-
1
-
-
0028283503
-
Molecular mechanisms of action of steroid/thyroid receptor superfamily members
-
Tsai M. J., O'Malley B. W. Molecular mechanisms of action of steroid/thyroid receptor superfamily members. Annu. Rev. Biochem. 63:1994;451-486.
-
(1994)
Annu. Rev. Biochem.
, vol.63
, pp. 451-486
-
-
Tsai, M.J.1
O'Malley, B.W.2
-
2
-
-
0029618368
-
Steroid hormone receptors: Many actors in search of a plot
-
Beato M., Herrlich P., Schutz G. Steroid hormone receptors: Many actors in search of a plot. Cell. 83:1995;851-857.
-
(1995)
Cell
, vol.83
, pp. 851-857
-
-
Beato, M.1
Herrlich, P.2
Schutz, G.3
-
3
-
-
0023663885
-
Functional domains of the human estrogen receptor
-
Kumar V., Green S., Stack G., Berry M., Jin J. R., Chambon P. Functional domains of the human estrogen receptor. Cell. 51:1987;941-951.
-
(1987)
Cell
, vol.51
, pp. 941-951
-
-
Kumar, V.1
Green, S.2
Stack, G.3
Berry, M.4
Jin, J.R.5
Chambon, P.6
-
4
-
-
0343285244
-
Transcriptional activity of the estrogen receptor requires a conformational change in the ligand binding domain
-
Beekman J. M., Allan G. F., Tsai S. Y., Tsai M.-J., O'Malley B. W. Transcriptional activity of the estrogen receptor requires a conformational change in the ligand binding domain. Mol. Endocrinol. 71:1993;266-274.
-
(1993)
Mol. Endocrinol.
, vol.71
, pp. 266-274
-
-
Beekman, J.M.1
Allan, G.F.2
Tsai, S.Y.3
Tsai, M.-J.4
O'Malley, B.W.5
-
5
-
-
0026703387
-
A ligand-induced conformational change in the estrogen receptor is localized in the steroid binding domain
-
Fritsch M., Leary C. M., Furlow D., Ahrens H., Schuh T. J., Mueller G. C., Gorski J. A ligand-induced conformational change in the estrogen receptor is localized in the steroid binding domain. Biochemistry. 31:1992;5303-5311.
-
(1992)
Biochemistry
, vol.31
, pp. 5303-5311
-
-
Fritsch, M.1
Leary, C.M.2
Furlow, D.3
Ahrens, H.4
Schuh, T.J.5
Mueller, G.C.6
Gorski, J.7
-
6
-
-
0031833450
-
The nuclear receptor ligand-binding domain: Structure and function
-
Moras D., Gronemeyer H. The nuclear receptor ligand-binding domain: Structure and function. Curr. Opin. Cell Biol. 10:1998;384-391.
-
(1998)
Curr. Opin. Cell Biol.
, vol.10
, pp. 384-391
-
-
Moras, D.1
Gronemeyer, H.2
-
7
-
-
0025062215
-
Role of the two activating domains of the estrogen receptor in cell-type and promoter context dependent antagonistic activity of the anti-estrogen 4-hydroxytamoxifen
-
Berry M., Metzger D., Chambon P. Role of the two activating domains of the estrogen receptor in cell-type and promoter context dependent antagonistic activity of the anti-estrogen 4-hydroxytamoxifen. EMBO J. 9:1990;2811-2818.
-
(1990)
EMBO J.
, vol.9
, pp. 2811-2818
-
-
Berry, M.1
Metzger, D.2
Chambon, P.3
-
8
-
-
0030734795
-
Altered ligand binding properties and enhanced stability of a constitutively active estrogen receptor: Evidence that an open pocket conformation is required for ligand interaction
-
Carlson K. E., Choi I., Gee A., Katzenellenbogen B. S., Katzenellenbogen J. A. Altered ligand binding properties and enhanced stability of a constitutively active estrogen receptor: Evidence that an open pocket conformation is required for ligand interaction. Biochemistry. 36:1997;14897-14905.
-
(1997)
Biochemistry
, vol.36
, pp. 14897-14905
-
-
Carlson, K.E.1
Choi, I.2
Gee, A.3
Katzenellenbogen, B.S.4
Katzenellenbogen, J.A.5
-
9
-
-
0029012163
-
Crystal structure of the ligand-binding domain of the human nuclear RXR-alpha
-
Bourguet W., Ruff M., Chambon P., Gronemeyer H., Moras D. Crystal structure of the ligand-binding domain of the human nuclear RXR-alpha. Nature. 375:1995;377-382.
-
(1995)
Nature
, vol.375
, pp. 377-382
-
-
Bourguet, W.1
Ruff, M.2
Chambon, P.3
Gronemeyer, H.4
Moras, D.5
-
10
-
-
0029643769
-
A structural role for hormone in the thyroid hormone receptor
-
Wagner R. L., Apriletti J. W., McGrath M. E., West B. L., Baxter J. D., Fletterick R. J. A structural role for hormone in the thyroid hormone receptor. Nature. 378:1995;690-697.
-
(1995)
Nature
, vol.378
, pp. 690-697
-
-
Wagner, R.L.1
Apriletti, J.W.2
McGrath, M.E.3
West, B.L.4
Baxter, J.D.5
Fletterick, R.J.6
-
11
-
-
0029643780
-
Crystal structure of the RAR-gamma ligand-binding domain bound to all-trans retinoic acid
-
Renaud J. P., Rochel N., Ruff M., Vivat V., Chambone P., Gronemeyer H., Moras D. Crystal structure of the RAR-gamma ligand-binding domain bound to all-trans retinoic acid. Nature. 378:1995;681-689.
-
(1995)
Nature
, vol.378
, pp. 681-689
-
-
Renaud, J.P.1
Rochel, N.2
Ruff, M.3
Vivat, V.4
Chambone, P.5
Gronemeyer, H.6
Moras, D.7
-
12
-
-
0030667676
-
Molecular basis of agonism and antagonism in the estrogen receptor
-
Brzozowski A. M., Pike A. C. W., Dauter Z., Hubbard R. E., Bonn T., Engstrom O., Ohman L., Greene G. L., Gustafsson J., Carlquist M. Molecular basis of agonism and antagonism in the estrogen receptor. Nature. 389:1997;753-757.
-
(1997)
Nature
, vol.389
, pp. 753-757
-
-
Brzozowski, A.M.1
Pike, A.C.W.2
Dauter, Z.3
Hubbard, R.E.4
Bonn, T.5
Engstrom, O.6
Ohman, L.7
Greene, G.L.8
Gustafsson, J.9
Carlquist, M.10
-
13
-
-
0032446607
-
The structural basis of estrogen receptor/coactivator recognition and the antagonism of the interaction by tamoxifen
-
Shiau A. K., Barstad D., Loria P. M., Cheng L. Kushner, P. J. Agard, D. A., Greene G. L. The structural basis of estrogen receptor/coactivator recognition and the antagonism of the interaction by tamoxifen. Cell. 95:1998;927-937.
-
(1998)
Cell
, vol.95
, pp. 927-937
-
-
Shiau, A.K.1
Barstad, D.2
Loria, P.M.3
Cheng, L.K.4
P., J.A.5
D., A.6
Greene, G.L.7
-
14
-
-
0032568527
-
Crystallographic comparison of the estrogen and progesterone receptor's ligand binding domains
-
Tanenbaum D. M., Wang Y., Williams S. P., Sigler P. B. Crystallographic comparison of the estrogen and progesterone receptor's ligand binding domains. Proc. Natl. Acad. Sci. USA. 95:1998;5998-6003.
-
(1998)
Proc. Natl. Acad. Sci. USA
, vol.95
, pp. 5998-6003
-
-
Tanenbaum, D.M.1
Wang, Y.2
Williams, S.P.3
Sigler, P.B.4
-
15
-
-
0342415628
-
19F NMR studies of fluorinated sugars binding to the glucose and galactose receptor protein
-
19F NMR studies of fluorinated sugars binding to the glucose and galactose receptor protein. Tech. Protein Chem. 6:1995;487-494.
-
(1995)
Tech. Protein Chem.
, vol.6
, pp. 487-494
-
-
Luck, L.A.1
-
17
-
-
18844480180
-
Structural and functional characterization of recombinant human cellular retinaldehyde-binding protein
-
Crabb J. W., Carlson A., Chen Y., Goldflam S. Intres, R. West, K. A. Hulmes, J. D. Kapron, J. T. Luck, L. A. Horwitz, J., Bok D. Structural and functional characterization of recombinant human cellular retinaldehyde-binding protein. Protein Sci. 7:1998;746-757.
-
(1998)
Protein Sci.
, vol.7
, pp. 746-757
-
-
Crabb, J.W.1
Carlson, A.2
Chen, Y.3
Goldflam, S.I.4
R. West5
K.A. Hulmes6
J. D. Kapron7
J.T. Luck8
L.A. Horwitz9
Bok, D.10
-
19
-
-
0002391667
-
19F NMR study of the binding of fluorinated diethylstilbestrol to the human estrogen receptor
-
19F NMR study of the binding of fluorinated diethylstilbestrol to the human estrogen receptor. Protein Peptide Lett. 6:1999;149-152.
-
(1999)
Protein Peptide Lett.
, vol.6
, pp. 149-152
-
-
Skeels, M.C.1
Sondi, B.S.2
Luck, L.A.3
-
21
-
-
0014273838
-
Mutants of Escherichia coli with an altered trptophanyl-transfer ribonucleic acid synthetase
-
Doolittle W. F., Yanofsky C. Mutants of Escherichia coli with an altered trptophanyl-transfer ribonucleic acid synthetase. J. Bacteriol. 95:1968;1283-1294.
-
(1968)
J. Bacteriol.
, vol.95
, pp. 1283-1294
-
-
Doolittle, W.F.1
Yanofsky, C.2
-
22
-
-
0025922013
-
19F NMR Studies of the d-galactose chemosensory receptor. 1. Sugar binding yields a global structural change
-
19F NMR Studies of the d-galactose chemosensory receptor. 1. Sugar binding yields a global structural change. Biochemistry. 30:1991;4248-4252.
-
(1991)
Biochemistry
, vol.30
, pp. 4248-4252
-
-
Luck, L.A.F.1
-
23
-
-
84969001783
-
The attractions of proteins for small molecules and ions
-
Scatchard G. The attractions of proteins for small molecules and ions. Ann. NY Acad. Sci. 51:1949;660-672.
-
(1949)
Ann. NY Acad. Sci.
, vol.51
, pp. 660-672
-
-
Scatchard, G.1
-
24
-
-
0028036401
-
The interaction of the human estrogen receptor with DNA is modulated by receptor-associated proteins
-
Landel C., Kushner P., Greene G. The interaction of the human estrogen receptor with DNA is modulated by receptor-associated proteins. Mol. Endocrinol. 8:1994;1407-1419.
-
(1994)
Mol. Endocrinol.
, vol.8
, pp. 1407-1419
-
-
Landel, C.1
Kushner, P.2
Greene, G.3
-
25
-
-
0028862855
-
Analysis of the structural core of the human estrogen receptor ligand binding domain by proteolysis/mass spectrometric analysis
-
Seielstad D. A., Carlson K. E., Kushner P. J., Greene G. L., Katzenellenbogen J. A. Analysis of the structural core of the human estrogen receptor ligand binding domain by proteolysis/mass spectrometric analysis. Biochemistry. 34:1995;12605-12615.
-
(1995)
Biochemistry
, vol.34
, pp. 12605-12615
-
-
Seielstad, D.A.1
Carlson, K.E.2
Kushner, P.J.3
Greene, G.L.4
Katzenellenbogen, J.A.5
-
26
-
-
0022555889
-
Observation of internal motility of proteins by nuclear magnetic resonance
-
Wagner G., Wuthrich K. Observation of internal motility of proteins by nuclear magnetic resonance. Methods Enzymol. 131:1986;307-326.
-
(1986)
Methods Enzymol.
, vol.131
, pp. 307-326
-
-
Wagner, G.1
Wuthrich, K.2
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