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ProteomicsMapping the mammalian ribosome quality control complex interactome using proximity labeling approaches
Proximity-based (APEX and BioID) and standard affinity capture proteomics of the mammalian ribosome associated quality control complex
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2018-01-31 | MSV000082006 | MassIVE
TranscriptomicsA comprehensive Xist interactome reveals cohesin repulsion and an RNA-directed chromosome conformation
The inactive X chromosome (Xi) serves as a model to understand gene silencing on a global scale. Here, we perform identification of direct RNA interacting proteins? (iDRiP) to isolate a comprehensive protein interactome for Xist, an RNA required for Xi silencing. We discover multiple classes of inte...
ORGANISM(S): Mus musculus 
2015-06-19 | E-GEOD-67516 | biostudies-arrayexpress
ProteomicsUnresolved stalled ribosome complexes restrict cycle progression after genotoxic stress
Translation of damaged mRNA can lead to ribosome stalling, thereby producing incomplete proteins toxic to the cell. The mechanism of ribosome-associated quality control (RQC) disassembles stalled ribosomes through the actions of the ASC-1 complex (ASCC). Here, we show that some reagents that chemica...
ORGANISM(S): Homo sapiens (Human) 
2022-02-07 | PXD023978 | Pride
Rna damage Rna interactome capture Ascc3 Asc-1 complex Ribosome-associated quality control 
ProteomicsUnresolved stalled ribosome complexes restrict cycle progression after genotoxic stress
Translation of damaged mRNA can lead to ribosome stalling, thereby producing incomplete proteins toxic to the cell. The mechanism of ribosome-associated quality control (RQC) disassembles stalled ribosomes through the actions of the ASC-1 complex (ASCC). Here, we show that some reagents that chemica...
ORGANISM(S): Homo sapiens (Human) 
2022-02-07 | PXD023976 | Pride
Rna damage Rna interactome capture Ascc3 Asc-1 complex Ribosome-associated quality control 
ProteomicsUnresolved stalled ribosome complexes restrict cycle progression after genotoxic stress
Translation of damaged mRNA can lead to ribosome stalling, thereby producing incomplete proteins toxic to the cell. The mechanism of ribosome-associated quality control (RQC) disassembles stalled ribosomes through the actions of the ASC-1 complex (ASCC). Here, we show that some reagents that chemica...
ORGANISM(S): Homo sapiens (Human) 
2022-02-07 | PXD023878 | Pride
Rna damage Rna interactome capture Ascc3 Asc-1 complex Ribosome-associated quality control 
ProteomicsUnresolved stalled ribosome complexes restrict cycle progression after genotoxic stress
Translation of damaged mRNA can lead to ribosome stalling, thereby producing incomplete proteins toxic to the cell. The mechanism of ribosome-associated quality control (RQC) disassembles stalled ribosomes through the actions of the ASC-1 complex (ASCC). Here, we show that some reagents that chemica...
ORGANISM(S): Homo sapiens (Human) 
2022-02-07 | PXD023861 | Pride
Rna damage Rna interactome capture Ascc3 Asc-1 complex Ribosome-associated quality control 
GenomicsX-chromosome dynamics revealed by the RNA interactome and chromosomal binding of CTCF
CTCF is a master regulator that plays a role in genome architecture and gene expression. A key aspect of CTCF’s mechanism involves bringing together distant genetic elements for intra- and inter-chromosomal interactions. Evidence from epigenetic processes, such as X-chromosome inactivation (XCI), su...
ORGANISM(S): Mus musculus 
2015-01-09 | E-GEOD-58242 | biostudies-arrayexpress
UnknownRNA-Protein Interactome at the Hepatitis E Virus Internal Ribosome Entry Site.
Not available
S-EPMC10434006 | biostudies-literature
UnknownDefining the interactome of the human mitochondrial ribosome identifies SMIM4 and TMEM223 as respiratory chain assembly factors.
Not available
S-EPMC8719881 | biostudies-literature
ProteomicsAnalysis of stalled ribosome-nascent chain complexes by quantitative proteomics
The cellular environment is critical for efficient protein maturation, but how proteins fold during biogenesis remains poorly understood. To understand how the cellular environment modulates folding, we studied the cotranslational chaperone-assisted folding of Escherichia coli dihydrofolate reductas...
ORGANISM(S): Escherichia coli 
2025-05-06 | PXD036784 | Pride
Protein biosynthesis Ribosome-nascent chain complexes Interactome Protein folding Lc-ms/ms 
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