Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2002-5-6
pubmed:abstractText
Novel ribozymes that couple the cleavage activity of hammerhead ribozymes with the unwinding activity of RNA helicase eIF4AI were constructed. This leads to extremely efficient cleavage of the target mRNA, regardless of the secondary structure of the RNA, and eliminates one of the major problems: many target sites on the RNA were previously inaccessible to cleavage due to secondary and/or tertiary structure formation. Moreover, libraries of hybrid ribozymes with randomized binding arms were introduced into cells. This procedure made it possible to readily identify the relevant genes associated with phenotype. Specifically, four genes known to be in the Fas-mediated apoptosis pathway were identified along with additional genes. This application of a randomized library of hybrid ribozymes represents a simple, powerful method for the identification of genes associated with specific phenotypes in the post-genome era.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/11964387-10021422, http://linkedlifedata.com/resource/pubmed/commentcorrection/11964387-10625515, http://linkedlifedata.com/resource/pubmed/commentcorrection/11964387-10871412, http://linkedlifedata.com/resource/pubmed/commentcorrection/11964387-10873382, http://linkedlifedata.com/resource/pubmed/commentcorrection/11964387-10900014, http://linkedlifedata.com/resource/pubmed/commentcorrection/11964387-11136250, http://linkedlifedata.com/resource/pubmed/commentcorrection/11964387-11278700, http://linkedlifedata.com/resource/pubmed/commentcorrection/11964387-11344300, http://linkedlifedata.com/resource/pubmed/commentcorrection/11964387-1378397, http://linkedlifedata.com/resource/pubmed/commentcorrection/11964387-16819465, http://linkedlifedata.com/resource/pubmed/commentcorrection/11964387-2441261, http://linkedlifedata.com/resource/pubmed/commentcorrection/11964387-2457170, http://linkedlifedata.com/resource/pubmed/commentcorrection/11964387-2687695, http://linkedlifedata.com/resource/pubmed/commentcorrection/11964387-7538907, http://linkedlifedata.com/resource/pubmed/commentcorrection/11964387-7692597, http://linkedlifedata.com/resource/pubmed/commentcorrection/11964387-8026475, http://linkedlifedata.com/resource/pubmed/commentcorrection/11964387-8026476, http://linkedlifedata.com/resource/pubmed/commentcorrection/11964387-8670879, http://linkedlifedata.com/resource/pubmed/commentcorrection/11964387-9204442, http://linkedlifedata.com/resource/pubmed/commentcorrection/11964387-9289491, http://linkedlifedata.com/resource/pubmed/commentcorrection/11964387-9548260, http://linkedlifedata.com/resource/pubmed/commentcorrection/11964387-9607768, http://linkedlifedata.com/resource/pubmed/commentcorrection/11964387-9844634, http://linkedlifedata.com/resource/pubmed/commentcorrection/11964387-9892698, http://linkedlifedata.com/resource/pubmed/commentcorrection/11964387-9918773
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Signal Transducing, http://linkedlifedata.com/resource/pubmed/chemical/Adenosine, http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD95, http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Eukaryotic Initiation Factor-4A, http://linkedlifedata.com/resource/pubmed/chemical/FADD protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Fas-Associated Death Domain Protein, http://linkedlifedata.com/resource/pubmed/chemical/Polymers, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Catalytic, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Transfer, Val, http://linkedlifedata.com/resource/pubmed/chemical/RNA Helicases, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins, http://linkedlifedata.com/resource/pubmed/chemical/polyadenosine
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
1469-221X
pubmed:author
pubmed:issnType
Print
pubmed:volume
3
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
443-50
pubmed:dateRevised
2010-9-14
pubmed:meshHeading
pubmed-meshheading:11964387-Adaptor Proteins, Signal Transducing, pubmed-meshheading:11964387-Adenosine, pubmed-meshheading:11964387-Antigens, CD95, pubmed-meshheading:11964387-Apoptosis, pubmed-meshheading:11964387-Base Sequence, pubmed-meshheading:11964387-Carrier Proteins, pubmed-meshheading:11964387-Eukaryotic Initiation Factor-4A, pubmed-meshheading:11964387-Fas-Associated Death Domain Protein, pubmed-meshheading:11964387-Gene Library, pubmed-meshheading:11964387-HeLa Cells, pubmed-meshheading:11964387-Humans, pubmed-meshheading:11964387-Molecular Sequence Data, pubmed-meshheading:11964387-Polymers, pubmed-meshheading:11964387-RNA, Catalytic, pubmed-meshheading:11964387-RNA, Messenger, pubmed-meshheading:11964387-RNA, Transfer, Val, pubmed-meshheading:11964387-RNA Helicases, pubmed-meshheading:11964387-Recombinant Proteins, pubmed-meshheading:11964387-Substrate Specificity
pubmed:year
2002
pubmed:articleTitle
Identification of genes by hybrid ribozymes that couple cleavage activity with the unwinding activity of an endogenous RNA helicase.
pubmed:affiliation
Department of Chemistry and Biotechnology, School of Engineering, The University of Tokyo, Hongo, Tokyo 113-8656, Japan.
pubmed:publicationType
Journal Article, Retracted Publication, Research Support, Non-U.S. Gov't