Draft:Regnase-1
| Submission declined on 29 January 2024 by WikiDan61 (talk). This submission is not adequately supported by reliable sources. Reliable sources are required so that information can be verified. If you need help with referencing, please see Referencing for beginners and Citing sources. This submission provides insufficient context for those unfamiliar with the subject matter. Please see the guide to writing better articles for information on how to better format your submission.
Where to get help
How to improve a draft
You can also browse Wikipedia:Featured articles and Wikipedia:Good articles to find examples of Wikipedia's best writing on topics similar to your proposed article. Improving your odds of a speedy review To improve your odds of a faster review, tag your draft with relevant WikiProject tags using the button below. This will let reviewers know a new draft has been submitted in their area of interest. For instance, if you wrote about a female astronomer, you would want to add the Biography, Astronomy, and Women scientists tags. Editor resources
|  |
Comment: This article is too short to give the reader an understanding of the topic. To start, it does not state what regnase-1 is, simply how it was found. Also, the cited sources appear to be primary research, not yet validated by other studies, so, per WP:MEDRS, these are not acceptable sources. WikiDan61ChatMe!ReadMe!! 19:46, 29 January 2024 (UTC)
 | This article has multiple issues. Please help improve it or discuss these issues on the talk page. (Learn how and when to remove these template messages)
|
Regnase-1 (MCPIP-1, ZC3H12A) is a protien that was first discovered in human peripheral blood monocytes treated the chemotactic protein MCP-1[1]. The protein contains an N-terminal domain, a PilT N-terminus like (PIN) domain, a zinc finger domain, a ubiquitin domain and a C-terminal domain. Two emerging functions of this protein include RNase-cleaving activity (PIN domain) and the control of ubiquitination. Regnase-1 also has implications in cell differentiation, apoptosis, and regulating inflammation[2].
Regulation of inflammation[edit]
NFκB is well known to induce proinflammatory cytokines. Pattern recognition receptors (PRRs) induce NFκB activation via mechanisms that utilize ubiquitylation of RIP1 and TRAF6. Recent studies have shown that Regnase-1 disrupts this ubiquitylation thereby blocking activation of NFκB and its downstream cytokines[3].
Regulation of apoptosis[edit]
References[edit]
- ^ Zhou, L; Azfer, A; Niu, J; Graham, S; Choudhury, M; Adamski, F; Younce, C; Binkley, P; Kolattukudy, PE (2006). "Monocyte chemoattractant protein-1 induces a novel transcription factor that causes cardiac myocyte apoptosis and ventricular dysfunction". Circ Res. 98 (9): 1177–85. doi:10.1161/01.RES.0000220106.64661.71. PMC 1523425. PMID 16574901.
- ^ Jin, Z; Zheng, E; Sareli, C; Kolattukudy, PE; Niu, J (2021). "Monocyte Chemotactic Protein-Induced Protein 1 (MCPIP-1): A Key Player of Host Defense and Immune Regulation". Front Immunol. 12: 727–861. doi:10.3389/fimmu.2021.727861. PMC 8519509. PMID 34659213.
- ^ Liang, J; Saad, Y; Lei, T; Wang, J; Qi, D; Yang, Q; Kolattukudy, PE; Fu, M (2010). "MCP-induced protein 1 deubiquitinates TRAF proteins and negatively regulates JNK and NF-kappaB signaling". J Exp Med. 207 (13): 2959–73. doi:10.1084/jem.20092641. PMC 3005225. PMID 21115689.