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GenomicsG-Quadruplex structures are stable and detectable in human genomic DNA.
The G-quadruplex is an alternative DNA structural motif that is considered to be functionally important in the mammalian genome. Herein, we address the hypothesis that G-quadruplex structures can exist within double-stranded genomic DNA using a G-quadruplex-specific probe. An engineered antibody is ...
ORGANISM(S): Homo sapiens 
2013-05-08 | E-GEOD-45241 | biostudies-arrayexpress
TranscriptomicsAltered gene expression in Werner & Bloom syndromes is associated with sequences having G-quadruplex forming potential
The human Werner and Bloom syndromes (WS and BS) are caused by deficiencies in the WRN and BLM RecQ helicases, respectively. WRN, BLM and their S. cerevisiae homologue Sgs1, are particularly active in vitro in unwinding G-quadruplex DNA (G4-DNA), a family of non-canonical nucleic acid structures fo...
ORGANISM(S): Homo sapiens 
2009-12-09 | E-GEOD-19205 | biostudies-arrayexpress
ProteomicsComprehensive identification of proteins binding to RNA G-quadruplex motifs in the 5’ UTR of tumor-associated mRNAs
G-quadruplex structures in the 5’ UTR of mRNAs are widely considered to suppress translation without affecting transcription. The current study describes the comprehensive analysis of proteins binding to four different G-quadruplex motifs located in mRNAs of the cancer-related genes Bcl-2, NRAS, MMP...
ORGANISM(S): Homo sapiens (Human) 
2017-11-14 | PXD005761 | Pride
Nras Cancer Translational regulation Silac Mmp16 Rna Rbps Shotgun proteomics G-quadruplexes Bcl-2 Arpc2 Post-transcriptional regulation 
GenomicsRNA Bind-N-Seq for purified α-Synuclein and BG4 (scFV for G-quadruplex)
RNA Bind-N-Seq for purified α-Synuclein and BG4 (scFV for G-quadruplex)
PRJNA986023 | ENA
ProteomicsNon-canonical RNA-binding of the histone lysine demethylase KDM5 through interactions with G-quadruplex sequences
RNA-binding proteins are important regulators of RNA biogenesis and function, and recent work shows that chromatin- and RNA-binding proteins can have regulatory roles in transcription. Several approaches have been developed to predict RNA-binding proteins and to identify them experimentally at large...
ORGANISM(S): Homo sapiens (Human) 
2024-04-11 | PXD050767 | Pride
Histone lysine demethylase kdm5  g-quadruplex  non-canonical rna-binding 
TranscriptomicsRNA G-quadruplexes cause eIF4A-dependent oncogene translation in cancer
The translational control of oncoprotein expression is implicated in many cancers. Here we report an eIF4A/DDX2 RNA helicase-dependent mechanism of translational control that contributes to oncogenesis and underlies the anticancer effects of Silvestrol and related compounds. For example, eIF4A promo...
ORGANISM(S): Homo sapiens 
2014-07-27 | E-GEOD-56887 | biostudies-arrayexpress
GenomicsSystematic identification of G-quadruplex sensitive lethality by genome-wide genetic screening
A375 and HT1080 cells are treated with G-quadruplex ligands PDS or PhenDC3 following genome-wide shRNA knockdown. This enables the identification of genes that when silenced, specifically compromises cell growth in the presence of the ligand. First, a pilot screen was performed to determine a ligand...
ORGANISM(S): Homo sapiens 
2019-06-22 | E-MTAB-6367 | biostudies-arrayexpress
ProteomicsCharacterizations of G-quadruplex RNA-Protein Interactions in Living Cells
RNA guanine quadruplexes (rG4s) are non-canonical nucleic acid structures essential for various cellular functions and disease pathways. Characterizing rG4-interacting proteins (rG4IPs) is crucial for deciphering biological roles of rG4s. Building upon the RNA-protein interaction detection (RaPID) m...
ORGANISM(S): Homo sapiens (Human) 
2026-06-01 | PXD070623 | Pride
G-quadruplex Rna-protein interactions Proteomics Lc-ms/ms 
GenomicsRNA G-quadruplex secondary structure promotes alternative splicing via the RNA binding protein hnRNPF
RNA G-quadruplex secondary structure promotes alternative splicing via the RNA binding protein hnRNPF
PRJNA420499 | ENA
ProteomicsG4-RNA binding proteins from K562
G-quadruplex RNA pulldown followed by mass spectrometry. G4A4 oligoribonucleotide (5’-AAAAAAGGGGAAAAGGGGAAAAGGGGAAAAGGGGAAAAAA-3’) was biotinylated and folded in either K+ or Li+ containing buffers, causing folding of G-quadruplex (K+) or destabilization of the secondary structure (Li+). G4A4 pulldo...
ORGANISM(S): Homo sapiens (Human) 
2024-02-20 | PXD041154 | Pride
Rna pulldown G-quadruplex rna 
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