Structure, function, and dynamics of the dimerization and DNA-binding domain of oncogenic transcription factor v-Myc
- 13 April 2001
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 307 (5) , 1395-1410
- https://doi.org/10.1006/jmbi.2001.4537
Abstract
No abstract availableKeywords
This publication has 74 references indexed in Scilit:
- The crystal structure of an intact human Max–DNA complex: new insights into mechanisms of transcriptional controlStructure, 1997
- Insight into a Random Coil Conformation and an Isolated Helix: Structural and Dynamical Characterisation of the C-Helix Peptide from Hen LysozymeJournal of Molecular Biology, 1996
- Backbone Dynamics of a Highly Disordered 131 Residue Fragment of Staphylococcal NucleaseJournal of Molecular Biology, 1994
- Mad: A heterodimeric partner for Max that antagonizes Myc transcriptional activityCell, 1993
- Myc and Max associate in vivo.Genes & Development, 1992
- Myc and Max function as a nucleoprotein complexCurrent Opinion in Genetics & Development, 1992
- Max: A Helix-Loop-Helix Zipper Protein That Forms a Sequence-Specific DNA-Binding Complex with MycScience, 1991
- Sequence-Specific DNA Binding by the c-Myc ProteinScience, 1990
- Temperature dependence of the hydrophobic interaction in protein folding.Proceedings of the National Academy of Sciences, 1986
- Oncogenes in Retroviruses and Cells: Biochemistry and Molecular GeneticsAdvances in Cancer Research, 1986