Results 31 to 40 of about 92,611 (279)
Cell Reports, 2020 Summary: Bacterial pathogens often employ RNA regulatory elements located in the 5′ untranslated regions (UTRs) to control gene expression. Using a comparative structural analysis, we examine the structure of 5′ UTRs at a global scale in the pathogenic ...
Dmitriy Ignatov +10 more
doaj +1 more source
SRA inhibition improves antitumor potency of antigen-targeted chaperone vaccine
Frontiers in Immunology, 2023 We have previously demonstrated that scavenger receptor A (SRA) acts as an immunosuppressive regulator of dendritic cell (DC) function in activating antitumor T cells.
Jie Qian +13 more
doaj +1 more source
Proteins That Chaperone RNA Regulation [PDF]
Microbiology Spectrum, 2018 ABSTRACT RNA-binding proteins chaperone the biological functions of noncoding RNA by reducing RNA misfolding, improving matchmaking between regulatory RNA and targets, and exerting quality control over RNP biogenesis. Recent studies of Escherichia coli CspA, HIV NCp, and E. coli Hfq
Sarah A, Woodson +2 more
openaire +2 more sources
Viruses, 2020 The 3′-terminal stem-loop (3′SL) of the RNA genome of the flavivirus West Nile (WNV) harbors, in its stem, one of the sequence elements that are required for genome cyclization.
Alexandra Meyer +7 more
doaj +1 more source
Chaperoning 5S RNA assembly [PDF]
Genes & Development, 2015 In eukaryotes, three of the four ribosomal RNAs (rRNAs)—the 5.8S, 18S, and 25S/28S rRNAs—are processed from a single pre-rRNA transcript and assembled into ribosomes. The fourth rRNA, the 5S rRNA, is transcribed by RNA polymerase III and is assembled into the 5S ribonucleoprotein particle (RNP), containing ribosomal proteins Rpl5/uL18 and Rpl11/uL5 ...
Madru, Clément +7 more
openaire +3 more sources
Protein solubility and folding enhancement by interaction with RNA. [PDF]
PLoS ONE, 2008 While basic mechanisms of several major molecular chaperones are well understood, this machinery has been known to be involved in folding of only limited number of proteins inside the cells. Here, we report a chaperone type of protein folding facilitated
Seong Il Choi +12 more
doaj +1 more source
Nature Communications, 2022 In this work, the authors determine the crystal structure of a ProQ/FinO RNA chaperone bound to its RNA target. This provides insight into how this family of bacterial proteins recognize transcriptional terminator structures.
Hyeong Jin Kim +16 more
doaj +1 more source
The yeast histone chaperone hif1p functions with RNA in nucleosome assembly. [PDF]
PLoS ONE, 2014 Hif1p is an H3/H4-specific histone chaperone that associates with the nuclear form of the Hat1p/Hat2p complex (NuB4 complex) in the yeast Saccharomyces cerevisiae. While not capable of depositing histones onto DNA on its own, Hif1p can act in conjunction
Amy R Knapp, Huanyu Wang, Mark R Parthun
doaj +1 more source
An improved method for surface immobilisation of RNA: application to small Non-Coding RNA - mRNA pairing [PDF]
, 2013 Characterisation of RNA and its intermolecular interactions is increasing in importance as the inventory of known RNA functions continues to expand. RNA-RNA interactions are central to post-transcriptional gene regulation mechanisms in bacteria, and the ...
Darren M. Gowers (485354) +29 more
core +1 more source
The RGG/RG motif of AUF1 isoform p45 is a key modulator of the protein’s RNA chaperone and RNA annealing activities [PDF]
RNA Biology, 2019 Tobias Schmidt +2 more
exaly +2 more sources