Mesothelinspecific T cell cytotoxicity against triple negative breast cancer is enhanced by 40s ribosomal protein subunit 3treated selfdifferentiated dendritic cells.
our results revealed the previously unknown crucial role of the uS3 tetrapeptide (60)GEKG(63) in translation initiation related to maintaining the proper structure of the 48S complex most likely via the prevention of premature mRNA loading into the ribosomal channel.
Quantitative model is presented for a tandem arrangement of two helicase active sites on the ribosome are tested. One of the proteins involved in helicase activity is RPS3.
abasic sites which can occur in mRNAs due to oxidative stress and ageing are able to interact directly with the uS3 fragment exposed on the 40S subunit surface near the mRNA entry channel during translation.
These results suggest that Tat inhibits cell proliferation via an interaction with RPS3 and thereby disrupts mitotic spindle formation during HIV-1 infection. These results might provide insight into the mechanism underlying lymphocyte pathogenesis during HIV-1 infection.
Results found that BfrB subverts the host innate immune system by binding the NF-kappaB subunit RPS3 and promotes the survival of mycobacteria in macrophages by inhibiting cytokine production in host cells.
Short 5'UTR mRNAs are enriched with TISU (translation initiator of short 5'UTR) a 12-nucleotide element directing efficient scanning-independent translation. This study demonstrate that TISU is particularly dependent on eukaryotic initiation factor 1A (eIF1A) which interacts with both RPS3 and RPS10e.
a novel cell fate determination mechanism to ensure cells undergo programed cell death through interfering with RPS3/NF-kappaB-conferred anti-apoptotic transcription by the fragment from partial p65 cleavage by activated Caspase-3
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