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19 in total

1. MondoA, a novel basic helix-loop-helix-leucine zipper transcriptional activator that constitutes a positive branch of a max-like network.

Authors: A N Billin; A L Eilers; K L Coulter; J S Logan; D E Ayer
Journal: Mol Cell Biol Date: 2000-12 Impact factor: 4.272

2. Functional analysis of the Mad1-mSin3A repressor-corepressor interaction reveals determinants of specificity, affinity, and transcriptional response.

Authors: Shaun M Cowley; Richard S Kang; John V Frangioni; Jason J Yada; Alec M DeGrand; Ishwar Radhakrishnan; Robert N Eisenman
Journal: Mol Cell Biol Date: 2004-04 Impact factor: 4.272

3. Solution NMR studies of apo-mSin3A and -mSin3B reveal that the PAH1 and PAH2 domains are structurally independent.

Authors: Yuan He; Ishwar Radhakrishnan
Journal: Protein Sci Date: 2007-11-27 Impact factor: 6.725

4. Targeted deletion of the S-phase-specific Myc antagonist Mad3 sensitizes neuronal and lymphoid cells to radiation-induced apoptosis.

Authors: C Quéva; G A McArthur; B M Iritani; R N Eisenman
Journal: Mol Cell Biol Date: 2001-02 Impact factor: 4.272

5. Identification of the Sin3-binding site in Ume6 defines a two-step process for conversion of Ume6 from a transcriptional repressor to an activator in yeast.

Authors: B K Washburn; R E Esposito
Journal: Mol Cell Biol Date: 2001-03 Impact factor: 4.272

6. Solution structure of the mSin3A PAH2-Pf1 SID1 complex: a Mad1/Mxd1-like interaction disrupted by MRG15 in the Rpd3S/Sin3S complex.

Authors: Ganesan Senthil Kumar; Tao Xie; Yongbo Zhang; Ishwar Radhakrishnan
Journal: J Mol Biol Date: 2011-04-01 Impact factor: 5.469

The Mad protein family links transcriptional repression to cell differentiation.

1. MondoA, a novel basic helix-loop-helix-leucine zipper transcriptional activator that constitutes a positive branch of a max-like network.

2. Functional analysis of the Mad1-mSin3A repressor-corepressor interaction reveals determinants of specificity, affinity, and transcriptional response.

3. Solution NMR studies of apo-mSin3A and -mSin3B reveal that the PAH1 and PAH2 domains are structurally independent.

4. Targeted deletion of the S-phase-specific Myc antagonist Mad3 sensitizes neuronal and lymphoid cells to radiation-induced apoptosis.

5. Identification of the Sin3-binding site in Ume6 defines a two-step process for conversion of Ume6 from a transcriptional repressor to an activator in yeast.

6. Solution structure of the mSin3A PAH2-Pf1 SID1 complex: a Mad1/Mxd1-like interaction disrupted by MRG15 in the Rpd3S/Sin3S complex.

7. The transcriptional repressor dMnt is a regulator of growth in Drosophila melanogaster.

8. The FK506-binding protein 25 functionally associates with histone deacetylases and with transcription factor YY1.

9. A novel role of the Mad family member Mad3 in cerebellar granule neuron precursor proliferation.

10. Thermodynamics of protein-protein interactions of cMyc, Max, and Mad: effect of polyions on protein dimerization.