MYC coordinates protein synthesis through the transcriptional control of RNA and protein ... Sears, R. & Lu, H. Feedback regulation of c-Myc by ribosomal protein L11. Cell Cycle 6, 2735–2741 ...

In tumors, MYC protein expression can be elevated as a consequence of gene amplification, ... On the other hand, MAX- and E-box-independent functions of MYC in transcriptional regulation have also ...

Max deletion destabilizes MYC protein and abrogates Eµ-Myc lymphomagenesis. Genes Dev Sept 1; 33(17-18): 1252-1264. This work was supported by the National Institutes of Health. Cancer Consortium ...

Researchers have developed a peptide that targets a protein implicated in 75% of human cancers and found that it slowed the proliferation of cancer cells in the lab. It’s the first step towards ...

Like any protein, MYC is built using the instructions that are stored in the MYC gene. First, in a process called transcription, the cell uses these instructions to make a blueprint, called mRNA.

Finally, the authors sought to understand how MLX works with other MYC network proteins to regulate germ cell gene expression. Chromatin immunoprecipitation showed that MLX and MAX, MYC’s obligate ...

We identified USP17 as a novel deubiquitinating enzyme regulating c-Myc levels to control cell proliferation. Overexpression of USP17 stabilized the c-Myc protein by promoting its deubiquitination ...

The growth protein, MYC, was consistently found with RBM42, which spurs MYC production, in human pancreatic tumors. Above, microscopy for MYC (red) and RBM42 (green) in a representative pancreatic ...

Myc is a cancer-causing gene responsible for disrupting the normal 24-hour internal rhythm and metabolic pathways in cancer cells. Researchers have found that MYC protein may affect circadian ...

Meet MYC, the shapeless protein responsible for making the majority of human cancer cases worse. UC Riverside researchers have found a way to rein it in, offering hope for a new era of treatments.

A gene known as Myc is linked to cancer growth, but has long been considered “undruggable." Now, researchers at Vanderbilt University have found a way to bypass it and shut down a protein that ...