ArticleNucleic acids research1993
A topoisomerase II-like protein is part of an inducible DNA-binding protein complex that binds 5' of an immunoglobulin promoter.
Article in Nucleic acids research, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed, 15 citations in OpenAlex.
- The Bright Side of Hematopoiesis: Regulatory Roles of ARID3a/Bright in Human and Mouse Hematopoiesis.Frontiers in immunology · 2014Review
- Transcription-induced DNA double strand breaks: both oncogenic force and potential therapeutic target?Clinical cancer research : an official journal of the American Association for Cancer Research · 2011Article
- Bruton's tyrosine kinase regulates immunoglobulin promoter activation in association with the transcription factor Bright.Molecular and cellular biology · 2005Article
- The transcription factor, Bright, and immunoglobulin heavy chain expression.Immunologic research · 2001Review
- Structure and function of type II DNA topoisomerases.The Biochemical journal · 1994Review
- Altered stability of etoposide-induced topoisomerase II-DNA complexes in resistant human leukaemia K562 cells.British journal of cancer · 1994Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
We previously identified a B cell-specific protein-DNA complex 5' of an immunoglobulin mu heavy chain promoter. The sequences to which this protein complex bound were required for induction of immunoglobulin mRNA levels with interleukin-5 + antigen. Further studies identified a second sequence 5' of these regulatory sequences that bound to both the nuclear matrix and to a similar interleukin-5 + antigen inducible protein complex. Therefore, we sought to identify the putative regulatory proteins that comprised this DNA-binding complex. In this study, we have used anti-topoisomerase II antibodies to demonstrate that one of the proteins found in the interleukin-5 + antigen inducible complexes is serologically related to topoisomerase II. To our knowledge, this is the first report where a topoisomerase II related protein participates in an inducible mobility shifted protein-DNA complex. These data suggest a model in which the enhanced immunoglobulin gene transcription observed after treatment with interleukin-5 + antigen might be explained by the induction of a protein complex that acts to relieve torsional stress along the gene.
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Registered trials
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