GCN4 Binds with High Affinity to DNA Sequences Containing a Single Consensus Half-Site
- 1 May 2000
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 39 (21) , 6380-6389
- https://doi.org/10.1021/bi992705n
Abstract
No abstract availableKeywords
This publication has 75 references indexed in Scilit:
- Theoretical aspects of DNA-protein interactions: Co-operative and non-co-operative binding of large ligands to a one-dimensional homogeneous latticePublished by Elsevier ,2004
- Temperature dependence of intramolecular dynamics of the basic leucine zipper of GCN4: implications for the entropy of association with DNAJournal of Molecular Biology, 1999
- Thermodynamics of the interactions of Lac repressor with variants of the symmetric Lac operator: effects of converting a consensus site to a non-specific siteJournal of Molecular Biology, 1997
- Crystal Structure of a bZIP/DNA Complex at 2.2 Å: Determinants of DNA Specific RecognitionJournal of Molecular Biology, 1995
- Only one of the two DNA-bound orientations of AP-1 found in solution cooperates with NFATpCurrent Biology, 1995
- X-Ray Structure of the GCN4 Leucine Zipper, a Two-Stranded, Parallel Coiled CoilScience, 1991
- Defining Target Sequences of DNA-Binding Proteins by Random Selection and PCR: Determination of the GCN4 Binding Sequence RepertoireDNA and Cell Biology, 1990
- Thermal unfolding studies of a leucine zipper domain and its specific DNA complex: implications for scissor's grip recognitionBiochemistry, 1990
- A Fos protein containing the Jun leucine zipper forms a homodimer which binds to the AP1 binding siteNature, 1989
- The carboxy‐terminal domain of the LexA repressor oligomerises essentially as the entire proteinFEBS Letters, 1988