W
Wei Li
Researcher at Brigham and Women's Hospital
Publications - 7
Citations - 2523
Wei Li is an academic researcher from Brigham and Women's Hospital. The author has contributed to research in topics: Stress granule & Phosphoprotein. The author has an hindex of 5, co-authored 7 publications receiving 2268 citations. Previous affiliations of Wei Li include Harvard University.
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Journal ArticleDOI
RNA-Binding Proteins Tia-1 and Tiar Link the Phosphorylation of Eif-2α to the Assembly of Mammalian Stress Granules
TL;DR: The ability of a TIA-1 mutant lacking its RNA-binding domains to function as a transdominant inhibitor of SG formation suggests that this RNA- binding protein acts downstream of the phosphorylation of eIF-2α to promote the sequestration of untranslated mRNAs at SGs.
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Dynamic shuttling of TIA-1 accompanies the recruitment of mRNA to mammalian stress granules.
Nancy Kedersha,Michael Cho,Wei Li,Patrick W. Yacono,Samantha Chen,Natalie Gilks,David E. Golan,Paul A. Anderson +7 more
TL;DR: Fluorescence recovery after photobleaching shows that both TIA-1 and PABP-I rapidly and continuously shuttle in and out ofSGs, indicating that the assembly of SGs is a highly dynamic process, and proposes that mammalian SGs are sites at which untranslated mRNAs are sorted and processed for either reinitiation, degradation, or packaging into stable nonpolysomal mRNP complexes.
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Evidence that ternary complex (eIF2-GTP-tRNA(i)(Met))-deficient preinitiation complexes are core constituents of mammalian stress granules.
TL;DR: This paper showed that environmental stress-induced phosphorylation of eIF2α inhibits protein translation by reducing the availability of the ternary complex that joins initiator tRNAMet to the 43S pre...
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FAST Is a Survival Protein That Senses Mitochondrial Stress and Modulates TIA-1-Regulated Changes in Protein Expression
TL;DR: It is shown that RNA interference-mediated knockdown of endogenous FAST results in apoptosis, whereas overexpressed recombinant FAST inhibits Fas- and UV-induced apoptosis; indicating that FAST is a survival protein.
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FAST is a BCL-XL-associated mitochondrial protein
TL;DR: The results suggest that FAST-BCL-X(L) interactions are likely to regulate mitochondrial metabolism during Fas-induced apoptosis.