The solution structure and dynamics of the DNA-binding domain of HMG-D from Drosophila melanogaster
- 31 July 1994
- Vol. 2 (7), 609-627
- https://doi.org/10.1016/s0969-2126(00)00063-0
Abstract
No abstract availableKeywords
This publication has 45 references indexed in Scilit:
- Harnessing the writhe: a role for DNA chaperonesin nucleoprotein- complex formationTrends in Biochemical Sciences, 1994
- The SRY high-mobility-group box recognizes DNA by partial intercalation in the minor groove: a topological mechanism of sequence specificity.Proceedings of the National Academy of Sciences, 1993
- High-mobility-group 1 protein mediates DNA bending as determined by ring closures.Proceedings of the National Academy of Sciences, 1993
- The nonspecific DNA-binding and -bending proteins HMG1 and HMG2 promote the assembly of complex nucleoprotein structures.Genes & Development, 1993
- A high-mobility-group protein and its cDNAs from Drosophila melanogaster.Molecular and Cellular Biology, 1992
- HMGs everywhereCurrent Biology, 1992
- The HMG domain of lymphoid enhancer factor 1 bends DNA and facilitates assembly of functional nucleoprotein structuresCell, 1992
- LEF-1, a gene encoding a lymphoid-specific protein with an HMG domain, regulates T-cell receptor alpha enhancer function [corrected]Genes & Development, 1991
- A gene from the human sex-determining region encodes a protein with homology to a conserved DNA-binding motifNature, 1990
- Nucleolar transcription factor hUBF contains a DNA-binding motif with homology to HMG proteinsNature, 1990