Journal of Molecular Biology
Volume 248, Issue 3, 5 May 1995, Pages 541-550
Regular ArticleAnalysis of the Myc and Max Interaction Specificity with λ Repressor-HLH Domain Fusions
References (0)
Cited by (27)
BCL2 is a downstream effector of MIZ-1 essential for blocking c-MYC-induced apoptosis
2007, Journal of Biological ChemistryCitation Excerpt :As with any point mutation, it has remained possible that the mutation interferes with other functions of c-MYC. For example, valine 394 is located within the helix-loop-helix domain, an area necessary for interaction with the transcription factor MAX, the ubiquitin ligase SKP2, and the histone acetyltransferase p300 (55–58). To fully validate the c-MYC/MIZ-1/apoptosis pathway, it was necessary to conclusively establish whether the V394D mutation selectively blocks MIZ-1 binding.
IS911 transposition is regulated by protein-protein interactions via a leucine zipper motif
2000, Journal of Molecular BiologyGenetic systems for analyzing protein-protein interactions in bacteria
2000, Research in MicrobiologyUnique DNA binding specificity of the binuclear zinc AlcR activator of the ethanol utilization pathway in Aspergillus nidulans
1999, Journal of Biological Chemistry
- f1
Corresponding author
Copyright © 1995 Academic Press. All rights reserved.