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rdf:type |
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lifeskim:mentions |
umls-concept:C0074785,
umls-concept:C0086418,
umls-concept:C0162326,
umls-concept:C0185026,
umls-concept:C0336791,
umls-concept:C0439855,
umls-concept:C0443286,
umls-concept:C0936012,
umls-concept:C1514433,
umls-concept:C1514562,
umls-concept:C1537502
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pubmed:issue |
17
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pubmed:dateCreated |
2011-4-15
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pubmed:abstractText |
We employed primer extension reactions to uncover folding motifs in a nuclease hypersensitive element (NHE) with a complex guanine pattern, located in the human KRAS promoter. We also identified and characterized a new G-rich motif of 21 nt capable of forming a parallel G-quadruplex that is disrupted by protein UP1.
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
1364-548X
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pubmed:author |
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pubmed:copyrightInfo |
© The Royal Society of Chemistry 2011
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pubmed:issnType |
Electronic
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pubmed:day |
7
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pubmed:volume |
47
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4965-7
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pubmed:meshHeading |
pubmed-meshheading:21424008-Amino Acid Motifs,
pubmed-meshheading:21424008-Binding Sites,
pubmed-meshheading:21424008-DNA Primers,
pubmed-meshheading:21424008-Electrophoretic Mobility Shift Assay,
pubmed-meshheading:21424008-G-Quadruplexes,
pubmed-meshheading:21424008-Gene Expression Regulation,
pubmed-meshheading:21424008-Genes, ras,
pubmed-meshheading:21424008-Guanine,
pubmed-meshheading:21424008-Heterogeneous-Nuclear Ribonucleoprotein Group A-B,
pubmed-meshheading:21424008-Humans,
pubmed-meshheading:21424008-Nucleic Acid Conformation,
pubmed-meshheading:21424008-Promoter Regions, Genetic,
pubmed-meshheading:21424008-Protein Binding,
pubmed-meshheading:21424008-Protein Structure, Tertiary,
pubmed-meshheading:21424008-Spectroscopy, Fourier Transform Infrared,
pubmed-meshheading:21424008-Transcription, Genetic
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pubmed:year |
2011
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pubmed:articleTitle |
Primer extension reactions as a tool to uncover folding motifs within complex G-rich sequences: analysis of the human KRAS NHE.
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pubmed:affiliation |
Department of Medical and Biological Science, University of Udine, 33100 Udine, Italy.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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