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ProteomicsRNA pull-down-Confocal Nanoscanning (RP-CONA) detects quercetin as pri-miR-7/HuR interaction inhibitor that decreases a-Synuclein levels
RNA-protein interactions are central to all gene expression processes and contribute to a variety of human diseases. Therapeutic approaches targeting RNA-protein interactions have shown promising effects on some diseases that are previously regarded as ‘incurable’. Here we developed a fluorescent on...
ORGANISM(S): Homo sapiens (Human) 
2022-02-17 | PXD025617 | Pride
Rp-cona Α-synuclein Hur Parkinson’s disease Mir-7 
ProteomicsRNA-binding activity of TRIM25 is mediated by its PRY/SPRY domain and is required for ubiquitination
TRIM25 is a novel RNA-binding protein and a member of the Tripartite Motif (TRIM) family of E3 ubiquitin ligases, which plays a pivotal role in the innate immune response. Almost nothing is known about its RNA-related roles in cell biology. Furthermore, its RNA-binding domain has not been characteri...
ORGANISM(S): Homo sapiens (Human) 
2017-10-19 | PXD007960 | Pride
Human Hela Silac Ubiquitination Rna 
ProteomicsEffects of genetic ablation and pharmacological inhibition of HuR on gene expression, iron metabolism and hormone levels.
Background:HuR/ELAV1, a ubiquitous RNA-binding protein, belongs to the RNA-binding protein family and is crucial for stabilizing and regulating the translation of various mRNA targets, influencing gene expression. Elevated HuR levels are associated with multiple disorders, including cancer and neuro...
ORGANISM(S): Homo sapiens (Human) 
2024-12-20 | PXD050698 | Pride
Iron metabolism Dia. Elavl1 Shotgun proteomics Hur Eltrombopag 
TranscriptomicsDGCR8 HITS-CLIP reveals novel functions for the Microprocessor (CLIP-seq)
The Drosha-DGCR8 complex (Microprocessor) is required for microRNA (miRNA) biogenesis. DGCR8 contains two double-stranded RNA binding motifs that recognize the RNA substrate, whereas Drosha functions as the endonuclease. We have used high-throughput sequencing of RNAs isolated by crosslinking immuno...
ORGANISM(S): Homo sapiens 
2012-07-15 | E-GEOD-39086 | biostudies-arrayexpress
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