][10][11][12]

Brief summaries

hZimp10,[6] a protein similar to PIAS, activates the tumor suppressor p53. This article also cites other studies relating to PIAS.

PIAS1 [7] and PIAS3 [8] inhibit NF-kappaB activity, which may aid in disease prevention.

PIAS1 may prevent adipogenesis via sumoylation, which may have implications in obesity treatment.[9]

This article provides a general overview of PIAS, including its roles in sumoylation. It also describes PIAS's structural domains.[10]

PIAS interacts with the TATA-binding protein [11]

PIAS1 inhibits STAT-1 mediated gene activation in response to interferon. [12]

JAK-STAT signaling pathway and autoimmune disease. There is also a diagram with the PIAS shown.[13]

Images

p53 binding domain of PIAS-1
p53 binding domain of PIAS-1.

Infoboxes

click edit to get infobox template for proteins

Identifiers
Symbol?

Preliminary outline for PIAS article

Lead section

Introduction and summary of PIAS

History/Discovery

-Seminal papers/ timing for discovery placeholder

Structure

Known structural motifs:

-RING-finger-like zinc-binding domain (RLD)

-N-terminal SAP (contains LXXLL signature motif - all PIAS proteins have it)

-PINIT

-S/T

-AD/SIM

Mechanisms

-sumoylation

-recruitment of histone deacetylases

-preventing transcription factors from binding to DNA

-sending transcription factors to co-repressor complexes within the nucleus

Functions

-repression of NF-kappaB pathway

-inhibition of STAT

Applications in disease treatment

-obesity

-cancer

-inflammatory/autoimmune disease

Current Research

-placeholder

Possible references

  1. ^ Leaman, DW (1996 Dec). "Regulation of STAT-dependent pathways by growth factors and cytokines". FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology. 10 (14): 1578–88. doi:10.1096/fasebj.10.14.9002549. PMID 9002549. {{cite journal}}: Check date values in: |date= (help); Unknown parameter |coauthors= ignored (|author= suggested) (help)CS1 maint: unflagged free DOI (link)
  2. ^ Bourgeais, Jérome (1 October 2013). "Oxidative metabolism in cancer: A STAT affair?". JAK-STAT. 2 (4): e25764. doi:10.4161/jkst.25764. PMC 3876433. PMID 24416651. {{cite journal}}: Unknown parameter |coauthors= ignored (|author= suggested) (help)
  3. ^ Timofeeva, OA (2012 Oct 1). "Alternative ways of modulating JAK-STAT pathway: Looking beyond phosphorylation". JAK-STAT. 1 (4): 274–284. doi:10.4161/jkst.22313. PMC 3670285. PMID 24058784. {{cite journal}}: Check date values in: |date= (help); Unknown parameter |coauthors= ignored (|author= suggested) (help)
  4. ^ Shuai, K (2006 Feb). "Regulation of cytokine signaling pathways by PIAS proteins". Cell Research. 16 (2): 196–202. doi:10.1038/sj.cr.7310027. PMID 16474434. {{cite journal}}: Check date values in: |date= (help)
  5. ^ Shuai, Ke; Liu, Bin (August 2005). "Regulation of gene-activation pathways by PIAS proteins in the immune system". Nature Reviews Immunology. 5 (8): 593–605. doi:10.1038/nri1667. PMID 16056253.
  6. ^ a b Lee, Jane; Beliakoff, Jason; Sun, Zijie (18 June 2007). "The novel PIAS-like protein hZimp10 is a transcriptional co-activator of the p53 tumor suppressor". Nucleic Acids Research. 35 (13): 4523–4534. doi:10.1093/nar/gkm476. PMC 1935018. PMID 17584785.
  7. ^ a b Liu, B.; Yang, R.; Wong, K. A.; Getman, C.; Stein, N.; Teitell, M. A.; Cheng, G.; Wu, H.; Shuai, K. (2005 Feb). "Negative regulation of NF-kappaB signaling by PIAS1". Molecular and Cellular Biology. 25 (3): 1113–23. doi:10.1128/MCB.25.3.1113-1123.2005. PMC 544018. PMID 15657437. {{cite journal}}: Check date values in: |date= (help)
  8. ^ a b Jang, H. D.; Yoon, K.; Shin, Y. J.; Kim, J.; Lee, S. Y. (2004 Jun 4). "PIAS3 suppresses NF-kappaB-mediated transcription by interacting with the p65/RelA subunit". The Journal of Biological Chemistry. 279 (23): 24873–80. doi:10.1074/jbc.M313018200. PMID 15140884. {{cite journal}}: Check date values in: |date= (help)
  9. ^ a b Liu, Y. (23 September 2013). "Protein Inhibitor of Activated STAT 1 (PIAS1) Is Identified as the SUMO E3 Ligase of CCAAT/Enhancer-Binding Protein (C/EBP ) during Adipogenesis". Molecular and Cellular Biology. 33 (22): 4606–4617. doi:10.1128/MCB.00723-13. PMID 24061474. {{cite journal}}: Unknown parameter |coauthors= ignored (|author= suggested) (help)
  10. ^ a b Palvimo, J.J. (1 December 2007). "PIAS proteins as regulators of small ubiquitin-related modifier (SUMO) modifications and transcription". Biochemical Society Transactions. 35 (6): 1405–1408. doi:10.1042/BST0351405. PMID 18031232.
  11. ^ a b Prigge, JR (2006 May 5). "Interaction of protein inhibitor of activated STAT (PIAS) proteins with the TATA-binding protein, TBP". The Journal of Biological Chemistry. 281 (18): 12260–9. doi:10.1074/jbc.M510835200. PMC 2030495. PMID 16522640. {{cite journal}}: Check date values in: |date= (help); Unknown parameter |coauthors= ignored (|author= suggested) (help)
  12. ^ a b Liu, B.; Liao, J.; Rao, X.; Kushner, S. A.; Chung, C. D.; Chang, D. D.; Shuai, K. (1998 Sep 1). "Inhibition of Stat1-mediated gene activation by PIAS1". Proceedings of the National Academy of Sciences of the United States of America. 95 (18): 10626–31. doi:10.1073/pnas.95.18.10626. PMC 27945. PMID 9724754. {{cite journal}}: Check date values in: |date= (help)
  13. ^ Ortmann, Robert A.; Cheng, Tammy; Visconti, Roberta; Frucht, David M.; O'Shea, John J. (2000). "Janus kinases and signal transducers and activators of transcription: Their roles in cytokine signaling, development and immunoregulation". Arthritis Research. 2 (1): 16–32. doi:10.1186/ar66. PMC 129988. PMID 11094415.{{cite journal}}: CS1 maint: unflagged free DOI (link)
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