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Interacting proteins of the NRAS RNA G-quadruplex

ABSTRACT: Biotinylated RNA oligos were used as baits for affinity enrichments from cytoplasmic cell extracts.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Permanent Cell Line Cell, Cell Culture

DISEASE(S): Cervix Carcinoma

SUBMITTER: Barbara Herdy

LAB HEAD: Shankar Balasubramanian

PROVIDER: PXD010860 | Pride | 2019-11-12

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	PR585_BAH_12052015_BA.raw	Raw
	PR585_BAH_12052015_BB.raw	Raw
	PR585_BAH_12052015_G4A.raw	Raw
	PR585_BAH_12052015_G4B.raw	Raw
	PR585_BAH_12052015_SLA.raw	Raw

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1 - 5 of 16

Publications

Analysis of NRAS RNA G-quadruplex binding proteins reveals DDX3X as a novel interactor of cellular G-quadruplex containing transcripts.

Herdy Barbara B Mayer Clemens C Varshney Dhaval D Marsico Giovanni G Murat Pierre P Taylor Chris C D'Santos Clive C Tannahill David D Balasubramanian Shankar S

Nucleic acids research 20181101 21

RNA G-quadruplexes (rG4s) are secondary structures in mRNAs known to influence RNA post-transcriptional mechanisms thereby impacting neurodegenerative disease and cancer. A detailed knowledge of rG4-protein interactions is vital to understand rG4 function. Herein, we describe a systematic affinity proteomics approach that identified 80 high-confidence interactors that assemble on the rG4 located in the 5'-untranslated region (UTR) of the NRAS oncogene. Novel rG4 interactors included DDX3X, DDX5, ...[more]

PMID: 30256975

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An anionic phthalocyanine decreases NRAS expression by breaking down its RNA G-quadruplex.

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Analysis of NRAS RNA G-quadruplex binding proteins reveals DDX3X as a novel interactor of cellular G-quadruplex containing transcripts.

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