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G3BP1 encodes one of the DNA-unwinding enzymes which prefers partially unwound 3'-tailed substrates and can also unwind partial RNA/DNA and RNA/RNA duplexes in an ATP-dependent fashion. Additionally we are shipping GTPase Activating Protein (SH3 Domain) Binding Protein 1 Antibodies (150) and GTPase Activating Protein (SH3 Domain) Binding Protein 1 Proteins (13) and many more products for this protein.
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Activated glucocorticoid receptor (show NR3C1 ELISA Kits) induced phosphorylation of v-AKT (show AKT1 ELISA Kits) Murine Thymoma Viral Oncogene (show RAB1A ELISA Kits) Homologue (AKT (show AKT1 ELISA Kits)) kinase, which in turn phosphorylated and promoted nuclear translocation of G3BP1. The nuclear G3BP1 bound to the G3BP1 consensus sequence located on primary miR (show MLXIP ELISA Kits)-15b~16-2 and miR (show MLXIP ELISA Kits)-23a~27a~24-2 to inhibit their maturation.
Results show the crystal structure of the NTF2-like domain of G3BP-1 in complex with nsP3 protein revealing a poly-complex of G3BP-1 dimers interconnected through the FGDF motifs in nsP3. Although in vitro and in vivo binding studies revealed a hierarchical interaction of the two FGDF motifs with G3BP-1, viral growth curves clearly demonstrated that two intact FGDF motifs are required for efficient viral replication.
Based on insights from the structures and existing biochemical data, the existence of an evolutionarily conserved ribonucleoprotein (show RBP31 ELISA Kits) (RNP (show RNPC3 ELISA Kits)) complex consisting of Caprin-1, FMRP (show FMR1 ELISA Kits) and G3BP1 is proposed.
G3BP1 interacts directly with the foot-and-mouth disease virus internal ribosome entry site and negatively regulates translation.
The data suggested that JNK (show MAPK8 ELISA Kits)-enhanced Tudor-SN phosphorylation promotes the interaction between Tudor-SN and G3BP and facilitates the efficient recruitment of Tudor-SN into stress granules under conditions of sodium arsenite-induced oxidative stress.
These data support a role for casein kinase 2 in regulation of protein synthesis by downregulating stress granule formation through G3BP1.
G3BP1 is differentially methylated on specific arginine residues by protein arginine methyltransferase (PRMT) 1 and PRMT5 in its RGG domain.
Our data define G3BP1 as a novel independent prognostic factor that is correlated with gastric cancer progression.
G3BP mediates the condensation of stress granules by shifting between two different states that are controlled by the phosphorylation of S149 and by binding to Caprin1 or USP10.
Host G3BP1 captures HIV-1 RNA transcripts and thereby restricts mRNA translation, viral protein production and virus particle formation.
the aberrant mutant SOD1 (show SOD1 ELISA Kits)-G3BP1 interaction affects stress granule dynamics
G3BP is involved in a new functional mechanism to regulate non-coding RNAs including intron-retaining transcripts, and thus have broad implications for neuronal gene regulation, where intron retention is widespread
G3bp1 posttranscriptionally regulates miRNA-1 processing in the heart.
Our findings identified a novel function of G3BP1 in the progression of breast cancer via activation of the epithelial-to-mesenchymal transition
Cytoplasmic granule containing HERMES (show CD44 ELISA Kits), NonO (show NONO ELISA Kits), PSF (show IL-3 ELISA Kits), and G3BP1 is a neuronal RNA-protein granule that is transported in neurites during retinal differentiation.
These results show, for the first time, a requirement for G3BP1 in the control of neuronal plasticity and calcium homeostasis
Data show that protein kinase (show CDK7 ELISA Kits) R as the principal kinase that mediates eukaryotic initiation factor 2alpha (eIF2alpha (show EIF2S1 ELISA Kits)) phosphorylation by large RasGAP (show RASA1 ELISA Kits) SH3-binding protein (show SH3BP5 ELISA Kits) (G3BP)-induced granules.
Wnt3a-stimulated LRP6 phosphorylation is dependent upon arginine methylation of G3BP2.
arguments against G3BP1 being a genuine RasGAP (show RASA1 ELISA Kits)-binding partner
G3BP1 is a novel Ctnnb1 (show CTNNB1 ELISA Kits) mRNA binding protein. Methylation of G3BP1 constitutes a molecular switch that regulates Ctnnb1 (show CTNNB1 ELISA Kits) mRNA in response to Wnt3a (show WNT3A ELISA Kits).
It has been demonstrated a depletion of G3BP1 and TIA-1/TIAR in senescent cells and it was shown that the loss of G3BP1 contributed to impaired stress granules formation.
This gene encodes one of the DNA-unwinding enzymes which prefers partially unwound 3'-tailed substrates and can also unwind partial RNA/DNA and RNA/RNA duplexes in an ATP-dependent fashion. This enzyme is a member of the heterogeneous nuclear RNA-binding proteins and is also an element of the Ras signal transduction pathway. It binds specifically to the Ras-GTPase-activating protein by associating with its SH3 domain. Several alternatively spliced transcript variants of this gene have been described, but the full-length nature of some of these variants has not been determined.
ras GTPase-activating protein-binding protein 1
, Ras-GTPase-activating protein SH3-domain-binding protein
, GTPase activating protein (SH3 domain) binding protein 1
, ATP-dependent DNA helicase VIII
, GAP SH3 domain-binding protein 1
, GAP binding protein
, RasGAP-associated endoribonuclease G3BP
, ATP-dependent DNA/RNA helicase G3BP
, Ras-GTPase-activating protein SH3-domain binding protein 1
, GAP SH3 binding protein
, GAP SH3 domain-binding protein 2
, Ras-GTPase-activating protein (GAP120) SH3-domain binding protein 2
, Ras-GTPase-activating protein (GAP<120>) SH3-domain binding protein 2
, ras GTPase-activating protein-binding protein 2