Results 41 to 50 of about 2,639,376 (307)

RNA processing: Pocket guides to ribosomal RNA [PDF]

open access: yesCurrent Biology, 1997
The functional role of a recently identified class of small nucleolar (sno) RNAs has been elucidated: the 'box H/ACA' snoRNAs act as guide RNAs, specifying the position of evolutionarily conserved pseudouridines in ribosomal (r)RNA via an rRNA-snoRNA base-pairing interaction that forms a 'pseudouridine pocket'.
openaire   +2 more sources

MicroRNA-target binding structures mimic microRNA duplex structures in humans. [PDF]

open access: yesPLoS ONE, 2014
Traditionally, researchers match a microRNA guide strand to mRNA sequences using sequence comparisons to predict its potential target genes. However, many of the predictions can be false positives due to limitations in sequence comparison alone.
Xi Chen, Lu Shen, Hui-Hsien Chou
doaj   +1 more source

A guide to ions and RNA structure [PDF]

open access: yesRNA, 2004
RNA folding into stable tertiary structures is remarkably sensitive to the concentrations and types of cations present; an understanding of the physical basis of ion-RNA interactions is therefore a prerequisite for a quantitative accounting of RNA stability.
openaire   +2 more sources

A hepatitis C virus cis-acting replication element forms a long-range RNA-RNA interaction with upstream RNA sequences in NS5B [PDF]

open access: yes, 2008
The genome of hepatitis C virus (HCV) contains cis-acting replication elements (CREs) comprised of RNA stem-loop structures located in both the 5' and 3' non-coding regions (NCR), and in the NS5B coding sequence.
Diviney, Sinéad   +22 more
core   +1 more source

An improved in vivo tethering assay with single molecule FISH reveals that a nematode Nanos enhances reporter expression and mRNA stability

open access: yes, 2021
Robust methods are critical for testing the in vivo regulatory mechanism of RNA binding proteins. Here we report improvement of a protein–mRNA tethering assay to probe the function of an RNA binding protein in its natural context within the C.
Kimble, Judith   +3 more
core   +1 more source

Mechanistic Insights into Archaeal and Human Argonaute Substrate Binding and Cleavage Properties.

open access: yesPLoS ONE, 2016
Argonaute (Ago) proteins from all three domains of life are key players in processes that specifically regulate cellular nucleic acid levels.
Sarah Willkomm   +3 more
doaj   +1 more source

RNA-programmed genome editing in human cells

open access: yeseLife, 2013
Type II CRISPR immune systems in bacteria use a dual RNA-guided DNA endonuclease, Cas9, to cleave foreign DNA at specific sites. We show here that Cas9 assembles with hybrid guide RNAs in human cells and can induce the formation of double-strand DNA ...
Martin Jinek   +5 more
doaj   +1 more source

RNA-guided RNA silencing by an Asgard archaeal Argonaute

open access: yesNature Communications, 2023
Abstract Argonaute proteins are the central effectors of RNA-guided RNA silencing pathways in eukaryotes, playing crucial roles in gene repression and defense against viruses and transposons. Eukaryotic Argonautes are subdivided into two clades: AGOs generally facilitate miRNA- or siRNA-mediated silencing, while ...
Carolien Bastiaanssen   +13 more
openaire   +3 more sources

Diverging affinity of tospovirus RNA silencing suppressor proteins, NSs, for various RNA duplex molecules [PDF]

open access: yes, 2010
The tospovirus NSs protein was previously shown to suppress the antiviral RNA silencing mechanism in plants. Here the biochemical analysis of NSs proteins from different tospoviruses, using purified NSs or NSs containing cell extracts, is described.
Kormelink, R.J.M.   +16 more
core   +1 more source

Craspase is a CRISPR RNA-guided, RNA-activated protease

open access: yesScience, 2022
The CRISPR-Cas type III-E RNA-targeting effector complex gRAMP/Cas7-11 is associated with a caspase-like protein (TPR-CHAT/Csx29) to form Craspase (CRISPR-guided caspase). Here, we use cryo–electron microscopy snapshots of Craspase to explain its target RNA cleavage and protease activation mechanisms.
Hu, Chunyi   +11 more
openaire   +4 more sources

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