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This study demonstrated an important phosphorylated site of PML, which contributed to explore the role of PML in mitosis.
PML acts as an effector of antiviral effects of IFN-beta (show IFNB1 Proteins).
The activity of the PML internal ribosome entry site is induced by TNFalpha (show TNF Proteins) in a manner that involves MNK1 (show MKNK1 Proteins) activation.
The association of RNF168 (show RNF168 Proteins) with PML NBs (show NBN Proteins) resulted in increased ubiquitylation.
Data suggest that hematopoietically expressed homeobox protein (HHEX (show HHEX Proteins)) downmodulation by promyelocytic leukemia-retinoic acid receptor alpha (show RARA Proteins) fusion oncoprotein (PML-RARalpha (show RARA Proteins)) is a key event during acute promyelocytic leukemia (APL (show FASL Proteins)) pathogenesis.
The authors show that PML can inhibit HIV-1 and other lentiviruses as part of the IFN-I-mediated response.
PML contributes to the intrinsic restriction of HIV-1 infections in a cell type-dependent manner.
Suggest a novel role of PCGF2 (show PCGF2 Proteins) in arsenic trioxide-mediated degradation of PML-RARA (show RARA Proteins) that PCGF2 (show PCGF2 Proteins) might act as a negative regulator of UBE2I (show UBE2I Proteins) via direct interaction.
Indicate the important role of PML/c-Myc (show MYC Proteins) 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
both the PML-RARA (show RARA Proteins)-driven competitive transplantation advantage and development of acute promyelocytic leukemia (APL (show FASL Proteins)) required DNMT3A (show DNMT3A Proteins)
PML IV enhances global SUMO-1 (show SUMO1 Proteins) conjugation, particularly that of p53 (show TP53 Proteins), resulting in p53 (show TP53 Proteins) stabilization and activation.
our findings challenge the predominant model in the field and we propose that PML/RARA (show RARA Proteins) initiates leukemia by subtly shifting cell fate decisions within the promyelocyte compartment.
DNA-binding-defective PML/RARA (show RARA Proteins) 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 Proteins) activity and identified PML as an indispensable mediator of SFN (show SFN Proteins) activity.
pRB (show PGR Proteins) can interact with PML specifically during senescence, suggesting that signaling events in senescence regulate assembly of PML and pRB (show PGR Proteins) to establish heterochromatin and create a permanent cell cycle arrest.
Data suggest that acute promyelocytic leukemia (APL (show FASL Proteins)) differentiation is a default program triggered by clearance of promyelocytic leukemia-retinoic acid receptor alpha (show RARA Proteins) fusion oncoprotein PML/RARA (show RARA Proteins)-bound promoters.
Our results add PML/TRIM19 to the growing list of TRIM (show TRAT1 Proteins) proteins implicated in both intrinsic and innate immunity.
Oxidized PML spherical meshes recruit UBC9 (show UBE2I Proteins) and enhances PML sumoylation.
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