Results 41 to 50 of about 6,588 (185)

Targeting phosphoglycerate dehydrogenase in multiple myeloma

open access: yesExperimental Hematology & Oncology, 2021
Background Multiple myeloma (MM) is a hematological malignancy characterized by the clonal expansion of plasma cells in the bone marrow. To date, this disease is still incurable and novel therapeutic approaches are required.
Samah Elsaadi   +9 more
doaj   +1 more source

A PHGDH inhibitor reveals coordination of serine synthesis and one-carbon unit fate [PDF]

open access: yes, 2015
Serine is a both a proteinogenic amino acid and the source of one-carbon units essential for de novo purine and deoxythymidine synthesis. In the canonical glucose-derived serine synthesis pathway, Homo sapiens phosphoglycerate dehydrogenase (PHGDH ...
Chen, Walter W.   +16 more
core   +2 more sources

Can small molecular inhibitors that stop de novo serine synthesis be used in cancer treatment?

open access: yesCell Death Discovery, 2021
To sustain their malignancy, tumour cells acquire several metabolic adaptations such as increased oxygen, glucose, glutamine, and lipids uptake. Other metabolic processes are also enhanced as part of tumour metabolic reprogramming, for example, increased
Megan Jessica McNamee   +2 more
doaj   +1 more source

Validating and enabling phosphoglycerate dehydrogenase (PHGDH) as a target for fragment-based drug discovery in PHGDH-amplified breast cancer

open access: yesOncotarget, 2016
3-Phosphoglycerate dehydrogenase (PHGDH) has recently been identified as an attractive target in cancer therapy as it links upregulated glycolytic flux to increased biomass production in cancer cells. PHGDH catalyses the first step in the serine synthesis pathway and thus diverts glycolytic flux into serine synthesis.
Unterlass JE   +7 more
openaire   +3 more sources

Phgdh is dispensable for lymphomagenesis in λ-Myc transgenic mice.

open access: yes, 2012
(A) Survival curve of λ-Myc mice generated from interbreedings between Phgdh+/− and λ-Myc transgenic mice. λ-Myc; Phgdh+/+ n = 21, λ-Myc; Phgdh+/− n = 23. (B) Amount of adenomas in ApcMin mice with different Phgdh genotypes.
Georg W. Bornkamm (10665)   +6 more
core   +1 more source

The metabolic reprogramming and vulnerability of SF3B1 mutations

open access: yesMolecular & Cellular Oncology, 2020
Mutations in the splicing factor 3b subunit 1 (SF3B1) gene create a neomorphic protein that disrupts RNA splicing, but the downstream consequences of this missplicing are unclear.
W. Brian Dalton
doaj   +1 more source

Phosphoglycerate dehydrogenase promotes pancreatic cancer development by interacting with eIF4A1 and eIF4E

open access: yesJournal of Experimental & Clinical Cancer Research, 2019
Background Pancreatic cancer is one of the most malignant cancers. The overall 5-year survival rate of its patients is 8%, the lowest among major cancer types.
Xuhui Ma   +4 more
doaj   +1 more source

HMGA2/PHGDH axis-mediated glycolysis under hypoxia is required for cadmium-induced A549 cell migration

open access: yesEcotoxicology and Environmental Safety
Cadmium (Cd) is a widespread environmental contaminant, which has been classified as a human carcinogen. Phosphoglycerate dehydrogenase (PHGDH), the first rate-limiting enzyme involved in the serine biosynthesis pathway, was reported to be able to ...
Chunpeng Gao   +5 more
doaj   +1 more source

Targeting one-carbon metabolism requires mTOR inhibition: a new therapeutic approach in osteosarcoma

open access: yesMolecular & Cellular Oncology, 2021
The rate-limiting enzyme of serine biosynthesis, 3-phosphoglycerate dehydrogenase (PHGDH), contributes to rapid growth and proliferation when it is overexpressed in cancer.
Richa Rathore, Brian Van Tine
doaj   +1 more source

Nuclear PHGDH protects cancer cells from nutrient stress

open access: yesNature Metabolism, 2021
In this study, the serine biosynthetic enzyme PHGDH is shown to transition from the cytosol to the nucleus following nutrient stress. Nuclear PHGDH reduces local NAD+ availability needed for the PARylation of the transcription factor c-Jun. Consequently, c-Jun activity is reduced, contributing to sustained cancer cell proliferation.
Annibali, Daniela, Fendt, Sarah-Maria
openaire   +3 more sources

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