About: A novel superfamily of nucleoside triphosphate-binding motif containing proteins which are probably involved in duplex unwinding in DNA and RNA replication and recombination

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About: A novel superfamily of nucleoside triphosphate-binding motif containing proteins which are probably involved in duplex unwinding in DNA and RNA replication and recombination Goto Sponge NotDistinct Permalink

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

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	A novel superfamily of nucleoside triphosphate-binding motif containing proteins which are probably involved in duplex unwinding in DNA and RNA replication and recombination
Creator	Gorbalenya, Alexander Blinov, Vladimir Donchenko, Alexei Koonin, Eugene
Source	Elsevier; Medline; PMC
abstract	Abstract A statistically significant similarity was demonstrated between the amino acid sequences of 4 Escherichia coli helicases and helicase subunits, a family of non-structural proteins of eukaryotic positive-strand RNA viruses and 2 herpesvirus proteins all of which contain an NTP-binding sequence motif. Based on sequence analysis and secondary structure predictions, a generalized structural model for the ATP-binding core is proposed. It is suggested that all these proteins constitute a superfamily of helicases (or helicase subunits) involved in NTP-dependent duplex unwinding during DNA and RNA replication and recombination.
has issue date	1988-08-01(xsd:dateTime)
bibo:doi	10.1016/0014-5793(88)81226-2
bibo:pmid	2841153
has license	els-covid
sha1sum (hex)	ba54d4b7d5db3b5382fcbdbb98b14d6290717ce0
schema:url	https://doi.org/10.1016/0014-5793%2888%2981226-2
resource representing a document's title	A novel superfamily of nucleoside triphosphate-binding motif containing proteins which are probably involved in duplex unwinding in DNA and RNA replication and recombination
has PubMed Central identifier	PMC7130140
has PubMed identifier	2841153
schema:publication	FEBS Letters
resource representing a document's body	covid:ba54d4b7d5db3b5382fcbdbb98b14d6290717ce0#body_text
is schema:about of	named entity 'GENERALIZED' named entity 'SEQUENCE MOTIF' named entity 'SUPERFAMILY' named entity 'INVOLVED' named entity 'STRUCTURAL MODEL' covid:arg/ba54d4b7d5db3b5382fcbdbb98b14d6290717ce0 named entity 'helicases' named entity 'involved' named entity 'replication' named entity 'proteins' named entity 'coli' named entity 'unwinding' named entity 'NTP' named entity 'DNA and RNA' named entity 'non-structural proteins' named entity 'ATP-binding' named entity 'statistically significant' named entity 'sequence analysis' named entity 'superfamily' named entity 'eukaryotic' named entity 'recombination' named entity 'proteins' named entity 'binding motif' named entity 'DNA and RNA' named entity 'sequences' named entity 'eukaryotes' named entity 'additional members' named entity 'E. coli' named entity 'protein' named entity 'monophyletic' named entity 'helicase' named entity 'helicase' named entity 'amino acid sequences' named entity 'helicase' named entity 'VZV' named entity 'dsDNA' named entity 'helicases' named entity 'herpesvirus' named entity 'hydrophobic' named entity 'helicase' named entity 'catalytic sites' named entity 'RNA' named entity 'RNA' named entity 'ATP' named entity 'hydrolysis' named entity 'viral proteins' named entity 'conserved domains' named entity 'viruses' named entity 'RNA' named entity 'helicases' named entity 'genomes' named entity 'recBCD' named entity 'oligomers' named entity 'ATP' named entity 'gene product' named entity 'conserved sequence' named entity 'N-terminal' named entity 'protein families' named entity 'herpesvirus' named entity 'NTP' named entity 'protein' named entity 'highly conserved' named entity 'helicases' named entity 'RNA-dependent RNA polymerase' named entity 'RNA' named entity 'NTP' named entity 'biochemical processes' named entity 'nucleic acid' named entity 'conserved residues' named entity 'motif' named entity 'bacteriophage T4' named entity 'gene duplication' named entity 'retroviruses' named entity 'E. coli' named entity 'protein' named entity 'helicases' named entity 'protein' named entity 'retrovirus'

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