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GenomicsChromatin modification by SUMO-1 stimulates the promoters of translation machinery genes
We determined the occupancy of SUMO-1 on chromatin in HeLa cells by use of chromatin affinity purification coupled with next generation sequencing 18 samples examined in syncrhonized HeLa cells: Cells in G1, early S (S0)/mid (S3)/ late S phase (S6), and mitosis (M), triplicates for each sample. 1 Ch...
ORGANISM(S): Homo sapiens 
2012-10-02 | E-GEOD-41264 | biostudies-arrayexpress
ProteomicsProteome-wide analysis of SUMO2 targets in response to pathological DNA replication stress in human cells
SUMOylation is a form of post-translational modification involving covalent attachment of SUMO (Small Ubiquitin-like Modifier) polypeptides to specific lysine residues in the target protein. In human cells, there are four SUMO proteins, SUMO1–4, with SUMO2 and SUMO3 forming a closely related subfami...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-28 | MSV000080699 | MassIVE
ProteomicsProteome-wide identification of SUMO2 modification sites
Posttranslational modification with small ubiquitin-like modifiers (SUMOs) alters the function of proteins involved in diverse cellular processes. SUMOs are conjugated to lysine residues in target proteins by SUMO-specific enzymes. Although proteomic studies have identified hundreds of sumoylated su...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-29 | MSV000080741 | 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
ProteomicsIDENTIFICATION OF SUMO-2/3 MODIFIED PROTEINS ASSOCIATED WITH MITOTIC CHROMOSOMES
Sumoylation is essential for progression through mitosis, but the specific protein targets and functions remain poorly understood. In this study, we used chromosome spreads to more precisely define the localization of SUMO-2/3 to the inner-centromere and protein scaffold of mitotic chromosomes. We a...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2014-10-07 | MSV000078890 | MassIVE
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
UnknownA global S. cerevisiae small ubiquitin-related modifier (SUMO) system interactome.
Not available
S-EPMC4039371 | biostudies-literature
TranscriptomicsNOTCH1 activation in breast cancer confers sensitivity to inhibition of SUMOylation
Breast cancer is genetically heterogeneous, and recent studies have underlined a prominent contribution of epigenetics to the development of this disease. To uncover new synthetic lethalities with known breast cancer oncogenes, we screened an epigenome-focused short hairpin RNA library on a panel...
ORGANISM(S): Homo sapiens 
2014-11-21 | E-GEOD-61727 | biostudies-arrayexpress
ProteomicsIs transthyretin a regulator of Ubc9 SUMOylation?
Ageing and mutations of transthyretin (TTR), the thyroid hormones and retinol transporting protein lead to amyloidosis by destabilizing the structure of TTR. Because protein structure is regulated through posttranslational modifications, we investigated the Small Ubiquitin-like Modifier (SUMO)ylatio...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-29 | MSV000080754 | MassIVE
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