Results 171 to 180 of about 5,954 (200)
Hydrogel Elastic Energy: A Stressor Triggering an Adaptive Stress-Mediated Cell Response. [PDF]
Lipari S +9 more
europepmc +1 more source
Two Birds With One Stone: RNA Virus Strategies to Manipulate G3BP1 and Other Stress Granule Components. [PDF]
Firdaus MER +3 more
europepmc +1 more source
Mechanobiological regulation of T cells <i>via</i> transient viscoelastic microfluidic confinement.
Asghari M +7 more
europepmc +1 more source
Arabidopsis thaliana G3BP Ortholog Rescues Mammalian Stress Granule Phenotype across Kingdoms
Stress granules (SGs) are dynamic RNA–protein complexes localized in the cytoplasm that rapidly form under stress conditions and disperse when normal conditions are restored. The formation of SGs depends on the Ras-GAP SH3 domain-binding protein (G3BP).
Benjamin Götte +2 more
exaly +4 more sources
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Diverse CMT2 neuropathies are linked to aberrant G3BP interactions in stress granules
Cell, 2023Complex diseases often involve the interplay between genetic and environmental factors. Charcot-Marie-Tooth type 2 neuropathies (CMT2) are a group of genetically heterogeneous disorders, in which similar peripheral neuropathology is inexplicably caused by various mutated genes. Their possible molecular links remain elusive.
Peiguo Yang, Chengyong Shen, Jinsong Li
exaly +3 more sources
Role(s) of G3BPs in Human Pathogenesis
The Journal of Pharmacology and Experimental Therapeutics, 2023Ras-GTPase-activating protein (SH3 domain)-binding proteins (G3BP) are RNA binding proteins that play a critical role in stress granule (SG) formation. SGs protect critical mRNAs from various environmental stress conditions by regulating mRNA stability and translation to maintain regulated gene expression.
Chandrani Mukhopadhyay, Pengbo Zhou
openaire +2 more sources
G3BP–Caprin1–USP10 complexes mediate stress granule condensation and associate with 40S subunits [PDF]
Mammalian stress granules (SGs) contain stalled translation preinitiation complexes that are assembled into discrete granules by specific RNA-binding proteins such as G3BP. We now show that cells lacking both G3BP1 and G3BP2 cannot form SGs in response to eukaryotic initiation factor 2α phosphorylation or eIF4A inhibition, but are still SG-competent ...
Nancy Kedersha +2 more
exaly +4 more sources
RasGAP-Associated Endoribonuclease G3BP: Selective RNA Degradation and Phosphorylation-Dependent Localization [PDF]
Mitogen activation of mRNA decay pathways likely involves specific endoribonucleases, such as G3BP, a phosphorylation-dependent endoribonuclease that associates with RasGAP in dividing but not quiescent cells. G3BP exclusively cleaves between cytosine and adenine (CA) after a specific interaction with RNA through the carboxyl-terminal RRM-type RNA ...
Imed-Eddine Gallouzi +2 more
exaly +3 more sources

