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Items: 1 to 20 of 74

1.

Regnase-1 and Roquin Regulate a Common Element in Inflammatory mRNAs by Spatiotemporally Distinct Mechanisms.

Mino T, Murakawa Y, Fukao A, Vandenbon A, Wessels HH, Ori D, Uehata T, Tartey S, Akira S, Suzuki Y, Vinuesa CG, Ohler U, Standley DM, Landthaler M, Fujiwara T, Takeuchi O.

Cell. 2015 May 21;161(5):1058-1073. doi: 10.1016/j.cell.2015.04.029.

2.

Regnase-1 and Roquin Nonredundantly Regulate Th1 Differentiation Causing Cardiac Inflammation and Fibrosis.

Cui X, Mino T, Yoshinaga M, Nakatsuka Y, Hia F, Yamasoba D, Tsujimura T, Tomonaga K, Suzuki Y, Uehata T, Takeuchi O.

J Immunol. 2017 Dec 15;199(12):4066-4077. doi: 10.4049/jimmunol.1701211. Epub 2017 Nov 10.

3.

Regnase-1 and Roquin regulate inflammatory mRNAs.

Mino T, Takeuchi O.

Oncotarget. 2015 Jul 20;6(20):17869-70. No abstract available.

4.

Translation-dependent unwinding of stem-loops by UPF1 licenses Regnase-1 to degrade inflammatory mRNAs.

Mino T, Iwai N, Endo M, Inoue K, Akaki K, Hia F, Uehata T, Emura T, Hidaka K, Suzuki Y, Standley DM, Okada-Hatakeyama M, Ohno S, Sugiyama H, Yamashita A, Takeuchi O.

Nucleic Acids Res. 2019 Sep 19;47(16):8838-8859. doi: 10.1093/nar/gkz628.

PMID:
31329944
5.

Endonuclease Regnase-1/Monocyte chemotactic protein-1-induced protein-1 (MCPIP1) in controlling immune responses and beyond.

Takeuchi O.

Wiley Interdiscip Rev RNA. 2018 Jan;9(1). doi: 10.1002/wrna.1449. Epub 2017 Sep 20. Review.

PMID:
28929622
6.

[Post-transcriptional regulation of inflammatory mRNA by Regnase-1 and Roquin].

Mino T, Takeuchi O.

Nihon Yakurigaku Zasshi. 2016 Jun;147(6):351-6. doi: 10.1254/fpj.147.351. Japanese. No abstract available.

PMID:
27301309
7.

Roquin promotes constitutive mRNA decay via a conserved class of stem-loop recognition motifs.

Leppek K, Schott J, Reitter S, Poetz F, Hammond MC, Stoecklin G.

Cell. 2013 May 9;153(4):869-81. doi: 10.1016/j.cell.2013.04.016.

8.

A Distinct, Sequence-Induced Conformation Is Required for Recognition of the Constitutive Decay Element RNA by Roquin.

Codutti L, Leppek K, Zálešák J, Windeisen V, Masiewicz P, Stoecklin G, Carlomagno T.

Structure. 2015 Aug 4;23(8):1437-1447. doi: 10.1016/j.str.2015.06.001. Epub 2015 Jul 9.

9.

Cleavage of roquin and regnase-1 by the paracaspase MALT1 releases their cooperatively repressed targets to promote T(H)17 differentiation.

Jeltsch KM, Hu D, Brenner S, Zöller J, Heinz GA, Nagel D, Vogel KU, Rehage N, Warth SC, Edelmann SL, Gloury R, Martin N, Lohs C, Lech M, Stehklein JE, Geerlof A, Kremmer E, Weber A, Anders HJ, Schmitz I, Schmidt-Supprian M, Fu M, Holtmann H, Krappmann D, Ruland J, Kallies A, Heikenwalder M, Heissmeyer V.

Nat Immunol. 2014 Nov;15(11):1079-89. doi: 10.1038/ni.3008. Epub 2014 Oct 5.

PMID:
25282160
10.

Roquin targets mRNAs in a 3'-UTR-specific manner by different modes of regulation.

Essig K, Kronbeck N, Guimaraes JC, Lohs C, Schlundt A, Hoffmann A, Behrens G, Brenner S, Kowalska J, Lopez-Rodriguez C, Jemielity J, Holtmann H, Reiche K, Hackermüller J, Sattler M, Zavolan M, Heissmeyer V.

Nat Commun. 2018 Sep 19;9(1):3810. doi: 10.1038/s41467-018-06184-3.

11.

Regnase-1, a rapid response ribonuclease regulating inflammation and stress responses.

Mao R, Yang R, Chen X, Harhaj EW, Wang X, Fan Y.

Cell Mol Immunol. 2017 May;14(5):412-422. doi: 10.1038/cmi.2016.70. Epub 2017 Feb 13. Review.

12.

Regnase-1 Is an Endoribonuclease Essential for the Maintenance of Immune Homeostasis.

Uehata T, Takeuchi O.

J Interferon Cytokine Res. 2017 May;37(5):220-229. doi: 10.1089/jir.2017.0001. Review.

PMID:
28475459
13.

Regulation of mRNA stability by CCCH-type zinc-finger proteins in immune cells.

Maeda K, Akira S.

Int Immunol. 2017 Apr 1;29(4):149-155. doi: 10.1093/intimm/dxx015. Review.

14.

Regnase-1 Maintains Iron Homeostasis via the Degradation of Transferrin Receptor 1 and Prolyl-Hydroxylase-Domain-Containing Protein 3 mRNAs.

Yoshinaga M, Nakatsuka Y, Vandenbon A, Ori D, Uehata T, Tsujimura T, Suzuki Y, Mino T, Takeuchi O.

Cell Rep. 2017 May 23;19(8):1614-1630. doi: 10.1016/j.celrep.2017.05.009.

15.

The IκB kinase complex regulates the stability of cytokine-encoding mRNA induced by TLR-IL-1R by controlling degradation of regnase-1.

Iwasaki H, Takeuchi O, Teraguchi S, Matsushita K, Uehata T, Kuniyoshi K, Satoh T, Saitoh T, Matsushita M, Standley DM, Akira S.

Nat Immunol. 2011 Oct 30;12(12):1167-75. doi: 10.1038/ni.2137.

PMID:
22037600
16.

A translational silencing function of MCPIP1/Regnase-1 specified by the target site context.

Behrens G, Winzen R, Rehage N, Dörrie A, Barsch M, Hoffmann A, Hackermüller J, Tiedje C, Heissmeyer V, Holtmann H.

Nucleic Acids Res. 2018 May 4;46(8):4256-4270. doi: 10.1093/nar/gky106.

17.

The ROQUIN family of proteins localizes to stress granules via the ROQ domain and binds target mRNAs.

Athanasopoulos V, Barker A, Yu D, Tan AH, Srivastava M, Contreras N, Wang J, Lam KP, Brown SH, Goodnow CC, Dixon NE, Leedman PJ, Saint R, Vinuesa CG.

FEBS J. 2010 May;277(9):2109-27. doi: 10.1111/j.1742-4658.2010.07628.x.

18.

mRNA degradation by the endoribonuclease Regnase-1/ZC3H12a/MCPIP-1.

Uehata T, Akira S.

Biochim Biophys Acta. 2013 Jun-Jul;1829(6-7):708-13. doi: 10.1016/j.bbagrm.2013.03.001. Epub 2013 Mar 13. Review.

PMID:
23500036
19.

Binding of NUFIP2 to Roquin promotes recognition and regulation of ICOS mRNA.

Rehage N, Davydova E, Conrad C, Behrens G, Maiser A, Stehklein JE, Brenner S, Klein J, Jeridi A, Hoffmann A, Lee E, Dianzani U, Willemsen R, Feederle R, Reiche K, Hackermüller J, Leonhardt H, Sharma S, Niessing D, Heissmeyer V.

Nat Commun. 2018 Jan 19;9(1):299. doi: 10.1038/s41467-017-02582-1.

20.

A CAF40-binding motif facilitates recruitment of the CCR4-NOT complex to mRNAs targeted by Drosophila Roquin.

Sgromo A, Raisch T, Bawankar P, Bhandari D, Chen Y, Kuzuoğlu-Öztürk D, Weichenrieder O, Izaurralde E.

Nat Commun. 2017 Feb 6;8:14307. doi: 10.1038/ncomms14307.

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