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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
11
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pubmed:dateCreated |
1989-5-18
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pubmed:abstractText |
Stable complex formation on a Xenopus somatic 5 S RNA gene requires protein-protein interactions between the non-DNA binding domain of transcription factor (TF) IIIA and activities in a TFIIIC fraction. No significant changes in the structure of the TFIIIA.DNA complex can be detected as a consequence of stabilization, indicating that protein confirmation is the primary determinant of stability.
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pubmed:grant |
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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 |
Apr
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
264
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
6009-12
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:2703476-Animals,
pubmed-meshheading:2703476-DNA, Ribosomal,
pubmed-meshheading:2703476-DNA-Binding Proteins,
pubmed-meshheading:2703476-Gene Expression Regulation,
pubmed-meshheading:2703476-Peptide Fragments,
pubmed-meshheading:2703476-Protein Binding,
pubmed-meshheading:2703476-RNA, Ribosomal,
pubmed-meshheading:2703476-RNA, Ribosomal, 5S,
pubmed-meshheading:2703476-Regulatory Sequences, Nucleic Acid,
pubmed-meshheading:2703476-Structure-Activity Relationship,
pubmed-meshheading:2703476-Temperature,
pubmed-meshheading:2703476-Transcription, Genetic,
pubmed-meshheading:2703476-Transcription Factors,
pubmed-meshheading:2703476-Xenopus laevis
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pubmed:year |
1989
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pubmed:articleTitle |
A protein-protein interaction is essential for stable complex formation on a 5 S RNA gene.
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pubmed:affiliation |
Department of Chemistry, Johns Hopkins University, Baltimore, Maryland 21218.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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