Sort   by:  
 Page size 
ProteomicsAP-MS of C18ORF25 with AMPK- and S67 phosphorylation-depedent interactions
C18ORF25 is a homolog of Arkadia (RNF111), an E3 ubiquitin ligase with SUMO-interaction motifs (SIMs) (PMID: 31417085). However, C18ORF25 lacks the entire C-terminal RING domain of RNF111 which is required for ubiquitin binding suggesting it lacks ubiquitination activity and may therefore act as an ...
ORGANISM(S): Mus musculus (Mouse) 
2024-01-03 | PXD045629 | Pride
C18orf25 Ampk phosphorylation dependent protein interactions Exercise 
ProteomicsProteomic and phosphoproteomic of C18ORF25 KO skeletal muscle following electrical contraction
We recently identified C18ORF25 as a new exercise-regulated phophoprotein. To investigate potential in vivo functions of C18ORF25, we used CRISPR/Cas9 to generate a whole-body knock-out (KO) mouse model on a C57BL/6J background. Proteomic analysis was performed to identify potental changes in the pr...
ORGANISM(S): Mus musculus (Mouse) 
2022-07-18 | PXD031101 | Pride
Proteomics Electrical contraction C18orf25 Skeletal muscles Phosphoproteomics 
ProteomicsProteomic analysis of single muscle fibres from WT and C18ORF25 KO mice
C18ORF25 is a homolog of Arkadia (RNF111), an E3 ubiquitin ligase with SUMO-interaction motifs (SIMs) (PMID: 31417085). However, C18ORF25 lacks the entire C-terminal RING domain of RNF111 which is required for ubiquitin binding suggesting it lacks ubiquitination activity and may therefore act as an ...
ORGANISM(S): Mus musculus (Mouse) 
2024-01-03 | PXD045631 | Pride
Single muscle fibre proteomics C18orf25 
UnknownThe ARK2N (C18ORF25) Genetic Variant Is Associated with Muscle Fiber Size and Strength Athlete Status.
Not available
S-EPMC11676174 | biostudies-literature
UnknownGlobal Reprogramming of Host SUMOylation during Influenza Virus Infection.
Not available
S-EPMC4660286 | biostudies-literature
UnknownIdentification of a novel protein interaction motif in the regulatory subunit of casein kinase 2.
Not available
S-EPMC3911286 | biostudies-literature
UnknownA primary nasopharyngeal three-dimensional air-liquid interface cell culture model of the pseudostratified epithelium reveals differential donor- and cell type-specific susceptibility to Epstein-Barr virus infection.
Not available
S-EPMC8112674 | biostudies-literature
ProteomicsQuantitative analysis of SUMO1 and SUMO2 proteomes in human lung A549 cells during influenza A virus infection or heat-shock
Dynamic nuclear SUMO modifications play essential roles in orchestrating cellular responses to proteotoxic stress, DNA damageand DNA virus infections. Here, we describe the host SUMOylation response to the nuclear-replicating RNA pathogen, influenz A virus. Using quantitative proteomics to compare S...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-31 | MSV000080853 | MassIVE
ProteomicsPhosphoproteomic analysis of three exercise modalities in human skeletal muscle
To characterize phosphorylation-based signaling events across different exercise modalities we subjected eight healthy young men (age, 26.3±1.3 years; BMI, 23.5±0.7 kg/m2; maximal oxygen uptake (VO2 max), 42.6±1.5 ml/kg/min) that did not perform regular physical activity apart from local bicycling t...
ORGANISM(S): Homo sapiens (Human) 
2022-07-18 | PXD031049 | Pride
Skeletal muscle Phosphoproteomics Exericse 
Sort   by:  
 Page size