Letter to the Editor: Sequence-specific assignment of the PAH2 domain of Sin3B free and bound to Mad1
- 1 January 2001
- journal article
- Published by Springer Nature in Journal of Biomolecular NMR
- Vol. 19 (4) , 377-378
- https://doi.org/10.1023/a:1011262214741
Abstract
No abstract availableThis publication has 9 references indexed in Scilit:
- The Mad1-Sin3B interaction involves a novel helical fold.Nature Structural & Molecular Biology, 2000
- A 13-Amino Acid Amphipathic α-Helix Is Required for the Functional Interaction between the Transcriptional Repressor Mad1 and mSin3AJournal of Biological Chemistry, 1999
- Two MAD tails: what the recent knockouts of Mad1 and Mxi1 tell us about the MYC/MAX/MAD networkBiochimica et Biophysica Acta (BBA) - Reviews on Cancer, 1999
- Coactivator and corepressor complexes in nuclear receptor functionCurrent Opinion in Genetics & Development, 1999
- Repression by the Mad(Mxi1)-Sin3 complexBioEssays, 1998
- NMRPipe: A multidimensional spectral processing system based on UNIX pipesJournal of Biomolecular NMR, 1995
- The program XEASY for computer-supported NMR spectral analysis of biological macromoleculesJournal of Biomolecular NMR, 1995
- Mad-max transcriptional repression is mediated by ternary complex formation with mammalian homologs of yeast repressor Sin3Cell, 1995
- Stereospecific nuclear magnetic resonance assignments of the methyl groups of valine and leucine in the DNA-binding domain of the 434 repressor by biosynthetically directed fractional carbon-13 labelingBiochemistry, 1989