The Affinity of Nuclear Factor 1 for Its DNA Site Is Drastically Reduced by Nucleosome Organization Irrespective of Its Rotational or Translational Position
Open Access
- 1 January 1996
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 271 (1) , 153-159
- https://doi.org/10.1074/jbc.271.1.153
Abstract
No abstract availableKeywords
This publication has 51 references indexed in Scilit:
- Transcription factor nuclear factor I proteins form stable homo‐ and heterodimersFEBS Letters, 1994
- The glucocorticoid receptor acts as an antirepressor in receptor‐dependent in vitro transcriptionEuropean Journal of Biochemistry, 1993
- GC box binding induces phosphorylation of Sp1 by a DNA-dependent protein kinasePublished by Elsevier ,1990
- Nucleosome positioning modulates accessibility of regulatory proteins to the mouse mammary tumor virus promoterCell, 1990
- Structural and functional organization of a porcine gene coding for nuclear factor IBiochemistry, 1989
- Distinct sequence elements involved in the glucocorticoid regulation of the mouse mammary tumor virus promoter identified by linker scanning mutagenesisJournal of Molecular Biology, 1986
- Structure and function of the adenovirus origin of replicationCell, 1984
- Kinetic analysis of deoxyribonuclease I cleavages in the nucleosome core: Evidence for a DNA superhelixJournal of Molecular Biology, 1978
- Nucleosomal DNA is digested to repeats of 10 bases by exonuclease IIICell, 1978
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976