抗Human MNT 抗体:
抗Mouse (Murine) MNT 抗体:
抗Rat (Rattus) MNT 抗体:
In vitro, uremia induced dysregulation of DNA methylation in differentiating monocytes, which affected several transcription regulators important for monocyte differentiation (e.g., FLT3, HDAC1, MNT) and led to enhanced generation of intermediate monocytes.
Here we review the activities of MYC, MNT and other MAX interacting proteins in the setting of T and B cell activation and oncogenesis
The data demonstrate that the balance between c-Myc and Mnt activity determines the transcriptional outcome of the hTERT promoter by modulation of the chromatin architecture.
The results suggest that MNT, via interaction with Nck1, inhibits hepatoma cell migration.
downregulation MYCN was reflected in a decreased MYCN/Max DNA-binding activity while the Mnt/Max binding did not change during differentiation
Serum stimulation of quiescent cells results in phosphorylation of Mnt and disruption of the critical Mnt-mSin3-HDAC1 interaction. This in turn leads to increased expression of the Myc/Mnt target gene cyclin D2. Review.
Mad1, Mxi1 and Rox genes were expressed and displayed mutations in haematological malignancies.
Mxd1 D112a and Max N78a and H81d, which are located in the leucine zippers of the proteins, can dictate the specificity of heterodimerization and whether or not the Mxd1/Max/DNA complex forms.
Missense mutations in Mad1, Mxi1 and Rox were found in acute leukemia patients.
The switch from Mnt-Max to Myc-Max during bile duct ligation (cholestasis) and in hepatocytes treated with lithocholic acid is responsible for the induction in p53 and cyclin D1 expression and contributes to apoptosis.
Although mnt heterozygosity clearly slowed lymphomagenesis in vavP-MYC10 and Emu-myc mice, the change(s) in cellular properties responsible for this effect remain to be identified.
results redefine the physiological relationship between Mnt and Myc and requirements for Myc-driven oncogenesis
Mxd4 and Mnt upregulation following OX40 engagement most likely increases T-cell survival
There is a unique negative regulatory role for Mnt in governing key Myc functions associated with cell proliferation and tumorigenesis.
Mnt may serve a general role as a Myc antagonist.[Review]
Mnt represses Myc target genes and Myc functions as an oncogene by relieving Mnt-mediated repression
Loss of protein Mnt in mice results in decreased viability, defective embryonic growth and craniofacial defects.
These results demonstrate that Mnt-Myc antagonism plays a fundamental role in regulating cell cycle entry and proliferation.
Mnt is expressed both in growth-arrested and proliferating mouse fibroblasts and is phosphorylated when resting cells are induced to re-enter the cell cycle
Mnt functions as a tumor suppressor and reveal a critical and surprising role for Mnt in the regulation of T-cell development and in T-cell-dependent immune homeostasis.
The Myc/Max/Mad network comprises a group of transcription factors that co-interact to regulate gene-specific transcriptional activation or repression. This gene encodes a protein member of the Myc/Max/Mad network. This protein has a basic-Helix-Loop-Helix-zipper domain (bHLHzip) with which it binds the canonical DNA sequence CANNTG, known as the E box, following heterodimerization with Max proteins. This protein is likely a transcriptional repressor and an antagonist of Myc-dependent transcriptional activation and cell growth. This protein represses transcription by binding to DNA binding proteins at its N-terminal Sin3-interaction domain.
MAX binding protein
, Max-interacting protein
, class D basic helix-loop-helix protein 3
, max-binding protein MNT
, myc antagonist MNT
, max binding protein
, MNT, MAX dimerization protein