Results 11 to 20 of about 2,112,303 (205)
DEAD-box helicase proteins disrupt RNA tertiary structure through helix capture. [PDF]
PLoS Biology, 2014 DEAD-box helicase proteins accelerate folding and rearrangements of highly structured RNAs and RNA-protein complexes (RNPs) in many essential cellular processes. Although DEAD-box proteins have been shown to use ATP to unwind short RNA helices, it is not
Cynthia Pan +6 more
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Selective pharmacological targeting of a DEAD box RNA helicase. [PDF]
PLoS ONE, 2008 RNA helicases represent a large family of proteins implicated in many biological processes including ribosome biogenesis, splicing, translation and mRNA degradation. However, these proteins have little substrate specificity, making inhibition of selected
Lisa Lindqvist +11 more
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mBio, 2018 Present in every kingdom of life, generally in multiple copies, DEAD-box RNA helicases are specialized enzymes that unwind RNA secondary structures. They play major roles in mRNA decay, ribosome biogenesis, and adaptation to cold temperatures.
Lamya El Mortaji +7 more
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Structural basis for RNA-duplex unwinding by the DEAD-box helicase DbpA [PDF]
, 2023 DEAD-box RNA helicases are implicated in most aspects of RNA biology, where these enzymes unwind short RNA duplexes in an ATP-dependent manner. During the central step of the unwinding cycle, the two domains of the helicase core form a distinct closed ...
Jan Philip Wurm +1 more
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DEAD-Box Helicase DDX6 Facilitated RIG-I-Mediated Type-I Interferon Response to EV71 Infection
Frontiers in Cellular and Infection Microbiology, 2021 Previous studies have shown that DEAD (Asp-Glu-Ala-Asp)-box RNA helicases play important roles in viral infection, either as cytosolic sensors of pathogenic molecules or as essential host factors against viral infection.
Rui Zhang +9 more
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Allosteric activation of RhlB by RNase E induces partial duplex opening in substrate RNA
Frontiers in Molecular Biosciences, 2023 The E. coli DEAD-Box helicase RhlB is responsible for ATP-dependent unwinding of structured mRNA to facilitate RNA degradation by the protein complex degradosome.
Heidi Zetzsche +2 more
doaj +1 more source
PLoS Pathogens, 2020 Positive-stranded (+)RNA viruses greatly exploit host cells to support viral replication. However, unlike many other pathogens, (+)RNA viruses code for only a limited number of genes, making them highly dependent on numerous co-opted host factors for ...
Cheng-Yu Wu, Peter D Nagy
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DEAD-Box Helicases: Sensors, Regulators, and Effectors for Antiviral Defense
Viruses, 2020 DEAD-box helicases are a large family of conserved RNA-binding proteins that belong to the broader group of cellular DExD/H helicases. Members of the DEAD-box helicase family have roles throughout cellular RNA metabolism from biogenesis to decay ...
Frances Taschuk, Sara Cherry
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Recognition of two distinct elements in the RNA substrate by the RNA-binding domain of the T. thermophilus DEAD box helicase Hera [PDF]
, 2013 DEAD box helicases catalyze the ATP-dependent destabilization of RNA duplexes. Whereas duplex separation is mediated by the helicase core shared by all members of the family, flanking domains often contribute to binding of the RNA substrate.
Wöhnert, Jens +5 more
core +1 more source
Domain orientation in the RNA helicase YxiN and the role of conformational changes for RNA unwinding [PDF]
, 2010 The RNA helicase YxiN from Bacillus subtilis is a member of the family of DEAD box proteins. YxiN is able to unwind RNA double strands in an ATP-dependent manner. The ability to catalyse RNA rearrangement is in vivo presumably necessary for the bacterial
Karow, Anne R.
core +1 more source