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STAT3 (show STAT3 Proteins) is responsible, at least in part, for the transcriptional upregulation of PML in breast cancer. Moreover, PML targeting hampers breast cancer initiation and metastatic seeding. Mechanistically, this biological activity relies on the regulation of the stem cell gene SOX9 (show SOX9 Proteins) through interaction of PML with its promoter region.
Respiratory syncytial virus induces NRF2 (show GABPA Proteins) degradation through a PML-RNF4 (show RNF4 Proteins) pathway.
Data suggest that intracellular host defenses are counteracted by ICP0, which targets PML for degradation from the outset of nuclear infection to promote viral-DNA release from PML-nuclear bodies and the onset of HSV-1 lytic replication. (ICP0 = immediate early (show JUN Proteins) infected polypeptide-0; PML = promyelocytic leukemia protein; HSV-1 = herpes simplex virus-1)
the PML(NLS (show ALDH1A2 Proteins)-) protein was detectable in the cytoplasm of neutrophils from patients with acute promyelocytic leukemia.
The PML sumo interaction motif differentially affects nuclear body formation by each individual isoform.
inhibiting CK2 (show CSNK2A1 Proteins) can enhance sensitivity of Cisplatin to Non-small cell lung carcinoma cells through PML
Results show that PolySUMO5 conjugation on K160 of PML results in recruitment of proteins to form PML-nuclear bodies. SUMO5 conjugation on PML is gradually replaced by SUMO2 (show SUMO2 Proteins)/3 conjugation, which leads to RNF4 (show RNF4 Proteins)-mediated disruption of PML-NBs (show NBN Proteins).
the ND10 bodies become viral replication compartments, and ICP0, a viral E3 ligase, degrades both PML and SP100 (show SP100 Proteins). The amounts of PML and SP100 (show SP100 Proteins) and the number of ND10 structures increase in cells exposed to IFN-beta (show IFNB1 Proteins).
These results therefore indicate that EGCG targets PML/RARalpha oncoprotein for degradation and potentiates differentiation of promyelocytic leukemia cells in combination with ATRA via PTEN.
Mechanically, mutant NPM1 (show NPM1 Proteins) interacted with PML and mediated its delocalization as well as stabilization contributing to elevated autophagic activity and leukemic cell survival in vitro.
PML mediates the binding of PER2 (show PER2 Proteins) to BMAL1 (show ARNTL Proteins) in the BMAL1 (show ARNTL Proteins)/CLOCK heterodimer and is an important component in the organization of a functional clock complex in the nucleus.
Promyelocytic leukemia protein Pml -/- cells showed a higher proliferation rate, compared to Pml +/+ cells.
PML protein organizes heterochromatin domains where it regulates histone H3.3 (show H3F3A Proteins) deposition by ATRX (show ATRX Proteins) and DAXX (show DAXX Proteins).
Data indicate that promyelocytic leukemia protein knockout (Pml-/-) animals fail to properly activate oxidative stress-responsive p53 (show TP53 Proteins) targets, whereas the NRF2 (show NFE2L2 Proteins) response is amplified and accelerated.
data support a model in which activation of myogenic differentiation results in PML NB loss, chromatin reorganization and DAXX (show DAXX Proteins) relocalization, and provides a paradigm for understanding the consequence of PML loss in other cellular contexts, such as during cancer development and progression
a regulatory role of ZNF451-1 in fine-tuning physiological PML levels
PML loss promotes tumor development, providing a growth advantage to tumor cells that use autophagy as a cell survival strategy during stress conditions.
The data demonstrate a dual role of PML in protection and recovery after brain injury.
This study designates PML protein and PML-NBs (show NLRP2 Proteins) to be major cellular components involved in the control of Herpes simplex virus 1 (HSV-1) latency, probably during the entire life of an individual.
Study found that Promyelocytic leukemia protein (PML) is broadly expressed across the gray matter, with the highest levels in the cerebral and cerebellar cortices. PML bodies are broadly involved in activity-dependent nuclear phenomena in adult neurons
The protein encoded by this gene is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. This phosphoprotein localizes to nuclear bodies where it functions as a transcription factor and tumor suppressor. Its expression is cell-cycle related and it regulates the p53 response to oncogenic signals. The gene is often involved in the translocation with the retinoic acid receptor alpha gene associated with acute promyelocytic leukemia (APL). Extensive alternative splicing of this gene results in several variations of the protein's central and C-terminal regions\; all variants encode the same N-terminus. Alternatively spliced transcript variants encoding different isoforms have been identified.
RING finger protein 71
, probable transcription factor PML
, promyelocytic leukemia protein
, promyelocytic leukemia, inducer of
, protein PML
, tripartite motif protein TRIM19
, tripartite motif-containing protein 19
, promyelocytic leukemia
, probable transcription factor PML-like