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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
13
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pubmed:dateCreated |
1994-8-24
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pubmed:abstractText |
Searches with dsRNA-binding domain profiles detected two copies of the domain in each of RNA helicase A, Drosophila maleless and C. elegans ORF T20G5-11 (of unknown function). RNA helicase A is unusual in being one of the few characterised DEAD/DExH helicases that are active as monomers. Other monomeric DEAD/DExH RNA helicases (p68, NPH-II) have domains that match another RNA-binding motif, the RGG repeat. The DEAD/DExH domain appears to be insufficient on its own to promote helicase activity and additional RNA-binding capacity must be supplied either as domains adjacent to the DEAD/DExH-box or by bound partners as in the eIF-4AB dimer. The presence or absence of extra RNA-binding domains should allow classification of DEAD/DExH proteins as monomeric or multimeric helicases.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041617-1310794,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041617-1332061,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041617-1364113,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041617-1438297,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041617-1438302,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041617-1464325,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041617-1534753,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041617-1537828,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041617-1552844,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041617-1628625,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041617-1653648,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041617-1737751,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041617-1996094,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041617-2085318,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041617-2263459,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041617-2304461,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041617-2461520,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041617-2471939,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041617-3052853,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041617-3140040,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041617-3474607,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041617-6546423,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041617-7694397,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041617-7922339,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041617-8193951,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041617-8253085,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041617-8318535,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041617-8332519,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041617-8332529,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041617-8344961,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041617-8413273,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041617-8435768,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041617-8500177
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Chromosomal Proteins, Non-Histone,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Helicases,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Double-Stranded,
http://linkedlifedata.com/resource/pubmed/chemical/RNA Helicases,
http://linkedlifedata.com/resource/pubmed/chemical/RNA Nucleotidyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/mle protein, Drosophila
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0305-1048
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
11
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pubmed:volume |
22
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2552-6
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:8041617-Amino Acid Sequence,
pubmed-meshheading:8041617-Animals,
pubmed-meshheading:8041617-Chromosomal Proteins, Non-Histone,
pubmed-meshheading:8041617-DNA Helicases,
pubmed-meshheading:8041617-DNA-Binding Proteins,
pubmed-meshheading:8041617-Databases, Factual,
pubmed-meshheading:8041617-Drosophila,
pubmed-meshheading:8041617-Drosophila Proteins,
pubmed-meshheading:8041617-Humans,
pubmed-meshheading:8041617-Male,
pubmed-meshheading:8041617-Molecular Sequence Data,
pubmed-meshheading:8041617-Nuclear Proteins,
pubmed-meshheading:8041617-RNA, Double-Stranded,
pubmed-meshheading:8041617-RNA Helicases,
pubmed-meshheading:8041617-RNA Nucleotidyltransferases,
pubmed-meshheading:8041617-Repetitive Sequences, Nucleic Acid,
pubmed-meshheading:8041617-Sequence Homology, Amino Acid,
pubmed-meshheading:8041617-Transcription Factors
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pubmed:year |
1994
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pubmed:articleTitle |
Detection of dsRNA-binding domains in RNA helicase A and Drosophila maleless: implications for monomeric RNA helicases.
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pubmed:affiliation |
European Molecular Biology Laboratory, Heidelberg, Germany.
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pubmed:publicationType |
Journal Article
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