Results 71 to 80 of about 5,373 (162)

Acidic C-terminal domains autoregulate the RNA chaperone Hfq

open access: yeseLife, 2017
The RNA chaperone Hfq is an Sm protein that facilitates base pairing between bacterial small RNAs (sRNAs) and mRNAs involved in stress response and pathogenesis. Hfq possesses an intrinsically disordered C-terminal domain (CTD) that may tune the function
Andrew Santiago-Frangos   +3 more
doaj   +1 more source

RNA reflections: converging on Hfq [PDF]

open access: hybrid, 2015
Susan Gottesman, Gisela Storz
openalex   +1 more source

Hfq and sRNA 179 Inhibit Expression of the Pseudomonas aeruginosa cAMP-Vfr and Type III Secretion Regulons

open access: gold, 2020
Kayley H. Janssen   +10 more
openalex   +1 more source

Clostridium difficile Hfq can replace Escherichia coli Hfq for most of its function [PDF]

open access: hybrid, 2014
J. Caillet   +3 more
openalex   +1 more source

Reviewer #3 (Public Review): An Hfq-dependent post-transcriptional mechanism fine tunes RecB expression in Escherichia coli [PDF]

open access: gold
Irina Kalita   +5 more
openalex   +1 more source

Global analysis of small RNA and mRNA targets of Hfq [PDF]

open access: bronze, 2003
Aixia Zhang   +5 more
openalex   +1 more source

Additional file 2: Figure S1. of In vivo characterization of an Hfq protein encoded by the Bacillus anthracis virulence plasmid pXO1

open access: gold, 2017
Keefer Andrea   +8 more
openalex   +1 more source

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