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UnknownQUADRatlas: the RNA G-quadruplex and RG4-binding proteins database.
Not available
S-EPMC9825518 | biostudies-literature
ProteomicsLockd promotes myoblast proliferation and skeletal muscle regeneration through binding with DHX36 to facilitate unwinding of 5’UTR rG4 and translation of Anp32e mRNA
Adult muscle stem cells, also known as satellite cells (SCs) play pivotal roles in injury induced muscle regeneration and our knowledge of long non-coding RNA (lncRNA) functions in SCs remains limited. Here we identify a lncRNA, Lockd which is induced in activated SCs upon acute muscle injury. We de...
ORGANISM(S): Mus Musculus 
2022-05-24 | PXD033658 |
TranscriptomicsRG/RGG boxes are common binding motifs in RNA-G-quadruplex-interacting proteins
G-quadruplexes (rG4s) are recognized as key structures involved in RNA biology and are linked to neurodegenerative disease and cancer. However, detailed knowledge of rG4s and their binding partners is lacking. Here, a systematic, unbiased affinity proteomics approach identified 80 potential high-con...
ORGANISM(S): Homo sapiens 
2018-04-30 | GSE106476 | GEO
OtherMassively parallel characterization of RNA G-quadruplex stability and molecular recognition
RNA G-quadruplexes (rG4s) have been implicated as important regulators of RNA metabolism and are promising targets for RNA-targeted therapeutics. rG4s typically require a canonical (G≥2N1-7)4 motif, but the sequence features that affect rG4 stability and recognition by RNA-binding proteins (RBPs) an...
ORGANISM(S): synthetic construct 
2026-08-03 | GSE296171 | GEO
UnknownAnalysis of NRAS RNA G-quadruplex binding proteins reveals DDX3X as a novel interactor of cellular G-quadruplex containing transcripts.
Not available
S-EPMC6265444 | biostudies-literature
ProteomicsBLM helicase protein negatively regulates stress granule formation through unwinding RNA G-quadruplex structures
Bloom’s syndrome (BLM) protein is a known nuclear helicase that is able to unwind DNA secondary structures such as G-quadruplexes. However, its role in the regulation of cytoplasmic processes that involve RNA G-quadruplexes (rG4s) has not been previously studied. Here, we demonstrate that BLM is rec...
ORGANISM(S): Homo sapiens (Human) 
2023-10-24 | PXD039534 | Pride
Stress granule Apex Helicase Lc-msms G-quadruplex Rg4-binding proteins Blm Quma-1 
GenomicsRG/RGG boxes are common binding motifs in RNA-G-quadruplex-interacting proteins
RG/RGG boxes are common binding motifs in RNA-G-quadruplex-interacting proteins
PRJNA417119 | ENA
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 
TranscriptomicsContributions of Folded and Disordered Domains to RNA Binding by HNRNPR
RNA binding proteins (RBPs) interact with and tightly regulate the fate of messenger RNAs but how RNA targets are recognized remains a challenging question. RBPs often contain multiple domains known to directly bind RNA, such as RNA recognition motifs (RRMs), as well as domains whose RNA binding cap...
ORGANISM(S): synthetic construct 
2026-08-31 | GSE296428 | GEO
UnknownG3BP1 binds to guanine quadruplexes in mRNAs to modulate their stabilities.
Not available
S-EPMC8565330 | biostudies-literature
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