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Items: 1 to 20 of 96

1.

Human HOIP and LUBAC deficiency underlies autoinflammation, immunodeficiency, amylopectinosis, and lymphangiectasia.

Boisson B, Laplantine E, Dobbs K, Cobat A, Tarantino N, Hazen M, Lidov HG, Hopkins G, Du L, Belkadi A, Chrabieh M, Itan Y, Picard C, Fournet JC, Eibel H, Tsitsikov E, Pai SY, Abel L, Al-Herz W, Casanova JL, Israel A, Notarangelo LD.

J Exp Med. 2015 Jun 1;212(6):939-51. doi: 10.1084/jem.20141130. Epub 2015 May 25.

2.

Immunodeficiency, autoinflammation and amylopectinosis in humans with inherited HOIL-1 and LUBAC deficiency.

Boisson B, Laplantine E, Prando C, Giliani S, Israelsson E, Xu Z, Abhyankar A, Israël L, Trevejo-Nunez G, Bogunovic D, Cepika AM, MacDuff D, Chrabieh M, Hubeau M, Bajolle F, Debré M, Mazzolari E, Vairo D, Agou F, Virgin HW, Bossuyt X, Rambaud C, Facchetti F, Bonnet D, Quartier P, Fournet JC, Pascual V, Chaussabel D, Notarangelo LD, Puel A, Israël A, Casanova JL, Picard C.

Nat Immunol. 2012 Dec;13(12):1178-86. doi: 10.1038/ni.2457. Epub 2012 Oct 28.

3.

Posttranslational Modification of HOIP Blocks Toll-Like Receptor 4-Mediated Linear-Ubiquitin-Chain Formation.

Bowman J, Rodgers MA, Shi M, Amatya R, Hostager B, Iwai K, Gao SJ, Jung JU.

MBio. 2015 Nov 17;6(6):e01777-15. doi: 10.1128/mBio.01777-15.

4.

IFN-γ or IFN-α ameliorates chronic proliferative dermatitis by inducing expression of linear ubiquitin chain assembly complex.

Tamiya H, Terao M, Takiuchi T, Nakahara M, Sasaki Y, Katayama I, Yoshikawa H, Iwai K.

J Immunol. 2014 Apr 15;192(8):3793-804. doi: 10.4049/jimmunol.1302308. Epub 2014 Mar 14.

5.

Second Case of HOIP Deficiency Expands Clinical Features and Defines Inflammatory Transcriptome Regulated by LUBAC.

Oda H, Beck DB, Kuehn HS, Sampaio Moura N, Hoffmann P, Ibarra M, Stoddard J, Tsai WL, Gutierrez-Cruz G, Gadina M, Rosenzweig SD, Kastner DL, Notarangelo LD, Aksentijevich I.

Front Immunol. 2019 Mar 18;10:479. doi: 10.3389/fimmu.2019.00479. eCollection 2019.

6.

LUBAC is essential for embryogenesis by preventing cell death and enabling haematopoiesis.

Peltzer N, Darding M, Montinaro A, Draber P, Draberova H, Kupka S, Rieser E, Fisher A, Hutchinson C, Taraborrelli L, Hartwig T, Lafont E, Haas TL, Shimizu Y, Böiers C, Sarr A, Rickard J, Alvarez-Diaz S, Ashworth MT, Beal A, Enver T, Bertin J, Kaiser W, Strasser A, Silke J, Bouillet P, Walczak H.

Nature. 2018 May;557(7703):112-117. doi: 10.1038/s41586-018-0064-8. Epub 2018 Apr 25.

7.

Shigella flexneri suppresses NF-κB activation by inhibiting linear ubiquitin chain ligation.

de Jong MF, Liu Z, Chen D, Alto NM.

Nat Microbiol. 2016 May 27;1(7):16084. doi: 10.1038/nmicrobiol.2016.84.

8.

--LUBAC deficiency perturbs TLR3 signaling to cause immunodeficiency and autoinflammation.

Zinngrebe J, Rieser E, Taraborrelli L, Peltzer N, Hartwig T, Ren H, Kovács I, Endres C, Draber P, Darding M, von Karstedt S, Lemke J, Dome B, Bergmann M, Ferguson BJ, Walczak H.

J Exp Med. 2016 Nov 14;213(12):2671-2689. Epub 2016 Oct 24.

9.

SHARPIN is a component of the NF-κB-activating linear ubiquitin chain assembly complex.

Tokunaga F, Nakagawa T, Nakahara M, Saeki Y, Taniguchi M, Sakata S, Tanaka K, Nakano H, Iwai K.

Nature. 2011 Mar 31;471(7340):633-6. doi: 10.1038/nature09815.

PMID:
21455180
10.

Linear ubiquitination-mediated NF-κB regulation and its related disorders.

Tokunaga F.

J Biochem. 2013 Oct;154(4):313-23. doi: 10.1093/jb/mvt079. Epub 2013 Aug 21. Review.

PMID:
23969028
11.

SPATA2 Links CYLD to LUBAC, Activates CYLD, and Controls LUBAC Signaling.

Elliott PR, Leske D, Hrdinka M, Bagola K, Fiil BK, McLaughlin SH, Wagstaff J, Volkmar N, Christianson JC, Kessler BM, Freund SM, Komander D, Gyrd-Hansen M.

Mol Cell. 2016 Sep 15;63(6):990-1005. doi: 10.1016/j.molcel.2016.08.001. Epub 2016 Aug 30.

12.

The linear ubiquitin assembly complex (LUBAC) is essential for NLRP3 inflammasome activation.

Rodgers MA, Bowman JW, Fujita H, Orazio N, Shi M, Liang Q, Amatya R, Kelly TJ, Iwai K, Ting J, Jung JU.

J Exp Med. 2014 Jun 30;211(7):1333-47. doi: 10.1084/jem.20132486. Epub 2014 Jun 23.

13.

An Update on Autoinflammatory Diseases: Relopathies.

Steiner A, Harapas CR, Masters SL, Davidson S.

Curr Rheumatol Rep. 2018 May 30;20(7):39. doi: 10.1007/s11926-018-0749-x. Review.

PMID:
29846841
14.

MALT1 cleaves the E3 ubiquitin ligase HOIL-1 in activated T cells, generating a dominant negative inhibitor of LUBAC-induced NF-κB signaling.

Elton L, Carpentier I, Staal J, Driege Y, Haegman M, Beyaert R.

FEBS J. 2016 Feb;283(3):403-12. doi: 10.1111/febs.13597. Epub 2015 Nov 26.

15.

Gliotoxin suppresses NF-κB activation by selectively inhibiting linear ubiquitin chain assembly complex (LUBAC).

Sakamoto H, Egashira S, Saito N, Kirisako T, Miller S, Sasaki Y, Matsumoto T, Shimonishi M, Komatsu T, Terai T, Ueno T, Hanaoka K, Kojima H, Okabe T, Wakatsuki S, Iwai K, Nagano T.

ACS Chem Biol. 2015 Mar 20;10(3):675-81. doi: 10.1021/cb500653y. Epub 2014 Dec 17.

PMID:
25494483
16.

Biophysical and biological evaluation of optimized stapled peptide inhibitors of the linear ubiquitin chain assembly complex (LUBAC).

Aguilar-Alonso F, Whiting AL, Kim YJ, Bernal F.

Bioorg Med Chem. 2018 Mar 15;26(6):1179-1188. doi: 10.1016/j.bmc.2017.11.047. Epub 2017 Dec 5.

17.
18.

Roles of linear ubiquitinylation, a crucial regulator of NF-κB and cell death, in the immune system.

Sasaki K, Iwai K.

Immunol Rev. 2015 Jul;266(1):175-89. doi: 10.1111/imr.12308. Review.

19.

Suppression of LUBAC-mediated linear ubiquitination by a specific interaction between LUBAC and the deubiquitinases CYLD and OTULIN.

Takiuchi T, Nakagawa T, Tamiya H, Fujita H, Sasaki Y, Saeki Y, Takeda H, Sawasaki T, Buchberger A, Kimura T, Iwai K.

Genes Cells. 2014 Mar;19(3):254-72. doi: 10.1111/gtc.12128. Epub 2014 Jan 26.

20.

The multifaceted role of the E3 ubiquitin ligase HOIL-1: beyond linear ubiquitination.

Elton L, Carpentier I, Verhelst K, Staal J, Beyaert R.

Immunol Rev. 2015 Jul;266(1):208-21. doi: 10.1111/imr.12307. Review.

PMID:
26085217

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