Product References
Protein phosphatase 5 is a major component of glucocorticoid receptor.hsp90 complexes with properties of an FK506-binding immunophilin.
The Journal of biological chemistry
Silverstein AM,Galigniana MD,Chen MS,Owens-Grillo JK,Chinkers M,Pratt WB
MA1-2012 was used in immunoprecipitation to identify PP5 as an important component of glucocorticoid receptor-hsp90 complexes and investigate its functional properties
Fri Jun 27 00:00:00 EDT 1997
Folding of the glucocorticoid receptor by the reconstituted Hsp90-based chaperone machinery. The initial hsp90.p60.hsp70-dependent step is sufficient for creating the steroid binding conformation.
The Journal of biological chemistry
Dittmar KD,Pratt WB
MA1-2012 was used in immunoprecipitation to study the folding of hormone binding domain of glucocorticoid receptor in vitro using reconstituted receptor-hsp90 heterocomplex assembly system with purified components
Fri May 16 00:00:00 EDT 1997
Functional interference between hypoxia and dioxin signal transduction pathways: competition for recruitment of the Arnt transcription factor.
Molecular and cellular biology
Gradin K,McGuire J,Wenger RH,Kvietikova I,fhitelaw ML,Toftgård R,Tora L,Gassmann M,Poellinger L
MA1-2012 was used in immunoprecipitation to show HIF-1a is associated with the molecular chaperone hsp90 in vitro
Tue Oct 01 00:00:00 EDT 1996
A model of protein targeting mediated by immunophilins and other proteins that bind to hsp90 via tetratricopeptide repeat domains.
The Journal of biological chemistry
Owens-Grillo JK,Czar MJ,Hutchison KA,Hoffmann K,Perdew GH,Pratt WB
MA1-2012 was used in immunoprecipitation to study the mechanisms of immunophilin-mediated protein targeting
Fri Jun 07 00:00:00 EDT 1996
The basic helix-loop-helix/PAS factor Sim is associated with hsp90. Implications for regulation by interaction with partner factors.
The Journal of biological chemistry
McGuire J,Coumailleau P,Whitelaw ML,Gustafsson JA,Poellinger L
MA1-2012 was used in immunoprecipitation to study the interaction between Sim and hsp90
Fri Dec 29 00:00:00 EST 1995
Definition of a minimal domain of the dioxin receptor that is associated with Hsp90 and maintains wild type ligand binding affinity and specificity.
The Journal of biological chemistry
Coumailleau P,Poellinger L,Gustafsson JA,Whitelaw ML
MA1-2012 was used in immunoprecipitation to detect the interaction between the dioxin receptor and Hsp90
Fri Oct 20 00:00:00 EDT 1995
Identification of functional domains of the aryl hydrocarbon receptor.
The Journal of biological chemistry
Fukunaga BN,Probst MR,Reisz-Porszasz S,Hankinson O
MA1-2012 was used in immunoprecipitation to investigate the functional domains of mouse aryl hydrocarbon receptor
Fri Dec 08 00:00:00 EST 1995
A cellular factor stimulates ligand-dependent release of hsp90 from the basic helix-loop-helix dioxin receptor.
Molecular and cellular biology
McGuire J,Whitelaw ML,Pongratz I,Gustafsson JA,Poellinger L
MA1-2012 was used in immunoprecipitation to investigate the role of Arnt for release of hsp90 from the dioxin receptor in the presence of dioxin
Fri Apr 01 00:00:00 EST 1994
A tyrosine kinase-dependent pathway regulates ligand-dependent activation of the dioxin receptor in human keratinocytes.
The Journal of biological chemistry
Gradin K,Whitelaw ML,Toftgård R,Poellinger L,Berghard A
MA1-2012 was used in immunoprecipitation to investigate the role of a tyrosine kinase-dependent pathway during ligand-dependent activation of the dioxin receptor in human keratinocytes
Fri Sep 23 00:00:00 EDT 1994
Characterization of the protein-protein interactions determining the heat shock protein (hsp90.hsp70.hsp56) heterocomplex.
The Journal of biological chemistry
Czar MJ,Owens-Grillo JK,Dittmar KD,Hutchison KA,Zacharek AM,Leach KL,Deibel MR,Pratt WB
MA1-2012 was used in immunoprecipitation to investigate the interaction of different protein components of the heat shock protein heterocomplex
Fri Apr 15 00:00:00 EDT 1994