Results 101 to 110 of about 6,588 (185)
FBXO7 ubiquitinates PRMT1 to suppress serine synthesis and tumor growth in hepatocellular carcinoma
Cancer cells are often addicted to serine synthesis to support growth. How serine synthesis is regulated in cancer is not well understood. We recently demonstrated protein arginine methyltransferase 1 (PRMT1) is upregulated in hepatocellular carcinoma ...
Li Luo +9 more
doaj +1 more source
Non-canonical function of PHGDH promotes HCC metastasis by interacting with METTL3
Phosphoglycerate dehydrogenase (PHGDH), a pivotal enzyme in serine synthesis, plays a key role in the malignant progression of tumors through both its metabolic activity and moonlight functions. This study aims to elucidate the non-canonical function of PHGDH in promoting hepatocellular carcinoma (HCC) metastasis through its interaction with ...
Cheng, Bin +5 more
openaire +3 more sources
Argininosuccinate synthase (ASS1), a critical enzyme in the urea cycle, acts as a tumor suppressor in many cancers. To date, the anticancer mechanism of ASS1 has not been fully elucidated. Here, we found that phosphoglycerate dehydrogenase (PHGDH), a key
Wensong Luo +14 more
doaj +1 more source
Yuhai Zou,1,* Dongdong Li,1,* Ge Guan,1 Wenting Liu2 1Department of Cardiology, General Hospital of Southern Theatre Command of PLA, Guangzhou, 510010, People’s Republic of China; 2Department of Otorhinolaryngology, Guangzhou First People’s ...
Zou Y, Li D, Guan G, Liu W
doaj
PHGDH in cancer: a narrative review of its functions beyond serine metabolism. [PDF]
Li J, Zhang H, Zhu G, Xu H.
europepmc +1 more source
1p/19q codeletion induces targetable and imageable vulnerabilities in glucose metabolism in oligodendrogliomas. [PDF]
Udutha S +4 more
europepmc +1 more source
Mechanistic study of PHGDH enzyme inhibition : towards the development of new anticancer drugs
The selective targeting of metabolic differences that allow cancer cells to proliferate appears as a promising strategy to develop novel anticancer agents.
Spillier, Quentin
core

