About: RNA helicases and remodeling proteins

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An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	RNA helicases and remodeling proteins
Creator	Pyle, Anna Raney, Kevin Benkovic, Stephen
Source	Elsevier; Medline; PMC
abstract	It is becoming increasingly clear that RNA molecules play a major role in all aspects of metabolism. The conformational state and stability of RNA are controlled by RNA remodeling proteins, which are ubiquitous motor proteins in the cell. Here, we review advances in our understanding of the structure and function of three major structural families of RNA remodeling proteins, the hexameric ring proteins, the processive monomeric RNA translocase/helicases, and the functionally diverse DEAD-box remodeling proteins. New studies have revealed molecular mechanisms for coupling between ATP hydrolysis and unwinding, the physical basis for regulatory control by cofactors, and novel functions for RNA remodeling proteins.
has issue date	2011-08-20(xsd:dateTime)
bibo:doi	10.1016/j.cbpa.2011.07.019
bibo:pmid	21862383
has license	no-cc
sha1sum (hex)	b06ad4ab91a03fdb0daf5405d448224ef9857ca0
schema:url	https://doi.org/10.1016/j.cbpa.2011.07.019
resource representing a document's title	RNA helicases and remodeling proteins
has PubMed Central identifier	PMC7172669
has PubMed identifier	21862383
schema:publication	Curr Opin Chem Biol
resource representing a document's body	covid:b06ad4ab91a03fdb0daf5405d448224ef9857ca0#body_text
is schema:about of	named entity 'play' named entity 'cell' named entity 'ATP hydrolysis' named entity 'RNA' named entity 'control' named entity 'structural' named entity 'metabolism' named entity 'RNA' named entity 'FUNCTIONS' named entity 'MOLECULES' named entity 'RNA' named entity 'remodeling' named entity 'unwinding' named entity 'functions' named entity 'advances' named entity 'RNA' named entity 'RNA molecules' named entity 'RNA' named entity 'processive' named entity 'physical basis' named entity 'cofactors' named entity 'helicases' named entity 'hexameric' named entity 'regulatory control' named entity 'proteins' named entity 'Molecular Machines' named entity 'motor proteins' named entity 'small molecule' named entity 'RNA' named entity 'helicases' named entity 'motif' named entity 'hydrolyze ATP' named entity 'base pairs' named entity 'ATP' named entity 'RNA' named entity 'NS3' named entity 'ATP' named entity 'Dengue' named entity 'helicase' named entity 'ATP hydrolysis' named entity 'regulatory protein' named entity 'DEAD-box' named entity 'RNA' named entity 'helicase' named entity 'NS3' named entity 'molecule' named entity 'protein' named entity 'RNA duplex' named entity 'protease' named entity 'protein' named entity 'translocation' named entity 'binding cleft' named entity 'ATP hydrolysis' named entity 'papillomavirus' named entity 'conformations' named entity 'nucleotide' named entity 'group II intron' named entity 'motor proteins' named entity 'DEAD-box' named entity 'helicase' named entity 'HCV' named entity 'phosphate' named entity 'Biophysical' named entity 'RNA' named entity 'HCV' named entity 'RNA' named entity 'molecule' named entity 'RNA' named entity 'phylogenetic relationships' named entity 'change shape' named entity 'base-pair' named entity 'helicase' named entity '49, 50' named entity 'conformation' named entity 'protein' named entity 'RNA' named entity 'HCV' named entity 'ATP hydrolysis' named entity 'power stroke'

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