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Suggest a novel role of PCGF2 (show PCGF2 ELISA Kits) in arsenic trioxide-mediated degradation of PML-RARA (show RARA ELISA Kits) that PCGF2 (show PCGF2 ELISA Kits) might act as a negative regulator of UBE2I (show UBE2I ELISA Kits) via direct interaction.
Indicate the important role of PML/c-Myc (show MYC ELISA Kits) axis in the maintenance of glioblastoma tumor stem cells. Arsenic trioxide disrupts glioma stem cells via promoting PML degradation to inhibit tumor growth.
Our work provides a novel view of the physiologic function of PML, which participates in telomeres surveillance in normal cells. Our data further imply that a diminished PML function may contribute to cell senescence, genomic instability and tumorigenesis
Authors demonstrate leukemogenicity of PAX5 (show PAX5 ELISA Kits)-PML by introducing it into normal mouse pro-B cells; B-cell linker protein (Blnk (show BLNK ELISA Kits)) is repressed by PAX5 (show PAX5 ELISA Kits)-PML in leukemia cells; enforced expression of Blnk (show BLNK ELISA Kits) increases survival despite introduction of PAX5 (show PAX5 ELISA Kits)-PML.
Mutations affect both the rearranged and the unrearranged PML alleles in refractory acute promyelocytic leukaemia.
Methylated arsenic metabolites bind to PML protein but do not induce cellular differentiation and PML-RARalpha (show RARA ELISA Kits) protein degradation in acute promyelocytic leukemia.
Novel insight into the functional difference of acquired mutations of PML-RARA (show RARA ELISA Kits) both in vitro and in the clinical setting.
Authors performed mutational analysis to define a PML interaction motif within the E1B (show BCKDHB ELISA Kits)-55K polypeptide. Results showed that E1B (show BCKDHB ELISA Kits)-55K/PML binding is not required for p53 (show TP53 ELISA Kits), Mre11 (show MRE11A ELISA Kits) and Daxx (show DAXX ELISA Kits) interaction.
These data suggest that targeting PML by human herpesvirus 5 IE1 represents a strategy to antagonize both intrinsic and innate immune mechanisms.
The results corroborated that PML-II plays a critical role in generating nuclear Lipid droplets in specific cell types.
both the PML-RARA (show RARA ELISA Kits)-driven competitive transplantation advantage and development of acute promyelocytic leukemia (APL (show FASL ELISA Kits)) required DNMT3A (show DNMT3A ELISA Kits)
PML IV enhances global SUMO-1 (show SUMO1 ELISA Kits) conjugation, particularly that of p53 (show TP53 ELISA Kits), resulting in p53 (show TP53 ELISA Kits) stabilization and activation.
our findings challenge the predominant model in the field and we propose that PML/RARA (show RARA ELISA Kits) initiates leukemia by subtly shifting cell fate decisions within the promyelocyte compartment.
DNA-binding-defective PML/RARA (show RARA ELISA Kits) mutants could not repress the transcription of retinoic acid regulated genes.
A novel antioxidative mechanism by which PML regulates cellular oxidant homeostasis by controlling complex II integrity and Nrf2 (show NFE2L2 ELISA Kits) activity and identified PML as an indispensable mediator of SFN (show SFN ELISA Kits) activity.
pRB (show PGR ELISA Kits) can interact with PML specifically during senescence, suggesting that signaling events in senescence regulate assembly of PML and pRB (show PGR ELISA Kits) to establish heterochromatin and create a permanent cell cycle arrest.
Data suggest that acute promyelocytic leukemia (APL (show FASL ELISA Kits)) differentiation is a default program triggered by clearance of promyelocytic leukemia-retinoic acid receptor alpha (show RARA ELISA Kits) fusion oncoprotein PML/RARA (show RARA ELISA Kits)-bound promoters.
Our results add PML/TRIM19 to the growing list of TRIM (show TRAT1 ELISA Kits) proteins implicated in both intrinsic and innate immunity.
Oxidized PML spherical meshes recruit UBC9 (show UBE2I ELISA Kits) and enhances PML sumoylation.
ORF61 encoded the viral ribonucleotide reductase large subunit (show RRM1 ELISA Kits) is a second PML-modifying protein.
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.
, probable transcription factor PML
, promyelocytic leukemia protein
, protein PML
, probable transcription factor PML-like
, RING finger protein 71
, promyelocytic leukemia, inducer of
, tripartite motif protein TRIM19
, tripartite motif-containing protein 19