Results 171 to 180 of about 10,886 (208)

An Hfq-binding sRNA in Listeria monocytogenes regulates a virulence adhesin in an Hfq-independent manner [PDF]

open access: yes, 2012
Sievers, Susanne   +5 more
openaire   +1 more source

Transcriptome-scale analysis uncovers conserved residues in the hydrophobic core of the bacterial RNA chaperone Hfq required for small regulatory RNA stability. [PDF]

open access: yesNucleic Acids Res
McQuail J   +10 more
europepmc   +1 more source

Acoziborole resistance associated mutations in trypanosome CPSF3

open access: yes
Ridgway M   +6 more
europepmc   +1 more source

The type 6 secretion system immunity protein RhsFI has been repurposed for small RNA regulation in pathogenic Escherichia coli. [PDF]

open access: yesNucleic Acids Res
Zammit T   +15 more
europepmc   +1 more source

Hfq and its constellation of RNA [PDF]

open access: yesNature Reviews Microbiology, 2011
Hfq is an RNA-binding protein that is common to diverse bacterial lineages and has key roles in the control of gene expression. By facilitating the pairing of small RNAs with their target mRNAs, Hfq affects the translation and turnover rates of specific transcripts and contributes to complex post-transcriptional networks.
Jörg Vogel, Ben F Luisi
exaly   +3 more sources

Characterization of Vibrio cholerae Hfq Provides Novel Insights into the Role of the Hfq C-Terminal Region

open access: yesJournal of Molecular Biology, 2012
Hfq is a bacterial RNA binding protein that facilitates small RNA-mediated posttranscriptional gene regulation. In Vibrio cholerae, Hfq and four Hfq-dependent small RNAs are essential for the expression of virulence genes, but little is known about this mechanism at the molecular level. To better understand V.
Acely Garza-Garcia   +2 more
exaly   +5 more sources
Some of the next articles are maybe not open access.

Related searches:

Structure ofPseudomonas aeruginosaHfq protein

Acta Crystallographica Section D Biological Crystallography, 2005
The structure of the Hfq protein from Pseudomonas aeruginosa was determined using two different ionic conditions. In both cases the molecules formed identical hexameric rings, but some variations in the crystal packing were revealed. Hfq belongs to the family of Sm/LSm proteins, the members of which can form hexameric as well as heptameric rings ...
Nikulin, Alexey D.   +10 more
openaire   +3 more sources

Home - About - Disclaimer - Privacy