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Src– 1 and Hck– 1 complexes were used as references in the pull-down assay.
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This hypothesis was sustained by the myocardial histological changes observed in heart from patients suffering from SRC [1].
These were then crossed to ♂-SRC(1) and ♂-ParisC(1) sires.
We have generated "Adnectins", derived from 10th fibronectin type III domain (10Fn3), that target the PXR ligand binding domain (LBD) interactions with the steroid receptor co-activator-1 (SRC-1) peptide, displacing SRC-1 binding.
Substituting SRC-1 with Adnectin-1 does not alter the binding conformation of Compound-1 in the ligand binding pocket.
These results suggest that SRC-1 and KIN-22 play distinct roles under the control of CSK-1.
RNA interference of src-1, but not that of kin-22, caused a developmental arrest in early development.
Representative titrations for SRC-1 NR2 binding are shown in Figure S3.
These data indicate that trehalose-induced folding in AF1 facilitates AF1's interaction with SRC-1.
Immunoprecipitation was performed with antibodies against TRα1, DOR or SRC-1.
POMC and CRH seem to depend on the same coregulator molecule, namely SRC-1 [21], [21].
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