Jan 9, 2025 · Here we show that MDM2, the p53 ubiquitin ligase, is a key component of the timer mechanism triggering G1 arrest in response to prolonged mitosis. This timer function arises due to the...

In order to study how MDM2 stimulated the activity of HeLa DNA polymerase ε, the effects of MDM2 upon the apparent K M values for dTTP and poly(dA)·oligo(dT) primer/template were determined.

Mar 19, 2020 · In HeLa cells lacking endogenous parkin, we co-expressed myc-parkin and increasing amounts of HA-tagged Mdm2, treated cells with carbonylcyanide m-chlorophenylhydrazone (CCCP) to depolarize ...

Mar 20, 1998 · To further confirm complex formation between ARF and MDM2 proteins, HeLa tet-off cells were transfected with plasmids directing the expression of human MDM2 (pCMV-MDM2) together with either HA epitope–tagged ARF (pTRE-HA-ARF), INK4a (pTRE-HA-INK4a), or the parental vector (pTRE).

Feb 28, 2019 · Our data indicated that MDM2 overexpression-mediated repression of HBP1 delays DNA damage repair and causes cell death in a p53-independent manner.

In this study, we evaluated the impacts of NMD inhibitor, Mouse double minute 2 homolog (MDM2) inhibitor, and their combination on cell apoptosis, cell cycle, and p53 target genes in human papillomavirus-18-positive HeLa cells.

MDM2 also known as murine double minute 2 is an important regulator of the p53 tumor suppressor protein. It functions as an E3 ubiquitin ligase targeting p53 for proteasomal degradation. The MDM2 protein has a molecular weight of approximately 55 kDa.

In this study we demonstrate that ubiquitin over-expression promotes the destabilization of the ubiquitin protein ligase E6AP, by a mechanism involving self-ubiquitination, and the stabilization of p53.

Population: African American. Knockout cell: Method=CRISPR/Cas9; HGNC; HGNC:6973; MDM2. Transformant: NCBI_TaxID; 333761; Human papillomavirus type 18 (HPV18). Derived from site: In situ; Uterus, cervix; UBERON= UBERON_0000002.

3 days ago · After Hela cells were cultured for 72 h, the mRNA and protein expressions corresponding to EGFR, TNF-α, VEGFA, PI3K, AKT and MDM2 were decreased in the experimental group compared with the control group as confirmed by RT-PCR and Western blot, and the extent of the decrease was more obvious with …