Results 1 to 10 of about 4,876 (155)

SARS-CoV-2 N protein recruits G3BP to double membrane vesicles to promote translation of viral mRNAs [PDF]

open access: yesNature Communications
Ras-GTPase-activating protein SH3-domain-binding proteins (G3BP) are critical for the formation of stress granules (SGs) through their RNA- and ribosome-binding properties. SARS-CoV-2 nucleocapsid (N) protein exhibits strong binding affinity for G3BP and
Siwen Long   +11 more
doaj   +3 more sources

Genome-Wide Identification of G3BP Family in U’s Triangle Brassica Species and Analysis of Its Expression in B. napus [PDF]

open access: yesPlants
The RasGAP SH3 domain binding protein (G3BP) is a highly conserved family of proteins in eukaryotic organisms that coordinates signal transduction and post-transcriptional gene regulation and functions in the formation of stress granules.
Alain Tseke Inkabanga   +13 more
doaj   +3 more sources

Research Progress on the Structure and Function of G3BP

open access: yesFrontiers in Immunology, 2021
Ras-GTPase-activating protein (SH3 domain)-binding protein (G3BP) is an RNA binding protein. G3BP is a key component of stress granules (SGs) and can interact with many host proteins to regulate the expression of SGs.
Haixue Zheng
exaly   +3 more sources

Pharmacological modulation of stress granules via G3BP1/2: A pathway to treat cancer, inflammatory disease, and neurodegeneration [PDF]

open access: yesFrontiers in Pharmacology
Stress granules (SGs) are membraneless ribonucleoprotein condensates formed by liquid–liquid phase separation of non-translating mRNAs under stress, acting as dynamic platforms for translational reprogramming and cytoprotection.
Jinhua Yang, Fenfei Gao
doaj   +2 more sources

Identification of a non-canonical G3BP-binding sequence in a Mayaro virus nsP3 hypervariable domain

open access: yesFrontiers in Cellular and Infection Microbiology, 2022
Ras-GTPase-activating SH3 domain-binding-proteins 1 (G3BP1) and 2 (G3BP2) are multifunctional RNA-binding proteins involved in stress granule nucleation, previously identified as essential cofactors of Old World alphaviruses.
Laurence Briant   +2 more
exaly   +3 more sources

Role of G3BP1 phosphorylation in the regulation of plant immunity in Arabidopsis thaliana [PDF]

open access: yesFrontiers in Plant Science
A central regulator of condensate formation in mammals is the Ras GTPase-activating protein SH3 domain-binding protein (G3BP) family of RNA-binding proteins.
Fatimah Abdulhakim   +4 more
doaj   +2 more sources

The RNA-Binding Protein Rasputin/G3BP Enhances the Stability and Translation of Its Target mRNAs

open access: yesCell Reports, 2020
Summary: G3BP RNA-binding proteins are important components of stress granules (SGs). Here, we analyze the role of the Drosophila G3BP Rasputin (RIN) in unstressed cells, where RIN is not SG associated. Immunoprecipitation followed by microarray analysis
Stéphane Angers   +2 more
exaly   +3 more sources

Rasputin/G3BP mediates subversion of antiviral immunity by o'nyong-nyong virus in Anopheles coluzzii. [PDF]

open access: yesPLoS Pathogens
Cellular G3BP proteins are essential for alphavirus infection in both vertebrate and mosquito hosts, but the underlying mechanism of their proviral activity is poorly understood in any host.
Solène Cottis   +6 more
doaj   +2 more sources

Gadd45β is critical for regulation of type I interferon signaling by facilitating G3BP-mediated stress granule formation

open access: yesCell Reports, 2023
Summary: Stress granules (SGs) constitute a signaling hub that plays a critical role in type I interferon responses. Here, we report that growth arrest and DNA damage-inducible beta (Gadd45β) act as a positive regulator of SG-mediated interferon ...
Haryoung Poo
exaly   +3 more sources

Non-canonical amino acid incorporation enables minimally disruptive labeling of stress granule and TDP-43 proteinopathy [PDF]

open access: yeseLife
We report a minimally disruptive labeling strategy for stress granule protein, G3BP Stress Granule Assembly Factor 1 (G3BP1), and ALS-linked protein, TAR DNA-binding protein 43 (TDP-43), using the fluorescent non-canonical amino acid Anap. By integrating
Hao Chen   +6 more
doaj   +2 more sources

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