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ProteomicsThe dimeric SFiNX complex enables piRNA-guided co-transcriptional silencing through molecular condensate formation
Nuclear Argonaute proteins, guided by their bound small RNAs, orchestrate heterochromatin formation at transposon insertions and repetitive genomic loci. The molecular mechanisms that, besides recruiting heterochromatin effector proteins, are required for this silencing process are poorly understood...
ORGANISM(S): Mus musculus (Mouse) Drosophila melanogaster (Fruit fly) 
2021-02-12 | PXD022010 | Pride
Cut up/dlc8 Co-transcriptional gene silencing Dimerization Condensate formation Pirna pathway Sfinx 
ProteomicsSystematic investigation on the effect of O-GlcNAcylation on condensate formation under heat stress and recovery
O-GlcNAc is known to regulate the aggregation and condensate formation of several proteins, but how O-GlcNAc regulates protein solubilities globally has yet to be systematically investigated. Here, we employed a chemoproteomic workflow integrating selective enrichment and multiplex proteomics to qua...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2023-08-18 | MSV000092690 | MassIVE
GenomicsIGF2BP1 phosphorylation regulates ribonucleoprotein condensate formation by impairing low-affinity protein and RNA interactions (RIP-Seq)
IGF2BP1 phosphorylation regulates ribonucleoprotein condensate formation by impairing low-affinity protein and RNA interactions (RIP-Seq)
PRJNA1139157 | ENA
GenomicsIGF2BP1 phosphorylation regulates ribonucleoprotein condensate formation by impairing low-affinity protein and RNA interactions (RNA-Seq)
IGF2BP1 phosphorylation regulates ribonucleoprotein condensate formation by impairing low-affinity protein and RNA interactions (RNA-Seq)
PRJNA1139158 | ENA
GenomicsProteome-scale quantification of the interactions driving condensate formation of intrinsically disordered proteins
The authors develop Condensate Partitioning by mRNA display (CPmD) to quantify the weak interactions driving the partitioning into, as well as formation of biomolecular condensates by disordered proteins at the proteome scale.
PRJEB113191 | ENA
GenomicsMolecular features driving condensate formation and gene expression by the BRD4-NUT fusion oncoprotein are overlapping but distinct [RNA-seq]
Molecular features driving condensate formation and gene expression by the BRD4-NUT fusion oncoprotein are overlapping but distinct [RNA-seq]
PRJNA975833 | ENA
GenomicsMolecular features driving condensate formation and gene expression by the BRD4-NUT fusion oncoprotein are overlapping but distinct [ChIP-seq]
Molecular features driving condensate formation and gene expression by the BRD4-NUT fusion oncoprotein are overlapping but distinct [ChIP-seq]
PRJNA975834 | ENA
GenomicsNAB2::STAT6 Fusion Proteins Drive Nuclear Condensate Formation and Transcriptional Reprogramming in Solitary Fibrous Tumors
NAB2::STAT6 Fusion Proteins Drive Nuclear Condensate Formation and Transcriptional Reprogramming in Solitary Fibrous Tumors
PRJNA1463642 | ENA
TranscriptomicsIGF2BP1 phosphorylation regulates ribonucleoprotein condensate formation by impairing low-affinity protein and RNA interactions (RNA-Seq)
The insulin-like growth factor 2 mRNA binding protein (IGF2BP1) is a conserved RNA-binding protein that regulates RNA stability, localization, and translation. IGF2BP1 is part of various ribonucleoprotein (RNP) condensates. However, the mechanism that regulates its assembly into condensates remains ...
ORGANISM(S): Homo sapiens 
2024-10-10 | GSE272874 | GEO
OtherIGF2BP1 phosphorylation regulates ribonucleoprotein condensate formation by impairing low-affinity protein and RNA interactions (RIP-Seq)
The insulin-like growth factor 2 mRNA binding protein (IGF2BP1) is a conserved RNA-binding protein that regulates RNA stability, localization, and translation. IGF2BP1 is part of various ribonucleoprotein (RNP) condensates. However, the mechanism that regulates its assembly into condensates remains ...
ORGANISM(S): Homo sapiens 
2024-10-10 | GSE272873 | GEO
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