@article {321,
	title = {Toward a molecular understanding of RNA remodeling by DEAD-box proteins.},
	journal = {RNA Biol},
	volume = {10},
	number = {1},
	year = {2013},
	month = {2013 Jan},
	pages = {44-55},
	abstract = {DEAD-box proteins are superfamily 2 helicases that function in all aspects of RNA metabolism. They employ ATP binding and hydrolysis to generate tight, yet regulated RNA binding, which is used to unwind short RNA helices non-processively and promote structural transitions of RNA and RNA-protein substrates. In the last few years, substantial progress has been made toward a detailed, quantitative understanding of the structural and biochemical properties of DEAD-box proteins. Concurrently, progress has been made toward a physical understanding of the RNA rearrangements and folding steps that are accelerated by DEAD-box proteins in model systems. Here, we review the recent progress on both of these fronts, focusing on the mitochondrial DEAD-box proteins Mss116 and CYT-19 and their mechanisms in promoting the splicing of group I and group II introns.},
	keywords = {DEAD-box RNA Helicases, RNA},
	issn = {1555-8584},
	doi = {10.4161/rna.22210},
	url = {http://www.tandfonline.com/doi/abs/10.4161/rna.22210?url_ver=Z39.88-2003\&rfr_id=ori\%3Arid\%3Acrossref.org\&rfr_dat=cr_pub\%3Dpubmed\&$\#$.VN0CjbDF990},
	author = {Russell, Rick and Jarmoskaite, Inga and Lambowitz, Alan M}
}
