Results 31 to 40 of about 1,426,666 (312)

Heterotypic phase separation of Hfq is linked to its roles as an RNA chaperone.

open access: yesCell Reports, 2022
Hfq, an Sm-like protein and the major RNA chaperone in E. coli, has been shown to distribute non-uniformly along a helical path under normal growth conditions and to relocate to the cell poles under certain stress conditions.
Omer Goldberger   +3 more
semanticscholar   +1 more source

RNAs as chaperones [PDF]

open access: yesRNA Biology, 2016
Recently, we found that RNA is a remarkably powerful chaperone that can bind to unfolded proteins and transfer them to Hsp70 for refolding. Combined with past studies on RNA-chaperone interactions, we propose a model for how chaperone RNA activity may contribute to the cellular response to stress.
Scott, Horowitz, James C A, Bardwell
openaire   +2 more sources

Dissecting RNA chaperone activity [PDF]

open access: yesRNA, 2007
Many RNA-binding proteins help RNAs to fold via their RNA chaperone activity. This term has been used widely without accounting for the diversity of the observed reactions, which include complex events like restructuring of misfolded catalytic RNAs, promoting the assembly of RNA-protein complexes, and mediating RNA–RNA interactions.
Rajkowitsch, Lukas, Schroeder, Renée
openaire   +2 more sources

Chaperoning 5S RNA assembly [PDF]

open access: yesGenes & 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

The ribosome can prevent aggregation of partially folded protein intermediates: studies using the Escherichia coli ribosome. [PDF]

open access: yesPLoS ONE, 2014
BACKGROUND: Molecular chaperones that support de novo folding of proteins under non stress condition are classified as chaperone 'foldases' that are distinct from chaperone' holdases' that provide high affinity binding platform for unfolded proteins and ...
Bani Kumar Pathak   +3 more
doaj   +1 more source

SRA inhibition improves antitumor potency of antigen-targeted chaperone vaccine

open access: yesFrontiers 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

RNA Chaperones, RNA Annealers and RNA Helicases [PDF]

open access: yesRNA Biology, 2007
RNA molecules face difficulties when folding into their native structures. In the cell, proteins can assist RNAs in reaching their functionally active states by binding and stabilizing a specific structure or, in a quite opposite way, by interacting in a non-specific manner. These proteins can either facilitate RNA-RNA interactions in a reaction termed
Rajkowitsch, Lukas   +9 more
openaire   +3 more sources

An mRNA-mRNA Interaction Couples Expression of a Virulence Factor and Its Chaperone in Listeria monocytogenes

open access: yesCell 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

RNA chaperones encoded by RNA viruses [PDF]

open access: yesVirologica Sinica, 2015
RNAs are functionally diverse macromolecules whose proper functions rely strictly upon their correct tertiary structures. However, because of their high structural flexibility, correct folding of RNAs is challenging and slow. Therefore, cells and viruses encode a variety of RNA remodeling proteins, including helicases and RNA chaperones. In RNA viruses,
Yang, Jie   +3 more
openaire   +2 more sources

Could Upregulated Hsp70 Protein Compensate for the Hsp90-Silence-Induced Cell Death in Glioma Cells? [PDF]

open access: yes, 2014
The molecular chaperone heat shock protein 90 alpha (Hsp90α) has been recognized in various tumours including glioma. This pilot study using a proteomic approach analyses the downstream effects of Hsp90 inhibition using 17-allylamino-17 ...
Khan, Zarine Jamsher   +3 more
core   +4 more sources

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