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W B Pratt

Showing results (81-90 of 132) with videos related to

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The Journal of Biological Chemistry|March 30, 2001
Evidence that the peptidylprolyl isomerase domain of the hsp90-binding immunophilin FKBP52 is involved in both dynein interaction and glucocorticoid receptor movement to the nucleusM D Galigniana, C Radanyi, J M Renoir, et al.
The Journal of Biological Chemistry|August 5, 1990
Evidence that the conserved region in the steroid binding domain of the glucocorticoid receptor is required for both optimal binding of hsp90 and protection from proteolytic cleavage. A two-site model for hsp90 binding to the steroid binding domainP R Housley, E R Sanchez, M Danielsen, et al.
The Journal of Biological Chemistry|September 5, 1988
Localization of phosphorylation sites with respect to the functional domains of the mouse L cell glucocorticoid receptorF C Dalman, E R Sanchez, A L Lin, et al.
The Journal of Biological Chemistry|November 5, 1985
The molybdate-stabilized L-cell glucocorticoid receptor isolated by affinity chromatography or with a monoclonal antibody is associated with a 90-92-kDa nonsteroid-binding phosphoproteinP R Housley, E R Sanchez, H M Westphal, et al.
The Journal of Biological Chemistry|November 25, 1983
Evidence that the endogenous heat-stable glucocorticoid receptor-activating factor is thioredoxinJ F Grippo, W Tienrungroj, M K Dahmer, et al.
The Journal of Biological Chemistry|August 22, 1997
Folding of the glucocorticoid receptor by the heat shock protein (hsp) 90-based chaperone machinery. The role of p23 is to stabilize receptor.hsp90 heterocomplexes formed by hsp90.p60.hsp70K D Dittmar, D R Demady, L F Stancato, et al.
The Journal of Biological Chemistry|April 15, 2000
Stepwise assembly of a glucocorticoid receptor.hsp90 heterocomplex resolves two sequential ATP-dependent events involving first hsp70 and then hsp90 in opening of the steroid binding pocketY Morishima, P J Murphy, D P Li, et al.
Biochemistry|February 15, 2001
Evidence for iterative ratcheting of receptor-bound hsp70 between its ATP and ADP conformations during assembly of glucocorticoid receptor.hsp90 heterocomplexesY Morishima, K C Kanelakis, P J Murphy, et al.
The Journal of Biological Chemistry|August 1, 1998
A conserved proline in the hsp90 binding region of the glucocorticoid receptor is required for hsp90 heterocomplex stabilization and receptor signalingC A Caamaño, M I Morano, F C Dalman, et al.
The Journal of Biological Chemistry|March 5, 1990
In contrast to the glucocorticoid receptor, the thyroid hormone receptor is translated in the DNA binding state and is not associated with hsp90F C Dalman, R J Koenig, G H Perdew, et al.
Pageof 14

Showing results (81-90 of 132) with videos related to

Sort By:
Pageof 14
The Journal of Biological Chemistry|March 30, 2001
Evidence that the peptidylprolyl isomerase domain of the hsp90-binding immunophilin FKBP52 is involved in both dynein interaction and glucocorticoid receptor movement to the nucleusM D Galigniana, C Radanyi, J M Renoir, et al.
The Journal of Biological Chemistry|August 5, 1990
Evidence that the conserved region in the steroid binding domain of the glucocorticoid receptor is required for both optimal binding of hsp90 and protection from proteolytic cleavage. A two-site model for hsp90 binding to the steroid binding domainP R Housley, E R Sanchez, M Danielsen, et al.
The Journal of Biological Chemistry|September 5, 1988
Localization of phosphorylation sites with respect to the functional domains of the mouse L cell glucocorticoid receptorF C Dalman, E R Sanchez, A L Lin, et al.
The Journal of Biological Chemistry|November 5, 1985
The molybdate-stabilized L-cell glucocorticoid receptor isolated by affinity chromatography or with a monoclonal antibody is associated with a 90-92-kDa nonsteroid-binding phosphoproteinP R Housley, E R Sanchez, H M Westphal, et al.
The Journal of Biological Chemistry|November 25, 1983
Evidence that the endogenous heat-stable glucocorticoid receptor-activating factor is thioredoxinJ F Grippo, W Tienrungroj, M K Dahmer, et al.
The Journal of Biological Chemistry|August 22, 1997
Folding of the glucocorticoid receptor by the heat shock protein (hsp) 90-based chaperone machinery. The role of p23 is to stabilize receptor.hsp90 heterocomplexes formed by hsp90.p60.hsp70K D Dittmar, D R Demady, L F Stancato, et al.
The Journal of Biological Chemistry|April 15, 2000
Stepwise assembly of a glucocorticoid receptor.hsp90 heterocomplex resolves two sequential ATP-dependent events involving first hsp70 and then hsp90 in opening of the steroid binding pocketY Morishima, P J Murphy, D P Li, et al.
Biochemistry|February 15, 2001
Evidence for iterative ratcheting of receptor-bound hsp70 between its ATP and ADP conformations during assembly of glucocorticoid receptor.hsp90 heterocomplexesY Morishima, K C Kanelakis, P J Murphy, et al.
The Journal of Biological Chemistry|August 1, 1998
A conserved proline in the hsp90 binding region of the glucocorticoid receptor is required for hsp90 heterocomplex stabilization and receptor signalingC A Caamaño, M I Morano, F C Dalman, et al.
The Journal of Biological Chemistry|March 5, 1990
In contrast to the glucocorticoid receptor, the thyroid hormone receptor is translated in the DNA binding state and is not associated with hsp90F C Dalman, R J Koenig, G H Perdew, et al.
Pageof 14