Serine and one-carbon metabolism in cancer
By Ming Yang, Karen H. Vousden. Nature Reviews. Cancer, 2016
906 citations recorded by the source corpus.
Subfields: Biochemistry, Cancer Research, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/52df71256e3fb907b31a6ff031f20d84d6690fa7
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In Biochemistry
In Cancer Research
In Molecular Biology
Citations in the corpus
- Revisiting the Warburg effect: historical dogma versus current understanding (2020, background): “(c) The non-essential amino acids serine and glycine and the one-carbon metabolism pathway emanate from the intermediate 3-phosphoglycerate (Yang & Vousden, 2016).”
- Oxidative Stress in Cancer (2020, background): “glycine (from serine by serine hydroxymethyltransferase within the one-carbon pathway) and cysteine (from cystathionine by cystathionine lyase within the trans-sulfuration pathway), two of the amino acids used to synthesize GSH (Yang and Vousden, 2016); the supply of cysteine can be augmented by the”
- NAD(H) and NADP(H) Redox Couples and Cellular Energy Metabolism (2018, background): “In addition, other enzymes also contribute to the cytosolic NADPH pool, such as IDHs and MEs (87, 139), all of which have both cytosolic and mitochondrial isozymes.”
- Metabolic reprogramming and epigenetic modifications on the path to cancer (2021, background): “2). me-THF can also be produced by the glycine cleavage system (glycine dehydrogenase (GLDC) is the major component), in which glycine is cleaved into ammonia, carbon dioxide, and a carbon © The Author(s) 2021 887 P ro te in & C e ll unit, which is involved in the methylation of THF (Locasale, 2013;”
- Revisiting the hallmarks of cancer. (2017, neutral): “The acquisition of lipids or fatty acids, amino acids other than glutamine, and extracellular acetate, and their contribution and necessity to tumorigenesis are subjects of recent research [144, 155-157].”
- From Krebs to Clinic: Glutamine Metabolism to Cancer Therapy (2016, background): “BPTES inhibition of hGA(124-551), a truncated form of human kidneytype glutaminase.”