Sort   by:  
 Page size 
ProteomicsUncovering Global SUMOylation Signaling Networks in a Site-Specific Manner
SUMOylation is a reversible post-translational modification essential for genome stability. Using high-resolution mass spectrometry, we have studied global SUMOylation in mammalian cells and in a site-specific manner, identifying a total of over 4,300 SUMOylation sites in over 1,600 proteins. Moreov...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-29 | MSV000080793 | MassIVE
ProteomicsSystem-wide analysis of SUMOylation dynamics in response to replication stress reveals novel SUMO target proteins and acceptor lysines relevant for genome stability
Genotoxic agents can cause replication fork stalling in dividing cells due to DNA lesions, eventually leading to replication fork collapse when the damage is not repaired. Small Ubiquitin-like Modifiers (SUMOs) are known to counteract replication stress, nevertheless, only a small number of relevant...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-31 | MSV000080851 | MassIVE
ProteomicsSystem-Wide Identification of Wild-Type SUMO-2 Conjugation Sites
SUMOylation is a reversible post-translational modification regulating all nuclear processes. Identification of SUMOylation sites by mass spectrometry has been hampered by bulky tryptic fragments, which thus far necessitated the use of mutated SUMO. Here, we present a dataset generated through a SUM...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-28 | MSV000080714 | MassIVE
ProteomicsHA-mSLX4 wild type and SIMdependent interactors
SUMOylation is known to play important roles in the DNA damage response, however, a role for SUMOylation in interstrand crosslink repair remains enigmatic. We report on the regulation of the SLX4 nuclease scaffold protein by SUMOylation. SLX4 contains three SUMO-Interaction Motifs (SIMs). Mutating ...
ORGANISM(S): Mus musculus (Mouse) Homo sapiens (Human) 
2015-03-02 | PXD001681 | Pride
Dna repair Slx4 Fanconi anemia Sumo Ubiquitin 
OtherSystem-wide analysis of SUMOylation dynamics in response to replication stress reveals novel SUMO target proteins and acceptor lysines relevant for genome stability.
Data from ProteomeXchange, PXD ID: PXD001736. File: 20140408_QE_UP_U2OS1222_2h_04a.mzml. Published as part of . From the Abstract: {{i}} To address this, we have purified and identified SUMO-2 target proteins regulated by replication stress in human cells. The developed methodology enabled single s...
ORGANISM(S): Homo_sapiens_viruses, Human_female 
GPM32310018476 | GPMDB
Resource Reanalysis 
OtherSUMOylation and PARylation cooperate to recruit and stabilize SLX4 at DNA damage sites.
Data from ProteomeXchange, PXD ID: PXD001681. File: RGP-HA-mSLX4-coIP-Control-1b.mzml. Published as part of EMBO Rep. 2015 Feb 26 . From the Abstract: {{i}} ... We report that the SLX4 nuclease scaffold protein is regulated by SUMOylation. We have identified three SUMO interaction motifs (SIMs) in ...
ORGANISM(S): Homo_sapiens_viruses, Human_female 
GPM32310007055 | GPMDB
Resource Reanalysis 
ProteomicsSite-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation (part 2)
Small ubiquitin-like modifiers (SUMOs) are post-translational modifications (PTMs) that regulate nuclear cellular processes. Here we used an augmented K0â??SUMO proteomics strategy to identify 40,765 SUMO acceptor sites and quantify their fractional contribution for 6,747 human proteins. Structuralâ...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-04-01 | MSV000080869 | MassIVE
ProteomicsSite-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation (part 1)
Small ubiquitin-like modifiers (SUMOs) are post-translational modifications (PTMs) that regulate nuclear cellular processes. Here we used an augmented K0â??SUMO proteomics strategy to identify 40,765 SUMO acceptor sites and quantify their fractional contribution for 6,747 human proteins. Structuralâ...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-30 | MSV000080812 | MassIVE
Sort   by:  
 Page size