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Funnell, B.E. (1991) The P1 plasmid partition complex at parS. The influence of Escherichia coli integration host factor and of substrate topology. The Journal of Biological Chemistry, 266, 14328-14337.

has been cited by the following article:

• TITLE: SSINCC: Simple separation of interacting nucleoprotein complex components

  AUTHORS: Roderick A. Slavcev, Nafiseh Nafissi, Tranum Kaur

  KEYWORDS: DNA-Protein-DNA Interaction Assay; Plasmid Partition Nucleoprotein Complex; Specific Nucleoprotein Complex Separation

  JOURNAL NAME: Advances in Biological Chemistry, Vol.2 No.2, May 10, 2012

  ABSTRACT: Protein-DNA binding assays have been used in a va-riety of applications from fundamental studies re-garding the binding process itself to serve as probes for the detection, quantification and separation of target analytes. Here we describe a novel method of analyzing and identifying intermolecular DNA interactions that allows for the simple separation of interacting nucleoprotein complex components (SSINCC), focusing specifically on DNA-DNA interactions using P1 plasmid active partition system nucleoprotein complexes as a model to demonstrate DNA sequence specificity and tolerance of composite factor complexity. Traditional and recent assays of protein-DNA interaction are summarized and compared with SSINC. Although SSINC is examined here employing P1 partition nucleoprotein complex as an example of DNA-DNA intermolecular association, universal applications of this methodology to nucleo-protein complex studies can be envisioned.