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Regulates centrosome duplication, probably by inhibiting the kinase activity of ROCK2.
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suppression of miR (show MLXIP Proteins)-26b expression up-regulates its target gene CHORDC1, which increases HBV enhancer/promoter activities and promotes viral transcription, gene expression, and replication
morgana causes PTEN destabilization, by inhibiting ROCK activity
Chp-1 (show CHP Proteins) and melusin (show ITGB1BP2 Proteins) can interact with cochaperones PP5 (show PPP5C Proteins) and Sgt1 (show SUGT1 Proteins) and with each other in an ATP-dependent manner
A novel ADP-dependent HSP90 (show HSP90 Proteins) interaction with the cysteine- and histidine-rich domain (CHORD)-containing protein CHORDC1, is characterized.
This paper described the cloning of a barley CHORD containing protein, but it also described the CHORD containing proteins in other species including human and characterized the CHORD domains.
Loss of Morgana expression is associated with drug resistance and chronic myeloid leukemia (show BCL11A Proteins).
Chp-1 and melusin (show ITGB1BP2 Proteins) can interact with cochaperones PP5 (show PPP5C Proteins) and Sgt1 (show SUGT1 Proteins) and with each other in an ATP-dependent manner
Overexpression of morgana/CHP-1 in NIH3T3 cells leads to the increased stress resistance of the cells.
Morgana/chp-1 downregulation promotes the interaction between ROCK II (show ROCK2 Proteins) and nucleophosmin (show NPM1 Proteins), leading to an increased ROCK II (show ROCK2 Proteins) kinase activity, which results in centrosome amplification.
Full length sequence, gene structure and expression of Chp-1.
The first biochemical evidence demonstrating that mammalian Chp-1 is a novel Hsp90 (show HSP90 Proteins)-interacting protein.
results suggest that Chordc1 mRNA is under complex and widespread transcriptional regulation during development and implicate Chordc1 in circadian and/or homeostatic mechanisms in mammalian brain.
Regulates centrosome duplication, probably by inhibiting the kinase activity of ROCK2. Proposed to act as co-chaperone for HSP90. May play a role in the regulation of NOD1 via a HSP90 chaperone complex. In vitro, has intrinsic chaperone activity. This function may be achieved by inhibiting association of ROCK2 with NPM1. Involved in stress response. Prevents tumorigenesis (By similarity).
CHORD-containing protein 1
, chord domain-containing protein 1
, cysteine and histidine-rich domain (CHORD)-containing 1
, cysteine and histidine-rich domain (CHORD)-containing, zinc-binding protein 1
, cysteine and histidine-rich domain-containing protein 1
, protein morgana
, CHORD domain-containing protein 1
, cysteine and histidine-rich domain (CHORD)-containing, zinc binding protein 1
, CHORD containing protein-1