|
References for rGR aa 1 (show
notes above)
Carlstedt-Duke,
J., et al.
Domain structure of the glucocorticoid receptor
protein.
Proc. Natl. Acad. Sci. USA, 84, 4437-4440 (1987)
Eisen,
L. P., et al.
Monoclonal antibody to the rat glucocorticoid
receptor.
J. Biol. Chem., 260, 11805-11810 (1985)
References for rGR aa
16 (show
notes above)
Brandon,
D. D., et al.
Genetic variation of the glucocorticoid receptor from a
steroid-resistant primate.
J Mol Endocrinol. 1991 Oct 1; 7(2): 89-96.
Reynolds,
P. D. et al.
Database entry
References for rGR aa
24 (show
notes above)
de
Lange, P., et al.
Differential hormone-dependent transcriptional activation
and -repression by naturally occurring human glucocorticoid
receptor variants.
Mol Endocrinol 1997 Jul;11(8):1156-1164
References for rGR aa
28 (show
notes above)
Carlstedt-Duke,
J., et al.
Domain structure of the glucocorticoid receptor
protein.
Proc. Natl. Acad. Sci. USA, 84, 4437-4440 (1987)
References for rGR aa
74 (show
notes above)
Brandon,
D. D., et al.
Genetic variation of the glucocorticoid receptor from a
steroid-resistant primate.
J Mol Endocrinol. 1991 Oct 1; 7(2): 89-96.
Reynolds,
P. D. et al.
Database entry
References for rGR aa 134
(show notes
above)
Bodwell,
J. E., et al.
Identification of phosphorylated sites in the mouse
glucocorticoid receptor.
J. Biol. Chem., 266, 7549-7555 (1991)
Mason,
S. A., and Housley, P. R.
Site-directed mutagenesis of the phosphorylation sites in
the mouse glucocorticoid receptor.
J. Biol. Chem., 268, 21501-21504 (1993)
References for rGR aa
162 (show
notes above)
Bodwell,
J. E., et al.
Identification of phosphorylated sites in the mouse
glucocorticoid receptor.
J. Biol. Chem., 266, 7549-7555 (1991)
Mason,
S. A., and Housley, P. R.
Site-directed mutagenesis of the phosphorylation sites in
the mouse glucocorticoid receptor.
J. Biol. Chem., 268, 21501-21504 (1993)
References for rGR aa 171
(show notes
above)
Bodwell,
J. E., et al.
Identification of phosphorylated sites in the mouse
glucocorticoid receptor.
J. Biol. Chem., 266, 7549-7555 (1991)
Mason,
S. A., and Housley, P. R.
Site-directed mutagenesis of the phosphorylation sites in
the mouse glucocorticoid receptor.
J. Biol. Chem., 268, 21501-21504 (1993)
References for rGR aa 224
(show notes
above)
Bodwell,
J. E., et al.
Identification of phosphorylated sites in the mouse
glucocorticoid receptor.
J. Biol. Chem., 266, 7549-7555 (1991)
Mason,
S. A., and Housley, P. R.
Site-directed mutagenesis of the phosphorylation sites in
the mouse glucocorticoid receptor.
J. Biol. Chem., 268, 21501-21504 (1993)
Hu,
L.M. et al.
Glucocorticoid receptors in ATP-depleted cells.
Dephosphorylation, loss of hormone binding, HSP90
dissociation, and ATP-dependent cycling.
J. Biol. Chem. 269, 6571-7 (1994)
References for rGR aa
226 (show
notes above)
Chang,
C. et al.
Cloning and sequence analysis of the rat ventral prostate
glucocorticoid receptor cDNA
Nucleic Acids Res 1987 Nov 25;15(22):9603
References for rGR aa 232
(show notes
above)
Bodwell,
J. E., et al.
Identification of phosphorylated sites in the mouse
glucocorticoid receptor.
J. Biol. Chem., 266, 7549-7555 (1991)
Mason,
S. A., and Housley, P. R.
Site-directed mutagenesis of the phosphorylation sites in
the mouse glucocorticoid receptor.
J. Biol. Chem., 268, 21501-21504 (1993)
Hu,
L.M. et al.
Glucocorticoid receptors in ATP-depleted cells.
Dephosphorylation, loss of hormone binding, HSP90
dissociation, and ATP-dependent cycling.
J. Biol. Chem. 269, 6571-7 (1994)
References for rGR aa
234 (show notes
above)
Inguez-lluhi,
J.A., et al.
Three amino acid substitutions selectively disrupt the
activation but not the repression function of the
glucocorticoid receptor N terminus.
J Biol Chem 1997 Feb 14;272(7):4149-4156
References for rGR aa 246 (show
notes above)
Bodwell,
J. E., et al.
Identification of phosphorylated sites in the mouse
glucocorticoid receptor.
J. Biol. Chem., 266, 7549-7555 (1991)
Mason,
S. A., and Housley, P. R.
Site-directed mutagenesis of the phosphorylation sites in
the mouse glucocorticoid receptor.
J. Biol. Chem., 268, 21501-21504 (1993)
Hu,
L.M. et al.
Glucocorticoid receptors in ATP-depleted cells.
Dephosphorylation, loss of hormone binding, HSP90
dissociation, and ATP-dependent cycling.
J. Biol. Chem. 269, 6571-7 (1994)
References for rGR aa
260 (show
notes above)
Chang,
C. et al.
Cloning and sequence analysis of the rat ventral prostate
glucocorticoid receptor cDNA
Nucleic Acids Res 1987 Nov 25;15(22):9603
References for rGR aa 327
(show notes
above)
Bodwell,
J. E., et al.
Identification of phosphorylated sites in the mouse
glucocorticoid receptor.
J. Biol. Chem., 266, 7549-7555 (1991)
Mason,
S. A., and Housley, P. R.
Site-directed mutagenesis of the phosphorylation sites in
the mouse glucocorticoid receptor.
J. Biol. Chem., 268, 21501-21504 (1993)
References for rGR aa 345
(show notes
above)
Chang,
C. et al.
Cloning and sequence analysis of the rat ventral prostate
glucocorticoid receptor cDNA
Nucleic Acids Res 1987 Nov 25;15(22):9603
References for rGR aa 383
(show notes
above)
Gaitan
et al.
Glucocorticoid receptor structure and function in an
adrenocorticotropin-secreting small cell lung cancer.
Mol. Endo. 9:1193-1201(1995)).
Karl,
M., et al.
Familial glucocorticoid resistance caused by a splice
site deletion in the human glucocorticoid receptor gene.
J. Clin. Endocrinol. Metab., 76, 683-689 (1993)
References for rGR aa 409
(show notes
above)
Carlstedt-Duke,
J., et al.
Domain structure of the glucocorticoid receptor
protein.
Proc. Natl. Acad. Sci. USA, 84, 4437-4440 (1987)
Dahlman,
K., et al.
High level expression in Escherichia coli of the
DNA-binding domain of the glucocorticoid receptor in a
functional form utilizing domain-specific cleavage of a
fusion protein.
J. Biol. Chem., 264, 804-809 (1989)
References for rGR aa 413
(show notes
above)
Carlstedt-Duke,
J., et al.
Domain structure of the glucocorticoid receptor
protein.
Proc. Natl. Acad. Sci. USA, 84, 4437-4440 (1987)
Dahlman,
K., et al.
High level expression in Escherichia coli of the
DNA-binding domain of the glucocorticoid receptor in a
functional form utilizing domain-specific cleavage of a
fusion protein.
J. Biol. Chem., 264, 804-809 (1989)
References for rGR aa 435
(show notes
above)
Segard-Maurel,
I., et al.
Mutations in the "zinc fingers" or in the N-terminal
region of the DNA binding domain of the human glucocorticoid
receptor facilitate its salt- induced transformation, but do
not modify hormone binding.
J. Steroid Biochem. Molec. Biol., 41, 727-732 (1992)
References for rGR aa 439
(show notes
above)
Luisi,
B. F., et al.
Crystallographic analysis of the interaction of the
glucocorticoid receptor with DNA.
Nature, 352, 497-505 (1991)
References for rGR aa 440
(show notes
above)
Archer,
T. K., et al.
Sequence-specific DNA binding by glucocorticoid receptor
"zinc finger peptides".
Proc. Natl. Acad. Sci. USA, 87, 7560-7564 (1990)
Kellenbach,
E., et al.
Identification of the metal coordinating residues in the
DNA binding domain of the glucocorticoid receptor by
113Cd-1H heteronuclear NMR spectroscopy.
FEBS, 291, 367-370 (1991)
Luisi,
B. F., et al.
Crystallographic analysis of the interaction of the
glucocorticoid receptor with DNA.
Nature, 352, 497-505 (1991)
Powers,
J. H., et al.
Cloning and expression of mutant glucocorticoid receptors
from glucocorticoid-sensitive and resistant human leukemic
cells.
Cancer Res., 53, 4059-4065 (1993)
Ray,
A., et al.
Repressor to activator switch by mutations in the first
Zn finger of the glucocorticoid receptor: Is direct DNA
binding necessary?
Proc. Natl. Acad. Sci. USA, 88, 7086-7090 (1991)
References for rGR aa 443
(show notes
above)
Kellenbach,
E., et al.
Identification of the metal coordinating residues in the
DNA binding domain of the glucocorticoid receptor by
113Cd-1H heteronuclear NMR spectroscopy.
FEBS, 291, 367-370 (1991)
Luisi,
B. F., et al.
Crystallographic analysis of the interaction of the
glucocorticoid receptor with DNA.
Nature, (show notes above), 497-505 (1991)
References for rGR aa 444
(show notes
above)
Heck,
et al,.
A distinct modulating domain in glucocorticoid receptor
monomers in the repression of activity of the transcription
factor AP-1.
EMBO J 13, 4087-4095 (1994)
References for rGR aa 445
(show notes
above)
Guido,
et al,.
Determinants of promoter-specific activity by
glucocorticoid receptor.
Mol. Endo. 10:1178-1190 (1996)
References for rGR aa 449
(show notes
above)
Kasai,
Y.
Two naturally-occurring isoforms and their expression of
a glucocorticoid receptor gene from an androgen-dependent
mouse tumor.
FEBS Journal, 274, 99-102 (1990)
Zandi,
E., et al.
Zinc finger mutations that alter domain interactions in
the glucocorticoid receptor.
J. Mol. Biol., 230, 124-136 (1993)
References for rGR aa 450
(show notes
above)
Hollenberg,
S. M., and Evans, R. M.
Multiple and cooperative trans-activation domains of the
human glucocorticoid receptor.
Cell, 55, 899-906 (1988)
References for rGR aa 451
(show notes
above)
Zandi,
E., et al.
Zinc finger mutations that alter domain interactions in
the glucocorticoid receptor.
J. Mol. Biol., 230, 124-136 (1993)
References for rGR aa 452
(show notes
above)
Luisi,
B. F., et al.
Crystallographic analysis of the interaction of the
glucocorticoid receptor with DNA.
Nature, 352, 497-505 (1991)
References for rGR aa 455
(show notes
above)
Heck,
et al,.
A distinct modulating domain in glucocorticoid receptor
monomers in the repression of activity of the transcription
factor AP-1.
EMBO J 13, 4087-4095 (1994)
References for rGR aa 457
(show notes
above)
Kellenbach,
E., et al.
Identification of the metal coordinating residues in the
DNA binding domain of the glucocorticoid receptor by
113Cd-1H heteronuclear NMR spectroscopy.
FEBS, 291, 367-370 (1991)
Luisi,
B. F., et al.
Crystallographic analysis of the interaction of the
glucocorticoid receptor with DNA.
Nature, 352, 497-505 (1991)
References for rGR aa 458
(show notes
above)
Umesono,
K., and Evans, R. M.
Determinants of target gene specificity for
steroid/thyroid hormone receptors.
Cell, 57, 1139-1146 (1989)
Zilliacus,
J., et al.
Determinants for DNA-binding site recognition by the
glucocorticoid receptor.
J Biol Chem, 267, 24941-24947 (1992)
Zilliacus,
J. et al.
Evolution of distinct DNA-binding specificities within
the nuclear receptor family of transcription factors.
Proc Natl Acad Sci U S A 91, 4175-9 (1994)
References for rGR aa 459
(show notes
above)
Lefstin,
J.A., et al.
Influence of a steroid receptor DNA-binding domain on
transcriptional regulatory functions.
Genes and Development, 8, 2842-2856 (1994).
Zandi,
E., et al.
Zinc finger mutations that alter domain interactions in
the glucocorticoid receptor.
J. Mol. Biol., 230, 124-136 (1993)
Zilliacus,
J., et al.
Determinants for DNA-binding site recognition by the
glucocorticoid receptor.
J Biol Chem, 267, 24941-24947 (1992)
References for rGR aa 460
(show notes
above)
Kellenbach,
E., et al.
Identification of the metal coordinating residues in the
DNA binding domain of the glucocorticoid receptor by
113Cd-1H heteronuclear NMR spectroscopy.
FEBS, 291, 367-370 (1991)
Luisi,
B. F., et al.
Crystallographic analysis of the interaction of the
glucocorticoid receptor with DNA.
Nature, 352, 497-505 (1991)
References for rGR aa 461
(show notes
above)
Guido,
et al,.
Determinants of promoter-specific activity by
glucocorticoid receptor.
Mol. Endo. 10:1178-1190 (1996)
Hollenberg,
S. M., and Evans, R. M.
Multiple and cooperative trans-activation domains of the
human glucocorticoid receptor.
Cell, 55, 899-906 (1988)
Lefstin,
J.A., et al.
Influence of a steroid receptor DNA-binding domain on
transcriptional regulatory functions.
Genes and Development, 8, 2842-2856 (1994).
Lucibello,
F. C., et al.
Mutual transrepression of fos and the glucocorticoid
receptor: involvement of a functional domain in fos which is
absent in fosB.
EMBO, 9, 2827-2834 (1990)
Luisi,
B. F., et al.
Crystallographic analysis of the interaction of the
glucocorticoid receptor with DNA.
Nature, 352, 497-505 (1991)
Starr,
DB et al.
Intracellular receptors use a common mechanism to
interpret signaling information at response elements.
Genes and Develop., 10, 1271-1283(1996)
Yang-Yen,
H.-F., et al.
Transcriptional interference between c-Jun and the
glucocorticoid receptor: mutual inhibition of DNA binding
due to direct protein-protein interaction.
Cell, 62, 1205-1215 (1990)
References for rGR aa 462
(show notes
above)
Lefstin,
J.A., et al.
Influence of a steroid receptor DNA-binding domain on
transcriptional regulatory functions.
Genes and Development, 8, 2842-2856 (1994).
Luisi,
B. F., et al.
Crystallographic analysis of the interaction of the
glucocorticoid receptor with DNA.
Nature, 352, 497-505 (1991)
Zilliacus,
J., et al.
Determinants for DNA-binding site recognition by the
glucocorticoid receptor.
J Biol Chem, 267, 24941-24947 (1992)
Starr,
DB et al.
Intracellular receptors use a common mechanism to
interpret signaling information at response elements s.
Genes and Develop., 10, 1271-1283(1996)
References for rGR aa 463
(show notes
above)
Luisi,
B. F., et al.
Crystallographic analysis of the interaction of the
glucocorticoid receptor with DNA.
Nature, 352, 497-505 (1991)
References for rGR aa 464
(show notes
above)
Luisi,
B. F., et al.
Crystallographic analysis of the interaction of the
glucocorticoid receptor with DNA.
Nature, 352, 497-505 (1991)
References for rGR aa 465
(show notes
above)
Hollenberg,
S. M., and Evans, R. M.
Multiple and cooperative trans-activation domains of the
human glucocorticoid receptor.
Cell, 55, 899-906 (1988)
References for rGR aa 466
(show notes
above)
Lefstin,
J.A., et al.
Influence of a steroid receptor DNA-binding domain on
transcriptional regulatory functions.
Genes and Development, 8, 2842-2856 (1994).
Luisi,
B. F., et al.
Crystallographic analysis of the interaction of the
glucocorticoid receptor with DNA.
Nature, 352, 497-505 (1991)
Starr,
DB et al.
Intracellular receptors use a common mechanism to
interpret signaling information at response elements s.
Genes and Develop., 10, 1271-1283(1996)
References for rGR aa 468
(show notes
above)
Zandi,
E., et al.
Zinc finger mutations that alter domain interactions in
the glucocorticoid receptor.
J. Mol. Biol., 230, 124-136 (1993)
References for rGR aa 470
(show notes
above)
Kasai,
Y.
Two naturally-occurring isoforms and their expression of
a glucocorticoid receptor gene from an androgen-dependent
mouse tumor.
FEBS Journal, 274, 99-102 (1990)
Brandon,
D. D., et al.
Genetic variation of the glucocorticoid receptor from a
steroid-resistant primate.
J Mol Endocrinol. 1991 Oct 1; 7(2): 89-96.
Reynolds,
P. D. et al.
Database entryTamarin GR.
References for rGR aa 474
(show notes
above)
Hollenberg,
S. M., and Evans, R. M.
Multiple and cooperative trans-activation domains of the
human glucocorticoid receptor.
Cell, 55, 899-906 (1988)
Luisi,
B. F., et al.
Crystallographic analysis of the interaction of the
glucocorticoid receptor with DNA.
Nature, 352, 497-505 (1991)
References for rGR aa 476
(show notes
above)
Kellenbach,
E., et al.
Identification of the metal coordinating residues in the
DNA binding domain of the glucocorticoid receptor by
113Cd-1H heteronuclear NMR spectroscopy.
FEBS, 291, 367-370 (1991)
Luisi,
B. F., et al.
Crystallographic analysis of the interaction of the
glucocorticoid receptor with DNA.
Nature, 352, 497-505 (1991)
References for rGR aa 477
(show notes
above)
Heck,
et al,.
A distinct modulating domain in glucocorticoid receptor
monomers in the repression of activity of the transcription
factor AP-1. EMBO J 13, 4087-4095 (1994)
Liden,
J., et al.
A new function for the C-terminal zinc finger of the
glucocorticoid receptor. Repression of RelA
transactivation.
J Biol Chem 1997 Aug 22;272(34):21467-21472
References for rGR aa 479
(show notes
above)
Dahlman-Wright,
K., et al.
Protein-protein interactions between the DNA-binding
domains of nuclear receptors: influence on DNA-binding.
J. Steroid Biochem. Mol. Biol., 45, 239-250 (1993)
Hollenberg,
S. M., and Evans, R. M.
Multiple and cooperative trans-activation domains of the
human glucocorticoid receptor.
Cell, 55, 899-906 (1988)
Liden,
J., et al.
A new function for the C-terminal zinc finger of the
glucocorticoid receptor. Repression of RelA
transactivation.
J Biol Chem 1997 Aug 22;272(34):21467-21472
Liu,
W. , et al.
Steroid receptor transcriptional synergy is potentiated
by disruption of the DNA-binding domain dimer interface
Mol. Endo., 10,
1399-1406 (1996)
References for rGR aa 480
(show notes
above)
Lefstin,
J.A., et al.
Influence of a steroid receptor DNA-binding domain on
transcriptional regulatory functions.
Genes and Development, 8, 2842-2856 (1994).
References for rGR aa
481(show
notes above)
Dahlman-Wright,
K., et al.
Protein-protein interactions between the DNA-binding
domains of nuclear receptors: influence on DNA-binding.
J. Steroid Biochem. Mol. Biol., 45, 239-250 (1993)
Liden,
J., et al.
A new function for the C-terminal zinc finger of the
glucocorticoid receptor. Repression of RelA
transactivation.
J Biol Chem 1997 Aug 22;272(34):21467-21472
Hollenberg,
S. M., and Evans, R. M.
Multiple and cooperative trans-activation domains of the
human glucocorticoid receptor.
Cell, 55, 899-906 (1988)
Liu,
W., et al.
Steroid receptor heterodimerization demonstrated in vitro
and in vivo.
PNAS, 92, 12480-12484 (1988)
Pearce,
D and Yamamoto, K.
Mineralocorticoid and glucocorticoid receptor activities
distinguished by nonreceptor factors at a composite response
element
Science, 259, 1161 (1993).
References for rGR aa 482
(show notes
above)
Kellenbach,
E., et al.
Identification of the metal coordinating residues in the
DNA binding domain of the glucocorticoid receptor by
113Cd-1H heteronuclear NMR spectroscopy.
FEBS, 291, 367-370 (1991)
Luisi,
B. F., et al.
Crystallographic analysis of the interaction of the
glucocorticoid receptor with DNA.
Nature, 352, 497-505 (1991)
References for rGR aa 484
(show notes
above)
Lanz,
R. B., et al.
Active, interactive, and inactive steroid receptor
mutants.
Steroids, 59, 148-152 (1994)
References for rGR aa 486
(show notes
above)
Hollenberg,
S. M., and Evans, R. M.
Multiple and cooperative trans-activation domains of the
human glucocorticoid receptor.
Cell, 55, 899-906 (1988)
References for rGR aa 488
(show notes
above)
Lefstin,
J.A., et al.
Influence of a steroid receptor DNA-binding domain on
transcriptional regulatory functions.
Genes and Development, 8, 2842-2856 (1994).
Liden,
J., et al.
A new function for the C-terminal zinc finger of the
glucocorticoid receptor. Repression of RelA
transactivation.
J Biol Chem 1997 Aug 22;272(34):21467-21472
Schena,
M., et al.
Mutations in the glucocorticoid receptor zinc finger
region that distinguish interdigitated DNA binding and
transcriptional enhancement activities.
Genes and Develop., 3, 1590-1601 (1989)
References for rGR aa 489
(show notes
above)
Schena,
M., et al.
Mutations in the glucocorticoid receptor zinc finger
region that distinguish interdigitated DNA binding and
transcriptional enhancement activities.
Genes and Develop., 3, 1590-1601 (1989)
References for rGR aa 490
(show notes above)
Liden,
J., et al.
A new function for the C-terminal zinc finger of the
glucocorticoid receptor. Repression of RelA
transactivation.
J Biol Chem 1997 Aug 22;272(34):21467-21472
References for rGR aa 491 (show
notes above)
Lefstin,
J.A., et al.
Influence of a steroid receptor DNA-binding domain on
transcriptional regulatory functions.
Genes and Development, 8, 2842-2856 (1994).
Liden,
J., et al.
A new function for the C-terminal zinc finger of the
glucocorticoid receptor. Repression of RelA
transactivation.
J Biol Chem 1997 Aug 22;272(34):21467-21472
Schena,
M., et al.
Mutations in the glucocorticoid receptor zinc finger
region that distinguish interdigitated DNA binding and
transcriptional enhancement activities.
Genes and Develop., 3, 1590-1601 (1989)
Starr,
DB et al.
Intracellular receptors use a common mechanism to
interpret signaling information at response elements s.
Genes and Develop., 10, 1271-1283(1996)
References for rGR aa 492
(show notes
above)
Kellenbach,
E., et al.
Identification of the metal coordinating residues in the
DNA binding domain of the glucocorticoid receptor by
113Cd-1H heteronuclear NMR spectroscopy.
FEBS, 291, 367-370 (1991)
Luisi,
B. F., et al.
Crystallographic analysis of the interaction of the
glucocorticoid receptor with DNA.
Nature, 352, 497-505 (1991)
Zilliacus,
J., et al.
Zinc coordination scheme for the C-terminal zinc binding
site of nuclear hormone receptors.
J. Steroid Biochem. Molec. Biol., 42, 131-139 (1992a
References for rGR aa 493
(show notes
above)
Godowski, P. J., et al.
Signal transduction and transcriptional regulation by the
glucocorticoid receptor.
DNA-Protein Interactions in Transcription (UCLA
Symposium on Molecular and Cellular Biology. 95), 197-210
(1989)
Lefstin,
J.A., et al.
Influence of a steroid receptor DNA-binding domain on
transcriptional regulatory functions.
Genes and Development, 8, 2842-2856 (1994).
References for rGR aa 495
(show notes
above)
Heck,
et al,.
A distinct modulating domain in glucocorticoid receptor
monomers in the repression of activity of the transcription
factor AP-1. EMBO J 13, 4087-4095 (1994)
Kellenbach,
E., et al.
Identification of the metal coordinating residues in the
DNA binding domain of the glucocorticoid receptor by
113Cd-1H heteronuclear NMR spectroscopy.
FEBS, 291, 367-370 (1991)
Luisi,
B. F., et al.
Crystallographic analysis of the interaction of the
glucocorticoid receptor with DNA.
Nature, 352, 497-505 (1991)
Zilliacus,
J., et al.
Zinc coordination scheme for the C-terminal zinc binding
site of nuclear hormone receptors.
J. Steroid Biochem. Molec. Biol., 42, 131-139 (1992a
References for rGR aa 496
(show notes
above)
Danielsen,
M., et al.
The mouse glucocorticoid receptor: mapping of functional
domains by cloning, sequencing and expression of wild-type
and mutant receptor proteins.
EMBO J., 5, 2513-2522 (1986)
Danielsen,
M., et al.
Domains of the glucocorticoid receptor involved in
specific and nonspecific deoxyribonucleic acid binding,
hormone activation, and transcriptional enhancement.
Mol. Endo., 1, 816-822 (1987)
Heck,
et al,.
A distinct modulating domain in glucocorticoid receptor
monomers in the repression of activity of the transcription
factor AP-1. EMBO J 13, 4087-4095 (1994)
References for rGR aa 497
(show notes
above)
Heck,
et al,.
A distinct modulating domain in glucocorticoid receptor
monomers in the repression of activity of the transcription
factor AP-1. EMBO J 13, 4087-4095 (1994)
Luisi,
B. F., et al.
Crystallographic analysis of the interaction of the
glucocorticoid receptor with DNA.
Nature, 352, 497-505 (1991)
References for rGR aa 498
(show notes
above)
Heck,
et al,.
A distinct modulating domain in glucocorticoid receptor
monomers in the repression of activity of the transcription
factor AP-1. EMBO J 13, 4087-4095 (1994)
References for rGR aa 500
(show notes
above)
Schena,
M., et al.
Mutations in the glucocorticoid receptor zinc finger
region that distinguish interdigitated DNA binding and
transcriptional enhancement activities.
Genes and Develop., 3, 1590-1601 (1989)
Severne,
Y., et al.
Metal binding 'finger' structures in the glucocorticoid
receptor defined by site-directed mutagenesis.
EMBO J., 7, 2503-2508 (1988)
Ohara-Nemoto,
Y., et al.
The steroid-binding properties of recombinant
glucocorticoid receptor: A putative role for heat shock
protein hsp90.
J. Steroid Biochem. Molec. Biol., 37, 481-490 (1990)
References for rGR aa 505
(show notes
above)
Hollenberg,
S. M., and Evans, R. M.
Multiple and cooperative trans-activation domains of the
human glucocorticoid receptor.
Cell, 55, 899-906 (1988)
References for rGR aa 517
(show notes
above)
Carlstedt-Duke,
J., et al.
Domain structure of the glucocorticoid receptor
protein.
Proc. Natl. Acad. Sci. USA, 84, 4437-4440 (1987)
References for rGR Insert after 534
aa (show
notes above)
Brandon,
D. D., et al.
Genetic variation of the glucocorticoid receptor from a
steroid-resistant primate.
J. Molec. Endo., 7, 89-96 (1991)
References for rGR aa 536
(show notes
above)
Simons,
Jr., S. S., et al.
Steroid binding activity is retained in a 16-kDa fragment
of the steroid binding domain of rat glucocorticoid
receptors.
J. Biol. Chem., 264, 14493-14497 (1989)
References for rGR aa 550
(show notes
above)
Xu,
M., et al.
JBC, 271, 21430-21438 (1996)
Cadepond,
F. et al.
J. Biol. Chem. 266:5834-5841 (1991)
References for rGR aa 551
(show notes
above)
Xu,
M., et al.
JBC, 271, 21430-21438 (1996)
References for rGR aa 553
(show notes
above)
Milhon,
J. et al.,
Genetic analysis of the N-terminal end of the
glucocorticoid receptor hormone binding domain.
J. Steroid Biochem. Mol. Biol. 51, 11-9 (1994)
References for rGR aa 554
(show notes
above)
Milhon,
J. et al.,
Genetic analysis of the N-terminal end of the
glucocorticoid receptor hormone binding domain.
J. Steroid Biochem. Mol. Biol. 51, 11-9 (1994)
References for rGR aa 555
(show notes
above)
Milhon,
J. et al.,
Genetic analysis of the N-terminal end of the
glucocorticoid receptor hormone binding domain.
J. Steroid Biochem. Mol. Biol. 51, 11-9 (1994)
References for rGR aa 556
(show notes
above)
Milhon,
J. et al.,
Genetic analysis of the N-terminal end of the
glucocorticoid receptor hormone binding domain.
J. Steroid Biochem. Mol. Biol. 51, 11-9 (1994)
References for rGR aa 558
(show notes
above)
Danielsen,
M., et al.
The mouse glucocorticoid receptor: mapping of functional
domains by cloning, sequencing and expression of wild-type
and mutant receptor proteins.
EMBO J., 5, 2513-2522 (1986)
References for rGR aa 559
(show notes
above)
Byravan,
S., et al.
Two point mutations in the hormone binding domain of the
receptor that dramatically reduce its function.
Mol. Endocrinology, 5, 752-758 (1991)
References for rGR aa 560
(show notes above)
Milhon,
J. et al.,
Identification of amino acids in the tau2-region of the
mouse glucocorticoid receptor that contribute to hormone
binding and transcriptional activation.
Mol Endocrinol 1997 Nov;11(12):1795-1805
References for rGR aa 561
(show notes
above)
Milhon,
J. et al.,
Genetic analysis of the N-terminal end of the
glucocorticoid receptor hormone binding domain.
J. Steroid Biochem. Mol. Biol. 51, 11-9 (1994)
References for rGR aa 562
(show notes above)
Milhon,
J. et al.,
Identification of amino acids in the tau2-region of the
mouse glucocorticoid receptor that contribute to hormone
binding and transcriptional activation.
Mol Endocrinol 1997 Nov;11(12):1795-1805
References for rGR aa 567
(show notes above)
Milhon,
J. et al.,
Identification of amino acids in the tau2-region of the
mouse glucocorticoid receptor that contribute to hormone
binding and transcriptional activation.
Mol Endocrinol 1997 Nov;11(12):1795-1805
References for rGR aa 568
(show notes above)
Milhon,
J. et al.,
Identification of amino acids in the tau2-region of the
mouse glucocorticoid receptor that contribute to hormone
binding and transcriptional activation.
Mol Endocrinol 1997 Nov;11(12):1795-1805
Brandon,
D. D., et al.
Genetic variation of the glucocorticoid receptor from a
steroid-resistant primate.
J Mol Endocrinol. 1991 Oct 1; 7(2): 89-96.
Reynolds,
P. D. et al.
Database entry-Tamarin GR
References for rGR aa 572
(show notes above)
Milhon,
J. et al.,
Identification of amino acids in the tau2-region of the
mouse glucocorticoid receptor that contribute to hormone
binding and transcriptional activation.
Mol Endocrinol 1997 Nov;11(12):1795-1805
References for rGR aa 573
(show notes above)
Milhon,
J. et al.,
Identification of amino acids in the tau2-region of the
mouse glucocorticoid receptor that contribute to hormone
binding and transcriptional activation.
Mol Endocrinol 1997 Nov;11(12):1795-1805
References for rGR aa 577
(show notes above)
Karl et al.
Proc. Assoc. Amer. Phys., 108, 296 (1996)
References for rGR aa 581
(show notes
above)
Lee,
S. et al.
A somatic cell genetic method for identification of
untargeted mutations in the glucocorticoid receptor that
causes hormone binding deficiencies.
Molecular Endocrinology, 9, 826-837 (1995).
Garabedian,
M. J., and Yamamoto, K. R.
Genetic dissection of the signaling domain of a mammalian
steroid receptor in yeast.
Mol. Biol. Cell, 3, 1245-1257 (1992)
Wurtz,
J.-M., et al.
A canonical structure for the ligand-binding domain of
nuclear receptors.
Nature Structural Biol., 3, 87-94 (1996)
References for rGR aa 582
(show notes
above)
Wurtz,
J.-M., et al.
A canonical structure for the ligand-binding domain of
nuclear receptors.
Nature Structural Biol., 3, 87-94 (1996)
References for rGR aa 583
(show notes
above)
Carlstedt-Duke,
J., et al.
Domain structure of the glucocorticoid receptor
protein.
Proc. Natl. Acad. Sci. USA, 84, 4437-4440 (1987)
Warriar,
N, et al.
Hormone binding domain of human glucocorticoid receptor.
Enhancement of transactivation function by substitution
mutants M565R and A573Q.
J Biol Chem 269, 29010-29015 (1994).
References for rGR aa 584
(show notes
above)
Garabedian,
M. J., and Yamamoto, K. R.
Genetic dissection of the signaling domain of a mammalian
steroid receptor in yeast.
Mol. Biol. Cell, 3, 1245-1257 (1992)
Wurtz,
J.-M., et al.
A canonical structure for the ligand-binding domain of
nuclear receptors.
Nature Structural Biol., 3, 87-94 (1996)
References for rGR aa 585
(show notes
above)
Benhamou,
B, et al.
A single amino acid that determines the sensitivity of
progesterone receptors to RU486.
Science, 255, 206-209 (1992).
Warriar,
N, et al.
Hormone binding domain of human glucocorticoid receptor.
Enhancement of transactivation function by substitution
mutants M565R and A573Q.
J Biol Chem 269, 29010-29015 (1994).
Wurtz,
J.-M., et al.
A canonical structure for the ligand-binding domain of
nuclear receptors.
Nature Structural Biol., 3, 87-94 (1996)
References for rGR aa 588
(show notes
above)
Wurtz,
J.-M., et al.
A canonical structure for the ligand-binding domain of
nuclear receptors.
Nature Structural Biol., 3, 87-94 (1996)
References for rGR aa 591
(show notes above)
Warriar,
N, et al.
Hormone binding domain of human glucocorticoid receptor.
Enhancement of transactivation function by substitution
mutants M565R and A573Q.
J Biol Chem 269, 29010-29015 (1994).
References for rGR aa 618
(show notes
above)
Wurtz,
J.-M., et al.
A canonical structure for the ligand-binding domain of
nuclear receptors.
Nature Structural Biol., 3, 87-94 (1996)
References for rGR aa 620
(show notes
above)
Garabedian,
M. J., and Yamamoto, K. R.
Genetic dissection of the signaling domain of a mammalian
steroid receptor in yeast.
Mol. Biol. Cell, 3, 1245-1257 (1992)
References for rGR aa 622
(show notes
above)
Carlstedt-Duke,
J., et al.
Domain structure of the glucocorticoid receptor
protein.
Proc. Natl. Acad. Sci. USA, 84, 4437-4440 (1987)
Carlstedt-Duke,
J., et al.
Identification of hormone-interacting amino acid residues
within the steroid-binding domain of the glucocorticoid
receptor in relation to other steroid hormone receptors.
J. Biol. Chem., 263, 6842-6846 (1988)
Garabedian,
M. J., and Yamamoto, K. R.
Genetic dissection of the signaling domain of a mammalian
steroid receptor in yeast.
Mol. Biol. Cell, 3, 1245-1257 (1992)
Stromstedt,
P.-E., et al.
Radiosequence analysis of the human progestin receptor
charged with [3H]promegestone. A comparison with the
glucocorticoid receptor.
J. Biol. Chem., 265, 12973-12977 (1990)
Wurtz,
J.-M., et al.
A canonical structure for the ligand-binding domain of
nuclear receptors.
Nature Structural Biol., 3, 87-94 (1996)
References for rGR aa 626
(show notes
above)
Wurtz,
J.-M., et al.
A canonical structure for the ligand-binding domain of
nuclear receptors.
Nature Structural Biol., 3, 87-94 (1996)
References for rGR aa 629
(show notes
above)
Wurtz,
J.-M., et al.
A canonical structure for the ligand-binding domain of
nuclear receptors.
Nature Structural Biol., 3, 87-94 (1996)
References for rGR aa 634
(show notes
above)
Brandon,
D. D., et al.
Genetic variation of the glucocorticoid receptor from a
steroid-resistant primate.
J. Molec. Endo., 7, 89-96 (1991)
References for rGR aa 636
(show notes
above)
Brandon,
D. D., et al.
Genetic variation of the glucocorticoid receptor from a
steroid-resistant primate.
J. Molec. Endo., 7, 89-96 (1991)
References for rGR aa 640
(show notes
above)
Chakraborti,
P. K., et al.
Creation of "super" glucocorticoid receptors by point
mutations in the steroid binding domain.
J. Biol. Chem., 266, 22075-22078 (1991)
Chakraborti,
P. K., et al.
Role of cysteines 640, 656, and 661 in steroid binding to
rat glucocorticoid receptors.
J. Biol. Chem., 267, 11366-11373 (1992)
Chen,
D., and Stallcup, M. R.
The hormone-binding role of 2 cysteines near the C
terminus of the mouse glucocorticoid receptor.
J. Biol. Chem., 269, 7914-7918 (1994)
Ohara-Nemoto,
Y., et al.
The steroid-binding properties of recombinant
glucocorticoid receptor: A putative role for heat shock
protein hsp90.
J. Steroid Biochem. Molec. Biol., 37, 481-490 (1990)
Wurtz,
J.-M., et al.
A canonical structure for the ligand-binding domain of
nuclear receptors.
Nature Structural Biol., 3, 87-94 (1996)
References for rGR aa 641
(show notes
above)
Wurtz,
J.-M., et al.
A canonical structure for the ligand-binding domain of
nuclear receptors.
Nature Structural Biol., 3, 87-94 (1996)
References for rGR aa 656
(show notes
above)
Carlstedt-Duke,
J., et al.
Identification of hormone-interacting amino acid residues
within the steroid-binding domain of the glucocorticoid
receptor in relation to other steroid hormone receptors.
J. Biol. Chem., 263, 6842-6846 (1988)
Chakraborti,
P. K., et al.
Creation of "super" glucocorticoid receptors by point
mutations in the steroid binding domain.
J. Biol. Chem., 266, 22075-22078 (1991)
Chakraborti,
P. K., et al.
Role of cysteines 640, 656, and 661 in steroid binding to
rat glucocorticoid receptors.
J. Biol. Chem., 267, 11366-11373 (1992)
Chen,
D., and Stallcup, M. R.
The hormone-binding role of 2 cysteines near the C
terminus of the mouse glucocorticoid receptor.
J. Biol. Chem., 269, 7914-7918 (1994)
Garabedian,
M. J., and Yamamoto, K. R.
Genetic dissection of the signaling domain of a mammalian
steroid receptor in yeast.
Mol. Biol. Cell, 3, 1245-1257 (1992)
Hurley,
D. M., et al.
Point mutation causing a single amino acid substitution
in the hormone binding domain of the glucocorticoid receptor
in familial glucocorticoid resistance.
J. Clin. Invest., 87, 680-686 (1991)
Keightley,
M.-C., and Fuller, P. J.
Unique sequences in the guinea pig glucocorticoid
receptor induce constitutive transactivation and decrease
steroid sensitivity.
Mol. Endo., 8, 431-439 (1994)
Lopez,
S., et al.
Structurally based, selective interaction of arsenite
with steroid receptors.
J. Biol. Chem., 265, 16039-16042 (1990)
Simons,
Jr., S. S., et al.
Identification of cysteine-656 as the amino acid of HTC
cell glucocorticoid receptors that is covalently labeled by
dexamethasone 21-mesylate.
J. Biol. Chem., 262, 9676-9680 (1987)
Stromstedt,
P.-E., et al.
Radiosequence analysis of the human progestin receptor
charged with [3H]promegestone. A comparison with the
glucocorticoid receptor.
J. Biol. Chem., 265, 12973-12977 (1990)
Wurtz,
J.-M., et al.
A canonical structure for the ligand-binding domain of
nuclear receptors.
Nature Structural Biol., 3, 87-94 (1996)
References for rGR aa 657
(show notes
above)
Wurtz,
J.-M., et al.
A canonical structure for the ligand-binding domain of
nuclear receptors.
Nature Structural Biol., 3, 87-94 (1996)
References for rGR aa 659
(show notes
above)
de
Lange, P., et al.
Differential hormone-dependent transcriptional activation
and -repression by naturally occurring human glucocorticoid
receptor variants.
Mol Endocrinol 1997 Jul;11(8):1156-1164
Garabedian,
M. J., and Yamamoto, K. R.
Genetic dissection of the signaling domain of a mammalian
steroid receptor in yeast.
Mol. Biol. Cell, 3, 1245-1257 (1992)
References for rGR aa 661
(show notes
above)
Chakraborti,
P. K., et al.
Creation of "super" glucocorticoid receptors by point
mutations in the steroid binding domain.
J. Biol. Chem., 266, 22075-22078 (1991)
Chakraborti,
P. K., et al.
Role of cysteines 640, 656, and 661 in steroid binding to
rat glucocorticoid receptors.
J. Biol. Chem., 267, 11366-11373 (1992)
Chen,
D., and Stallcup, M. R.
The hormone-binding role of 2 cysteines near the C
terminus of the mouse glucocorticoid receptor.
J. Biol. Chem., 269, 7914-7918 (1994)
Garabedian,
M. J., and Yamamoto, K. R.
Genetic dissection of the signaling domain of a mammalian
steroid receptor in yeast.
Mol. Biol. Cell, 3, 1245-1257 (1992)
Lopez,
S., et al.
Structurally based, selective interaction of arsenite
with steroid receptors.
J. Biol. Chem., 265, 16039-16042 (1990)
Ohara-Nemoto,
Y., et al.
The steroid-binding properties of recombinant
glucocorticoid receptor: A putative role for heat shock
protein hsp90.
J. Steroid Biochem. Molec. Biol., 37, 481-490 (1990)
Yu
et al.
Cysteines 638 and 665 in the hormone binding domain of
the human glucocorticoid receptor define the specificity to
glucocorticoids.
Biochemistry, 43, 14163-14173 (1995).
References for rGR aa 664
(show notes
above)
Carlstedt-Duke,
J., et al.
Domain structure of the glucocorticoid receptor
protein.
Proc. Natl. Acad. Sci. USA, 84, 4437-4440 (1987)
References for rGR aa 671
(show notes
above)
Garabedian,
M. J., and Yamamoto, K. R.
Genetic dissection of the signaling domain of a mammalian
steroid receptor in yeast.
Mol. Biol. Cell, 3, 1245-1257 (1992)
References for rGR aa 673
(show notes
above)
Simons,
Jr., S. S., et al.
Steroid binding activity is retained in a 16-kDa fragment
of the steroid binding domain of rat glucocorticoid
receptors.
J. Biol. Chem., 264, 14493-14497 (1989)
References for rGR aa 682
(show notes
above)
Lee,
S. et al.
A somatic cell genetic method for identification of
untargeted mutations in the glucocorticoid receptor that
causes hormone binding deficiencies.
Molecular Endocrinology, 9, 826-837
(1995).
References for rGR aa 683 (show
notes above)
Chen,
D., and Stallcup, M. R.
The hormone-binding role of 2 cysteines near the C
terminus of the mouse glucocorticoid receptor.
J. Biol. Chem., 269, 7914-7918 (1994)
Ohara-Nemoto,
Y., et al.
The steroid-binding properties of recombinant
glucocorticoid receptor: A putative role for heat shock
protein hsp90.
J. Steroid Biochem. Molec. Biol., 37, 481-490 (1990)
Yu
et al.
Cysteines 638 and 665 in the hormone binding domain of
the human glucocorticoid receptor define the specificity to
glucocorticoids.
Biochemistry, 43, 14163-14173 (1995).
References for rGR aa 684
(show notes
above)
Carlstedt-Duke,
J., et al.
Domain structure of the glucocorticoid receptor
protein.
Proc. Natl. Acad. Sci. USA, 84, 4437-4440 (1987)
Yu
et al.
Cysteines 638 and 665 in the hormone binding domain of
the human glucocorticoid receptor define the specificity to
glucocorticoids.
Biochemistry, 43, 14163-14173 (1995).
References for rGR aa 706
(show notes
above)
Garabedian,
M. J., and Yamamoto, K. R.
Genetic dissection of the signaling domain of a mammalian
steroid receptor in yeast.
Mol. Biol. Cell, 3, 1245-1257 (1992)
References for rGR aa 715
(show notes
above)
Garabedian,
M. J., and Yamamoto, K. R.
Genetic dissection of the signaling domain of a mammalian
steroid receptor in yeast.
Mol. Biol. Cell, 3, 1245-1257 (1992)
References for rGR aa 747
(show notes
above)
Malchoff,
D. M., et al.
A mutation of the glucocorticoid receptor in primary
cortisol resistance.
J. Clin. Invest., 91, 1918-1925 (1993)
References for rGR aa 747
(show notes
above)
Byravan,
S., et al.
Two point mutations in the hormone binding domain of the
receptor that dramatically reduce its function.
Mol. Endocrinology, 5, 752-758 (1991)
Carlstedt-Duke,
J., et al.
Identification of hormone-interacting amino acid residues
within the steroid-binding domain of the glucocorticoid
receptor in relation to other steroid hormone receptors.
J. Biol. Chem., 263, 6842-6846 (1988)
Chen,
D., and Stallcup, M. R.
The hormone-binding role of 2 cysteines near the C
terminus of the mouse glucocorticoid receptor.
J. Biol. Chem., 269, 7914-7918 (1994)
de
Lange, P., et al.
Differential hormone-dependent transcriptional activation
and -repression by naturally occurring human glucocorticoid
receptor variants.
Mol Endocrinol 1997 Jul;11(8):1156-1164
Ohara-Nemoto,
Y., et al.
The steroid-binding properties of recombinant
glucocorticoid receptor: A putative role for heat shock
protein hsp90.
J. Steroid Biochem. Molec. Biol., 37, 481-490 (1990)
Stromstedt,
P.-E., et al.
Radiosequence analysis of the human progestin receptor
charged with [3H]promegestone. A comparison with the
glucocorticoid receptor.
J. Biol. Chem., 265, 12973-12977 (1990)
Wurtz,
J.-M., et al.
A canonical structure for the ligand-binding domain of
nuclear receptors.
Nature Structural Biol., 3, 87-94 (1996)
References for rGR aa 754
(show notes above)
Lind,
U., et al.
Identification of single amino acid substitutions of
Cys-736 that affect the steroid-binding affinity and
specificity of the glucocorticoid receptor using phenotypic
screening in yeast.
Mol Endocrinol 1996 Nov;10(11):1358-1370
References for rGR aa 757
(show notes
above)
Wurtz,
J.-M., et al.
A canonical structure for the ligand-binding domain of
nuclear receptors.
Nature Structural Biol., 3, 87-94 (1996)
References for rGR aa 761
(show notes
above)
Wurtz,
J.-M., et al.
A canonical structure for the ligand-binding domain of
nuclear receptors.
Nature Structural Biol., 3, 87-94 (1996)
References for rGR aa 762
(show notes
above)
Garabedian,
M. J., and Yamamoto, K. R.
Genetic dissection of the signaling domain of a mammalian
steroid receptor in yeast.
Mol. Biol. Cell, 3, 1245-1257 (1992)
References for rGR aa 765
(show notes
above)
Roux, S. et al
Mutation of isoleucine 747 by a threonine alters the
ligand responsiveness of the human glucocorticoid
receptor
Mol. Endo. 10, 1214-1226(1996)
References for rGR aa 767
(show notes
above)
Wurtz,
J.-M., et al.
A canonical structure for the ligand-binding domain of
nuclear receptors.
Nature Structural Biol., 3, 87-94 (1996)
References for rGR aa 770
(show notes
above)
Carlstedt-Duke,
J., et al.
Domain structure of the glucocorticoid receptor
protein.
Proc. Natl. Acad. Sci. USA, 84, 4437-4440 (1987)
Danielian,
P. S., et al.
Identification of a conserved region required for hormone
dependent transcriptional activation by steroid hormone
receptors.
EMBO J., 11, 1025-1033 (1992)
Lanz,
R. B., and Rusconi, S.
A conserved carboxy-terminal subdomain is important for
ligand interpretation and transactivation by nuclear
receptors.
Endocrinology, 135, 2183-2194 (1994)
Lanz,
R. B., et al.
Active, interactive, and inactive steroid receptor
mutants.
Steroids, 59, 148-152 (1994)
Schmitt,
J., and Stunnenberg, H. G.
The glucocorticoid receptor hormone binding domain
mediates transcriptional activation in vitro in the absence
of ligand.
Nucleic Acids Res., 21, 2673-2681 (1993)
References for rGR aa 771
(show notes
above)
Ashraf,
J., and Thompson, E. B.
Identification of the activation-labile gene: a single
point mutation in the human glucocorticoid receptor presents
as two distinct receptor phenotypes.
Mol. Endocrinol., 7, 631-642 (1993)
Danielian,
P. S., et al.
Identification of a conserved region required for hormone
dependent transcriptional activation by steroid hormone
receptors.
EMBO J., 11, 1025-1033 (1992)
Lanz,
R. B., and Rusconi, S.
A conserved carboxy-terminal subdomain is important for
ligand interpretation and transactivation by nuclear
receptors.
Endocrinology, 135, 2183-2194 (1994)
Lanz,
R. B., et al.
Active, interactive, and inactive steroid receptor
mutants.
Steroids, 59, 148-152 (1994)
Powers,
J. H., et al.
Cloning and expression of mutant glucocorticoid receptors
from glucocorticoid-sensitive and resistant human leukemic
cells.
Cancer Res., 53, 4059-4065 (1993)
Schmitt,
J., and Stunnenberg, H. G.
The glucocorticoid receptor hormone binding domain
mediates transcriptional activation in vitro in the absence
of ligand.
Nucleic Acids Res., 21, 2673-2681 (1993)
Wurtz,
J.-M., et al.
A canonical structure for the ligand-binding domain of
nuclear receptors.
Nature Structural Biol., 3, 87-94 (1996)
References for rGR aa 773
(show notes
above)
Danielian,
P. S., et al.
Identification of a conserved region required for hormone
dependent transcriptional activation by steroid hormone
receptors.
EMBO J., 11, 1025-1033 (1992)
References for rGR aa 774
(show notes
above)
Danielian,
P. S., et al.
Identification of a conserved region required for hormone
dependent transcriptional activation by steroid hormone
receptors.
EMBO J., 11, 1025-1033 (1992)
Lanz,
R. B., and Rusconi, S.
A conserved carboxy-terminal subdomain is important for
ligand interpretation and transactivation by nuclear
receptors.
Endocrinology, 135, 2183-2194 (1994)
Lanz,
R. B., et al.
Active, interactive, and inactive steroid receptor
mutants.
Steroids, 59, 148-152 (1994)
References for rGR aa 775
(show notes
above)
Danielian,
P. S., et al.
Identification of a conserved region required for hormone
dependent transcriptional activation by steroid hormone
receptors.
EMBO J., 11, 1025-1033 (1992)
Lanz,
R. B., and Rusconi, S.
A conserved carboxy-terminal subdomain is important for
ligand interpretation and transactivation by nuclear
receptors.
Endocrinology, 135, 2183-2194 (1994)
Lanz,
R. B., et al.
Active, interactive, and inactive steroid receptor
mutants.
Steroids, 59, 148-152 (1994)
Wurtz,
J.-M., et al.
A canonical structure for the ligand-binding domain of
nuclear receptors.
Nature Structural Biol., 3, 87-94 (1996)
References for rGR aa 779
(show notes
above)
Brandon,
D. D., et al.
Genetic variation of the glucocorticoid receptor from a
steroid-resistant primate.
J Mol Endocrinol. 1991 Oct 1; 7(2): 89-96.
Reynolds,
P. D. et al.
Database entry
References for rGR aa 780
(show notes
above)
Lanz,
R. B., and Rusconi, S.
A conserved carboxy-terminal subdomain is important for
ligand interpretation and transactivation by nuclear
receptors.
Endocrinology, 135, 2183-2194 (1994)
References for rGR aa 781
(show notes
above)
Lanz,
R. B., and Rusconi, S.
A conserved carboxy-terminal subdomain is important for
ligand interpretation and transactivation by nuclear
receptors.
Endocrinology, 135, 2183-2194 (1994)
References for rGR aa 782
(show notes
above)
Danielsen,
M., et al.
The mouse glucocorticoid receptor: mapping of functional
domains by cloning, sequencing and expression of wild-type
and mutant receptor proteins.
EMBO J., 5, 2513-2522 (1986)
Zhang, S., et al.
Role of the C terminus of the glucocorticoid receptor in
hormone binding and agonist/antagonist discrimination..
Mol. Endocrinology, 10, 24-34 (1996)
References for rGR aa 788
(show notes
above)
Brandon,
D. D., et al.
Genetic variation of the glucocorticoid receptor from a
steroid-resistant primate.
J. Molec. Endo., 7, 89-96 (1991)
References for rGR aa 792
(show notes
above)
Chen,
D. et al.
Phenylalanine-780 near the C-terminus of the mouse
glucocorticoid receptor is important for ligand binding
affinity and specificity.
Molecular Endocrinology, 8, 422-430 (1994).
References for rGR aa 793
(show notes
above)
Chen,
D. et al.
Phenylalanine-780 near the C-terminus of the mouse
glucocorticoid receptor is important for ligand binding
affinity and specificity.
Molecular Endocrinology, 8, 422-430 (1994).
References for rGR aa 794
(show notes
above)
Zhang, S., et al.
Role of the C terminus of the glucocorticoid receptor in
hormone binding and agonist/antagonist discrimination..
Mol. Endocrinology, 10, 24-34 (1996)
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