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JMJD5 depletion increases the susceptibility of cancer cells to microtubule-destabilizing agents.
JMJD5 is a tumor suppressor gene in HCC (zeige FAM126A ELISA Kits) pathogenesis, and the epigenetic silencing of JMJD5 promotes HCC (zeige FAM126A ELISA Kits) cell proliferation by directly down-regulating CDKN1A transcription.
Data suggest that JMJD5 partially accumulates on mitotic spindles during mitosis; depletion of JMJD5 results in significant mitotic arrest, spindle assembly defects, and sustained activation of spindle assembly checkpoint.
These results suggest that direct interaction of JMJD5 with HBx facilitates hepatitis B virus replication through the hydroxylase activity of JMJD5.
Suggest JMJD5 as a potential oncogene (zeige RAB1A ELISA Kits) in colon carcinogenesis.
results reveal that JMJD5 is a novel binding partner of p53 (zeige TP53 ELISA Kits) and it functions as a positive modulator of cell cycle and cell proliferation mainly through the repression of p53 (zeige TP53 ELISA Kits) pathway.
we provide genetic and biochemical evidence that the JMJD5/CDKN1A (p21 (zeige CDKN1A ELISA Kits)) axis is essential to maintaining the short G1 phase which is critical for pluripotency in human embryonic stem cells
RCCD1 and KDM8 form a histone demethylase (zeige MBD2 ELISA Kits) complex.
These results reveal that the N-terminal domain is essential for the nuclear localization of JMJD5 and its normal enzymatic function towards substrates in the nucleus
Comparison of the structure of JMJD5 with that of FIH (zeige CASR ELISA Kits), a well characterized protein hydroxylase, reveals that human JMJD5 might function as a protein hydroxylase.
Jmjd5 is involved in the transcriptional regulation of a subset of p53 (zeige TP53 ELISA Kits)-regulated genes, possibly through the control of p53 (zeige TP53 ELISA Kits) recruitment at the gene loci.
Data suggest that Jmjd5 partially accumulates on mitotic spindles during mitosis; depletion of Jmjd5 results in significant mitotic arrest, spindle assembly defects, and sustained activation of spindle assembly checkpoint.
Collectively, these data indicate that JMJD5 is essential during embryonal development and a repressor of p53 (zeige TP53 ELISA Kits) expression. The latter suggests that JMJD5 has oncogenic activity and accordingly JMJD5 is upregulated in leukemias and breast cancer.
Results suggest that Jmjd5 physiologically moderates embryonic cell proliferation through the epigenetic control of Cdkn1a (zeige CDKN1A ELISA Kits) expression.
This gene likely encodes a histone lysine demethylase. Studies of a similar protein in mouse indicate a potential role for this protein as a tumor suppressor. Alternatively spliced transcript variants have been described.
jumonji domain containing 5
, JmjC domain-containing protein 5
, Jumonji domain-containing protein 5
, lysine-specific demethylase 8
, jmjC domain-containing protein 5
, jumonji domain-containing protein 5