Results 151 to 160 of about 4,644 (183)

Connecting the Dots: Stress Granule and Cardiovascular Diseases. [PDF]

J Cardiovasc Transl Res
Yang G, Wang Y, Guo J, Rui T.
europepmc   +1 more source

Stress granule formation helps to mitigate neurodegeneration. [PDF]

Nucleic Acids Res
Glineburg MR, Yildirim E, Gomez N, Rodriguez G, Pak J, Li X, Altheim C, Waksmacki J, McInerney GM, Barmada SJ, Todd PK.   +10 more
europepmc   +1 more source

UBAP2L contributes to formation of P-bodies and modulates their association with stress granules. [PDF]

J Cell Biol
Riggs CL, Kedersha N, Amarsanaa M, Zubair SN, Ivanov P, Anderson P.   +5 more
europepmc   +1 more source

Convergent evolution of the G3BP1-binding motif in betacoronavirus nucleocapsid proteins. [PDF]

Virus Evol
Borgogna C, Cislaghi I, Turati S, Mozzi A, Forni D, Cagliani R, Sironi M, Gariglio M.   +7 more
europepmc   +1 more source

Mechanobiological regulation of T cells <i>via</i> transient viscoelastic microfluidic confinement.

Lab Chip
Asghari M, Aramesh M, Mathur P, Meng Y, Bernero M, Vogel V, Stavrakis S, deMello AJ.   +7 more
europepmc   +1 more source

Arabidopsis thaliana G3BP Ortholog Rescues Mammalian Stress Granule Phenotype across Kingdoms

International Journal of Molecular Sciences, 2021
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 Gotte, Timothy J C Tan, Gerald M Mcinerney   +2 more
exaly   +4 more sources

G3BP–Caprin1–USP10 complexes mediate stress granule condensation and associate with 40S subunits [PDF]

Journal of Cell Biology, 2016
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, Marc D Panas, Shawn M Lyons   +2 more
exaly   +6 more sources

Tudor‐SN interacts with and co‐localizes with G3BP in stress granules under stress conditions [PDF]

FEBS Letters, 2010
MINT‐7968768, MINT‐7968779: Tudor‐SN (uniprotkb:Q7KZF4) physically interacts (MI:0915) with G3BP (uniprotkb:Q13283) by anti bait coimmunoprecipitation (MI:0006) MINT‐7968800: Tudor‐SN (uniprotkb:Q7KZF4) and TIA‐1 (uniprotkb:P31483) colocalize (MI:0403) by fluorescence microscopy (MI:0416) MINT‐7968789: Tudor‐SN (uniprotkb:Q7KZF4) and G3BP (uniprotkb ...
Xingjie Gao, Lin Ge, Jie Shao
exaly   +4 more sources