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The nucleoporin RanBP2 has SUMO1 E3 ligase activity.
Pichler A, Gast A, Seeler JS, Dejean A, Melchior F. Pichler A, et al. Cell. 2002 Jan 11;108(1):109-20. doi: 10.1016/s0092-8674(01)00633-x. Cell. 2002. PMID: 11792325
A family of E3-like factors, PIAS proteins, was discovered recently. Here we show that the nucleoporin RanBP2/Nup358 also has SUMO1 E3-like activity. ...The E3-like activity is contained within a 33 kDa domain of RanBP2 that lacks RING finger motifs and does not res
A family of E3-like factors, PIAS proteins, was discovered recently. Here we show that the nucleoporin RanBP2/Nup358 also has SUMO1 E
The Tumor Suppressor Hace1 Is a Critical Regulator of TNFR1-Mediated Cell Fate.
Tortola L, Nitsch R, Bertrand MJM, Kogler M, Redouane Y, Kozieradzki I, Uribesalgo I, Fennell LM, Daugaard M, Klug H, Wirnsberger G, Wimmer R, Perlot T, Sarao R, Rao S, Hanada T, Takahashi N, Kernbauer E, Demiröz D, Lang M, Superti-Furga G, Decker T, Pichler A, Ikeda F, Kroemer G, Vandenabeele P, Sorensen PH, Penninger JM. Tortola L, et al. Cell Rep. 2016 May 17;15(7):1481-1492. doi: 10.1016/j.celrep.2016.04.032. Epub 2016 May 5. Cell Rep. 2016. PMID: 27160902 Free PMC article.
The HECT domain E3 ligase HACE1 has been identified as a tumor suppressor in multiple cancers. Here, we report that HACE1 is a central gatekeeper of TNFR1-induced cell fate. ...Thus, HACE1 controls TNF-elicited cell fate decisions and exerts tumor suppressor and ant …
The HECT domain E3 ligase HACE1 has been identified as a tumor suppressor in multiple cancers. Here, we report that HACE1 is a
The SUMO2/3 specific E3 ligase ZNF451-1 regulates PML stability.
Koidl S, Eisenhardt N, Fatouros C, Droescher M, Chaugule VK, Pichler A. Koidl S, et al. Int J Biochem Cell Biol. 2016 Oct;79:478-487. doi: 10.1016/j.biocel.2016.06.011. Epub 2016 Jun 22. Int J Biochem Cell Biol. 2016. PMID: 27343429
Our data suggest a regulatory role of ZNF451-1 in fine-tuning physiological PML levels in a RNF4 cooperative manner in the mouse neuroblastoma N2a cell-line....
Our data suggest a regulatory role of ZNF451-1 in fine-tuning physiological PML levels in a RNF4 cooperative manner in the mou …
Ubc9 sumoylation regulates SUMO target discrimination.
Knipscheer P, Flotho A, Klug H, Olsen JV, van Dijk WJ, Fish A, Johnson ES, Mann M, Sixma TK, Pichler A. Knipscheer P, et al. Mol Cell. 2008 Aug 8;31(3):371-82. doi: 10.1016/j.molcel.2008.05.022. Mol Cell. 2008. PMID: 18691969
Considering the large number of known targets, the number of enzymes involved in modification seems surprisingly low: a single E1, a single E2, and a few distinct E3 ligases. ...Enhancement depends on a SUMO-interacting motif (SIM) in Sp100 that create …
Considering the large number of known targets, the number of enzymes involved in modification seems surprisingly low: a single E1, …
The SUMO E3 ligase RanBP2 promotes modification of the HDAC4 deacetylase.
Kirsh O, Seeler JS, Pichler A, Gast A, Müller S, Miska E, Mathieu M, Harel-Bellan A, Kouzarides T, Melchior F, Dejean A. Kirsh O, et al. EMBO J. 2002 Jun 3;21(11):2682-91. doi: 10.1093/emboj/21.11.2682. EMBO J. 2002. PMID: 12032081 Free PMC article.
A sumoylation-deficient point mutant (HDAC4-K559R) shows a slightly impaired ability to repress transcription as well as reduced histone deacetylase activity. ...Moreover, the modification depends on the presence of an intact nuclear localization signal and is catal
A sumoylation-deficient point mutant (HDAC4-K559R) shows a slightly impaired ability to repress transcription as well as reduc
The RanBP2 SUMO E3 ligase is neither HECT- nor RING-type.
Pichler A, Knipscheer P, Saitoh H, Sixma TK, Melchior F. Pichler A, et al. Nat Struct Mol Biol. 2004 Oct;11(10):984-91. doi: 10.1038/nsmb834. Epub 2004 Sep 19. Nat Struct Mol Biol. 2004. PMID: 15378033
Here we show that RanBP2's 30-kDa catalytic fragment is a largely unstructured protein. Despite two distinct but partially overlapping 79-residue catalytic domains, one of which is sufficient for maximal activity, RanBP2 binds to Ubc9 in a 1:1 stoichiometry. ...
Here we show that RanBP2's 30-kDa catalytic fragment is a largely unstructured protein. Despite two distinct but partially overlappin …
How DNA vicinity controls SUMO E3 ligase activity.
Pichler A. Pichler A. EMBO J. 2018 Jun 15;37(12):e99705. doi: 10.15252/embj.201899705. Epub 2018 May 24. EMBO J. 2018. PMID: 29794112 Free PMC article.
Ubc9 sumoylation controls SUMO chain formation and meiotic synapsis in Saccharomyces cerevisiae.
Klug H, Xaver M, Chaugule VK, Koidl S, Mittler G, Klein F, Pichler A. Klug H, et al. Mol Cell. 2013 Jun 6;50(5):625-36. doi: 10.1016/j.molcel.2013.03.027. Epub 2013 May 2. Mol Cell. 2013. PMID: 23644018
Although less than 1% of Ubc9 is sumoylated at Lys153 at steady state, a sumoylation-deficient mutant showed significantly reduced meiotic SUMO conjugates and abrogates synaptonemal complex formation. ...Thus, sumoylation of Ubc9 converts an active enzyme into a cof …
Although less than 1% of Ubc9 is sumoylated at Lys153 at steady state, a sumoylation-deficient mutant showed significantly reduced me …
A Fluorescent In Vitro Assay to Investigate Paralog-Specific SUMO Conjugation.
Eisenhardt N, Chaugule VK, Pichler A. Eisenhardt N, et al. Methods Mol Biol. 2016;1475:67-78. doi: 10.1007/978-1-4939-6358-4_5. Methods Mol Biol. 2016. PMID: 27631798
Protein modification with the small ubiquitin-related modifier SUMO is a potent regulatory mechanism implicated in a variety of biological pathways. ...These assays provide a fast readout for in vitro SUMO chain formation activity of E3 ligases in a pa …
Protein modification with the small ubiquitin-related modifier SUMO is a potent regulatory mechanism implicated in a variety o …
Structural basis for catalytic activation by the human ZNF451 SUMO E3 ligase.
Cappadocia L, Pichler A, Lima CD. Cappadocia L, et al. Nat Struct Mol Biol. 2015 Dec;22(12):968-75. doi: 10.1038/nsmb.3116. Epub 2015 Nov 2. Nat Struct Mol Biol. 2015. PMID: 26524494 Free PMC article.
The ZNF451 catalytic module contains tandem SUMO-interaction motifs (SIMs) bridged by a Pro-Leu-Arg-Pro (PLRP) motif. The first SIM and PLRP motif engage thioester-charged E2~SUMO while the next SIM binds a second molecule of SUMO bound to the back side of E2. ...Ou …
The ZNF451 catalytic module contains tandem SUMO-interaction motifs (SIMs) bridged by a Pro-Leu-Arg-Pro (PLRP) motif. The first SIM a …
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