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Items: 1 to 20 of 78


Purification and identification of endogenous polySUMO conjugates.

Bruderer R, Tatham MH, Plechanovova A, Matic I, Garg AK, Hay RT.

EMBO Rep. 2011 Feb;12(2):142-8. doi: 10.1038/embor.2010.206. Epub 2011 Jan 21.


Multivalent interactions of the SUMO-interaction motifs in RING finger protein 4 determine the specificity for chains of the SUMO.

Keusekotten K, Bade VN, Meyer-Teschendorf K, Sriramachandran AM, Fischer-Schrader K, Krause A, Horst C, Schwarz G, Hofmann K, Dohmen RJ, Praefcke GJ.

Biochem J. 2014 Jan 1;457(1):207-14. doi: 10.1042/BJ20130753.


Identification of endogenous SUMO1 accepter sites by mass spectrometry.

Hsiao HH, Meulmeester E, Urlaub H.

Methods Mol Biol. 2012;893:431-41. doi: 10.1007/978-1-61779-885-6_27.


Proteomic analyses identify a diverse array of nuclear processes affected by small ubiquitin-like modifier conjugation in Arabidopsis.

Miller MJ, Barrett-Wilt GA, Hua Z, Vierstra RD.

Proc Natl Acad Sci U S A. 2010 Sep 21;107(38):16512-7. doi: 10.1073/pnas.1004181107. Epub 2010 Sep 2.


SUMOylation pathway in Trypanosoma cruzi: functional characterization and proteomic analysis of target proteins.

Bayona JC, Nakayasu ES, Laverrière M, Aguilar C, Sobreira TJ, Choi H, Nesvizhskii AI, Almeida IC, Cazzulo JJ, Alvarez VE.

Mol Cell Proteomics. 2011 Dec;10(12):M110.007369. doi: 10.1074/mcp.M110.007369. Epub 2011 Aug 10.


System-wide changes to SUMO modifications in response to heat shock.

Golebiowski F, Matic I, Tatham MH, Cole C, Yin Y, Nakamura A, Cox J, Barton GJ, Mann M, Hay RT.

Sci Signal. 2009 May 26;2(72):ra24. doi: 10.1126/scisignal.2000282.


Role of SUMO-interacting motif in Daxx SUMO modification, subnuclear localization, and repression of sumoylated transcription factors.

Lin DY, Huang YS, Jeng JC, Kuo HY, Chang CC, Chao TT, Ho CC, Chen YC, Lin TP, Fang HI, Hung CC, Suen CS, Hwang MJ, Chang KS, Maul GG, Shih HM.

Mol Cell. 2006 Nov 3;24(3):341-54.


Structural insight into SUMO chain recognition and manipulation by the ubiquitin ligase RNF4.

Xu Y, Plechanovov√° A, Simpson P, Marchant J, Leidecker O, Kraatz S, Hay RT, Matthews SJ.

Nat Commun. 2014 Jun 27;5:4217. doi: 10.1038/ncomms5217.


Analysis of cellular SUMO and SUMO-ubiquitin hybrid conjugates.

Schnellhardt M, Uzunova K, Bade VN, Krause A, Weisshaar SR, Praefcke GJ, Dohmen RJ.

Methods Mol Biol. 2012;832:81-92. doi: 10.1007/978-1-61779-474-2_4.


A novel proteomics approach to identify SUMOylated proteins and their modification sites in human cells.

Galisson F, Mahrouche L, Courcelles M, Bonneil E, Meloche S, Chelbi-Alix MK, Thibault P.

Mol Cell Proteomics. 2011 Feb;10(2):M110.004796. doi: 10.1074/mcp.M110.004796. Epub 2010 Nov 22.


Proteomic revelation: SUMO changes partners when the heat is on.

Flick K, Kaiser P.

Sci Signal. 2009 Jul 28;2(81):pe45. doi: 10.1126/scisignal.281pe45.


Proteome-wide screens for small ubiquitin-like modifier (SUMO) substrates identify Arabidopsis proteins implicated in diverse biological processes.

Elrouby N, Coupland G.

Proc Natl Acad Sci U S A. 2010 Oct 5;107(40):17415-20. doi: 10.1073/pnas.1005452107. Epub 2010 Sep 20.


Structural basis for regulation of poly-SUMO chain by a SUMO-like domain of Nip45.

Sekiyama N, Arita K, Ikeda Y, Hashiguchi K, Ariyoshi M, Tochio H, Saitoh H, Shirakawa M.

Proteins. 2010 May 1;78(6):1491-502. doi: 10.1002/prot.22667.


Different proteomic strategies to identify genuine Small Ubiquitin-like MOdifier targets and their modification sites in Trypanosoma brucei procyclic forms.

Iribarren PA, Berazategui MA, Bayona JC, Almeida IC, Cazzulo JJ, Alvarez VE.

Cell Microbiol. 2015 Oct;17(10):1413-22. doi: 10.1111/cmi.12467. Epub 2015 Jul 24.


A SIM-ultaneous role for SUMO and ubiquitin.

Perry JJ, Tainer JA, Boddy MN.

Trends Biochem Sci. 2008 May;33(5):201-8. doi: 10.1016/j.tibs.2008.02.001. Epub 2008 Apr 9. Review.


Site-specific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif.

Matic I, Schimmel J, Hendriks IA, van Santen MA, van de Rijke F, van Dam H, Gnad F, Mann M, Vertegaal AC.

Mol Cell. 2010 Aug 27;39(4):641-52. doi: 10.1016/j.molcel.2010.07.026.


In situ SUMOylation analysis reveals a modulatory role of RanBP2 in the nuclear rim and PML bodies.

Saitoh N, Uchimura Y, Tachibana T, Sugahara S, Saitoh H, Nakao M.

Exp Cell Res. 2006 May 1;312(8):1418-30.

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