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Results: 1-8 |
Results: 8
The histone fold is a key structural motif of transcription factor TFIID
Authors: Gangloff, YG Romier, C Thuault, S Werten, S Davidson, I
Citation: Yg. Gangloff et al., The histone fold is a key structural motif of transcription factor TFIID, TRENDS BIOC, 26(4), 2001, pp. 250-257
Histone folds mediate selective heterodimerization of yeast TAF(II)25 withTFIID components yTAF(II)47 and yTAF(II)65 and with SAGA component ySPT7
Authors: Gangloff, YG Sanders, SL Romier, C Kirschner, D Weil, PA Tora, L Davidson, I
Citation: Yg. Gangloff et al., Histone folds mediate selective heterodimerization of yeast TAF(II)25 withTFIID components yTAF(II)47 and yTAF(II)65 and with SAGA component ySPT7, MOL CELL B, 21(5), 2001, pp. 1841-1853
The TFIID components human TAF(II)140 and Drosophila BIP2 (TAF(II)155) arenovel metazoan homologues of yeast TAF(II)47 containing a histone fold anda PHD finger
Authors: Gangloff, YG Pointud, JC Thuault, S Carre, L Romier, C Muratoglu, S Brand, M Tora, L Couderc, JL Davidson, I
Citation: Yg. Gangloff et al., The TFIID components human TAF(II)140 and Drosophila BIP2 (TAF(II)155) arenovel metazoan homologues of yeast TAF(II)47 containing a histone fold anda PHD finger, MOL CELL B, 21(15), 2001, pp. 5109-5121
Dissecting the interaction network of multiprotein complexes by pairwise coexpression of subunits in E-coli
Authors: Fribourg, S Romier, C Werten, S Gangloff, YG Poterszman, A Moras, D
Citation: S. Fribourg et al., Dissecting the interaction network of multiprotein complexes by pairwise coexpression of subunits in E-coli, J MOL BIOL, 306(2), 2001, pp. 363-373
The human TFIID components TAF(II)135 and TAF(II)20 and the yeast SAGA components ADA1 and TAF(II)68 heterodimerize to form histone-like pairs
Authors: Gangloff, YG Werten, S Romier, C Carre, L Poch, O Moras, D Davidson, I
Citation: Yg. Gangloff et al., The human TFIID components TAF(II)135 and TAF(II)20 and the yeast SAGA components ADA1 and TAF(II)68 heterodimerize to form histone-like pairs, MOL CELL B, 20(1), 2000, pp. 340-351
The human transcription factor IID subunit human TATA-binding protein-associated factor 28 interacts in a ligand-reversible manner with the vitamin D-3 and thyroid hormone receptors
Authors: Mengus, G Gangloff, YG Carre, L Lavigne, AC Davidson, I
Citation: G. Mengus et al., The human transcription factor IID subunit human TATA-binding protein-associated factor 28 interacts in a ligand-reversible manner with the vitamin D-3 and thyroid hormone receptors, J BIOL CHEM, 275(14), 2000, pp. 10064-10071
Human TAF(Pi)55 interacts with the vitamin D-3 and thyroid hormone receptors and with derivatives of the retinoid X receptor that have altered transactivation properties
Authors: Lavigne, AC Mengus, G Gangloff, YG Wurtz, JM Davidson, I
Citation: Ac. Lavigne et al., Human TAF(Pi)55 interacts with the vitamin D-3 and thyroid hormone receptors and with derivatives of the retinoid X receptor that have altered transactivation properties, MOL CELL B, 19(8), 1999, pp. 5486-5494
Synergistic transcriptional activation by TATA-binding protein and hTAF(II)28 requires specific amino acids of the hTAF(II)28 histone fold
Authors: Lavigne, AC Gangloff, YG Carre, L Mengus, G Birck, C Poch, O Pomier, C Moras, D Davidson, I
Citation: Ac. Lavigne et al., Synergistic transcriptional activation by TATA-binding protein and hTAF(II)28 requires specific amino acids of the hTAF(II)28 histone fold, MOL CELL B, 19(7), 1999, pp. 5050-5060
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