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• 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. WikiDan61 ^ChatMe! _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) A major contributor to this article appears to have a close connection with its subject. It may require cleanup to comply with Wikipedia's content policies, particularly neutral point of view. Please discuss further on the talk page. (January 2024) ( Learn how and when to remove this message) This article relies excessively on references to primary sources. Please improve this article by adding secondary or tertiary sources. Find sources:  "Regnase-1" –  news · newspapers · books · scholar · JSTOR (January 2024) ( Learn how and when to remove this message) This article has no links to other Wikipedia articles. Please help improve this article by adding links that are relevant to the context within the existing text. (January 2024) ( Learn how and when to remove this message)

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].

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].