Sort   by:  
 Page size 
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
TranscriptomicsE2-RING expansion of the NEDD8 cascade confers specificity to cullin modification
Ubiquitin and ubiquitin-like proteins (UBLs) are directed to targets by cascades of E1, E2, and E3 enzymes. The largest ubiquitin E3 subclass consists of cullin-RING ligases (CRLs), which contain one each of several cullins (CUL1, -2, -3, -4, or -5) and RING proteins (RBX1 or -2). CRLs are activated...
ORGANISM(S): Mus musculus 
2009-03-23 | E-GEOD-14088 | biostudies-arrayexpress
ProteomicsE2/E3-independent ubiquitin-like protein conjugation by Urm1 is directly coupled to cysteine persulfidation
Posttranslational modifications by ubiquitin-like proteins (UBL) are essential for nearly all cellular processes. Ubiquitin related modifier 1 (Urm1) is a non-canonical UBL which plays a key role in tRNA anticodon thiolation as a sulfur carrier protein (SCP). While Urm1 has also been observed to con...
ORGANISM(S): Chaetomium Thermophilum (ncbitaxon:209285) Saccharomyces Cerevisiae (ncbitaxon:4932) Homo Sapiens (ncbitaxon:9606) 
2021-11-16 | MSV000088390 | MassIVE
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
ProteomicsUbiquitin profiling of drug-like small molecule-treated cells
The ubiquitin system regulates eukaryotic physiology by modifying specific substrate proteins. Substrate recognition and the assembly of ubiquitin signals are determined by ubiquitin ligases, some of which also modify non-protein biomolecules. Here we expand this substrate realm, revealing that the ...
ORGANISM(S): Homo sapiens (Human) 
2025-09-10 | PXD067088 | Pride
Drug-like small molecules Digly Ubiquitin Huwe1 
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
UnknownPosttranslational modification of cellular proteins by a ubiquitin-like protein in bacteria.
Not available
S-EPMC3366818 | biostudies-literature
UnknownTaking it step by step: mechanistic insights from structural studies of ubiquitin/ubiquitin-like protein modification pathways.
Not available
S-EPMC2174906 | biostudies-literature
ProteomicsRhes, a striatal enriched protein regulates post-translational Small-Ubiquitin like-Modifier (SUMO) Modification of nuclear proteins and alters gene expression
Rhes (Ras homolog enriched in the striatum) is a multifunctional protein that orchestrates striatal toxicity, motor behaviors and abnormal movements associated with dopaminergic signaling, Huntington disease and Parkinson disease signaling in the striatum. Rhes engineers membranous tunneling nanotub...
ORGANISM(S): Homo sapiens (Human) 
2024-06-10 | PXD023394 | Pride
Perinuclear membrane Morphology Brain Medium spiny neurons Differentiation Gene regulation Sumo e3-ligase Signaling 
Sort   by:  
 Page size