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In addition to central functions in cell adhesion signalling, integrin-associated proteins have wider roles at sites distal to adhesion receptors. In experimentally defined adhesomes, we noticed that there is clear enrichment of proteins that localise to the nucleus, and conversely, we now report th...
ORGANISM(S): Mus musculus (Mouse) 
2022-06-01 | PXD025868 | Pride
Identifying the effect of the co-regulator Hic-5 (TGFB1I1) on global androgen receptor transcriptional activity in PShTert-AR prostate fibroblast cells with view to further elucidating the broader biological role of Hic-5 on fibroblast spceific androgen signaling. Knockdown of Hic5 for 48 hours in ...
ORGANISM(S): Homo sapiens 
The LIM domain and tumour suppressor protein Testin (Tes) is downregulated in a variety of human tumours and tumour cell lines. Depending on its conformation, Tes localises to stress fibres and focal adhesions where it forms protein complexes with other members of the actin c...
ORGANISM(S): Homo sapiens (Human) 
2018-10-26 | PXD005058 | Pride
The glucocorticoid receptor (GR) recruits many coregulators via the well characterized AF2 interaction surface in the GR ligand binding domain, but LIM domain coregulator Hic-5 binds to the relatively uncharacterized tau2 activation domain in the hinge region of GR. Requirement of Hic-5 for glucocor...
ORGANISM(S): Homo sapiens 
The estrogen receptor (ER) recruits many coregulators but not as well as GR? We investigate the relationship between ER and Hic5 and identify classes of genes that respond differently when cells are induced with hormone and when Hic5 is knocked down We knock down Hic-5 (TGFB1I1) in U2OS cells using ...
ORGANISM(S): Homo sapiens 
The glucocorticoid receptor (GR) recruits many coregulators via the well characterized AF2 interaction surface in the GR ligand binding domain, but LIM domain coregulator Hic-5 binds to the relatively uncharacterized tau2 activation domain in the hinge region of GR. Requirement of Hic-5 for glucocor...
ORGANISM(S): Homo sapiens 
Hic-5 drives epithelial mechanotransduction promoting a feed-forward cycle of bronchoconstriction.
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