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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. De plus, nous expédions GTPase Activating Protein (SH3 Domain) Binding Protein 1 Anticorps (156) et GTPase Activating Protein (SH3 Domain) Binding Protein 1 Protéines (15) et beaucoup plus de produits pour cette protéine.
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G3BP1 interacts directly with the foot-and-mouth disease virus internal ribosome entry site and negatively regulates translation.
The data suggested that JNK (Montrer MAPK8 Kits ELISA)-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 (Montrer PRMT1 Kits ELISA) (PRMT) 1 (Montrer PRMT1 Kits ELISA) and PRMT5 (Montrer PRMT5 Kits ELISA) 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 (Montrer USP10 Kits ELISA).
Host G3BP1 captures HIV-1 RNA transcripts and thereby restricts mRNA translation, viral protein production and virus particle formation.
Our findings identified a novel function of G3BP1 in the progression of breast cancer via activation of the epithelial-to-mesenchymal transition
G3BP1 granules were assembled independently of TIA-1 (Montrer TIA1 Kits ELISA) and had a negative impact on Dengue virus replication.
The G3BP1-Caprin1-PKR (Montrer PKLR Kits ELISA) complex represents a new mode of PKR (Montrer PKLR Kits ELISA) activation and is important for antiviral activity of G3BP1 and PKR (Montrer PKLR Kits ELISA) during infection with mengovirus.
the aberrant mutant SOD1 (Montrer SOD1 Kits ELISA)-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.
Cytoplasmic granule containing HERMES (Montrer CD44 Kits ELISA), NonO (Montrer NONO Kits ELISA), PSF (Montrer IL-3 Kits ELISA), 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 (Montrer CDK7 Kits ELISA) R as the principal kinase that mediates eukaryotic initiation factor 2alpha (eIF2alpha (Montrer EIF2S1 Kits ELISA)) phosphorylation by large RasGAP (Montrer RASA1 Kits ELISA) SH3-binding protein (Montrer SH3BP5 Kits ELISA) (G3BP)-induced granules.
Wnt3a-stimulated LRP6 phosphorylation is dependent upon arginine methylation of G3BP2.
arguments against G3BP1 being a genuine RasGAP (Montrer RASA1 Kits ELISA)-binding partner
G3BP1 is a novel Ctnnb1 (Montrer CTNNB1 Kits ELISA) mRNA binding protein. Methylation of G3BP1 constitutes a molecular switch that regulates Ctnnb1 (Montrer CTNNB1 Kits ELISA) mRNA in response to Wnt3a (Montrer WNT3A Kits ELISA).
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