The DOI matches its Crossref record; 263 of the 269 references it cites were found in a registry or an index.
Chapter 1 Folate‐Mediated One‐Carbon Metabolism
Abstract
Tetrahydrofolate (THF) polyglutamates are a family of cofactors that carry and chemically activate one-carbon units for biosynthesis. THF-mediated one-carbon metabolism is a metabolic network of interdependent biosynthetic pathways that is compartmentalized in the cytoplasm, mitochondria, and nucleus. One-carbon metabolism in the cytoplasm is required for the synthesis of purines and thymidylate and the remethylation of homocysteine to methionine. One-carbon metabolism in the mitochondria is required for the synthesis of formylated methionyl-tRNA; the catabolism of choline, purines, and histidine; and the interconversion of serine and glycine. Mitochondria are also the primary source of one-carbon units for cytoplasmic metabolism. Increasing evidence indicates that folate-dependent de novo thymidylate biosynthesis occurs in the nucleus of certain cell types. Disruption of folate-mediated one-carbon metabolism is associated with many pathologies and developmental anomalies, yet the biochemical mechanisms and causal metabolic pathways responsible for the initiation and/or progression of folate-associated pathologies have yet to be established. This chapter focuses on our current understanding of mammalian folate-mediated one-carbon metabolism, its cellular compartmentation, and knowledge gaps that limit our understanding of one-carbon metabolism and its regulation.
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“Folate is a crucial constituent of one‐carbon metabolism (OCM) and is important for biosynthesis of purines and thymidylate, and remethylation of homocysteine to methionine (Fox & Stover, 2008; Li, Vijayanathan, Gulinello, & Cole, 2010).”
From Brain structure, working memory and response inhibition in childhood leukemia survivors (2017) · cites this paper as Fox & Stover, 2008
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“Since MTX is delivered through all phases of ALL treatment, folate metabolism may be altered for an extended period, possibly resulting in build‐up of homocysteine (Fox & Stover, 2008; Krull et al., 2016; Li et al., 2010; Steinfeld et al., 2009), and/or secondary metabolic alterations (van der Plas et al., 2015; Steinfeld et al., 2009; Strain et al., 2013).”
From Brain structure, working memory and response inhibition in childhood leukemia survivors (2017) · cites this paper as Fox & Stover, 2008
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Homocysteine and Cardiovascular Disease
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Folate, Vitamin B12, and Serum Total Homocysteine Levels in Confirmed Alzheimer Disease
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Folate and Carcinogenesis: An Integrated Scheme
Choi, S., & Mason, J. B. (2000) · Journal of Nutrition · doi:10.1093/jn/130.2.129 · Cited by 954
MTHFR 677C→T Polymorphism and Risk of Coronary Heart Disease
Klerk, M., Verhoef, P., Clarke, R., Blom, H. J., Kok, F. J., & Schouten, E. G. (2002) · JAMA · doi:10.1001/jama.288.16.2023 · Cited by 932
Mutated methylenetetrahydrofolate reductase as a risk factor for spina bifida
van der Put, N. M. J., Trijbels, F. J. M., van den Heuvel, L. P., Blom, H. J., Steegers‐Theunissen, R. P. M., Eskes, T. K. A. B., Mariman, E. C. M., den Heyer, M., Frosst, P. D., & Rozen, R. R. (1995) · The Lancet · doi:10.1016/s0140-6736(95)91743-8 · Cited by 862
THE CATALYTIC MECHANISM AND STRUCTURE OF THYMIDYLATE SYNTHASE
Carreras, C. W., & Santi, D. V. (1995) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.64.070195.003445 · Cited by 789
Ma, J., Stampfer, M. J., Giovannucci, E. L., Artigas, C., Hunter, D. J., Fuchs, C. S., Willett, W. C., Selhub, J., Hennekens, C. H., & Rozen, R. R. (1997) · PubMed · Cited by 774
DNA methylation: The nuts and bolts of repression
Miranda, T. B., & Jones, P. A. (2007) · Journal of Cellular Physiology · doi:10.1002/jcp.21224 · Cited by 701
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Mitochondria are the powerhouses of immunity
Mills, E. L., Kelly, B., & O'Neill, L. A. J. (2017) · Nature Immunology · doi:10.1038/ni.3704 · Cited by 1,161
Biomarkers of Nutrition for Development—Folate Review
Bailey, L. B., Stover, P. J., McNulty, H., Fenech, M. F., Gregory, J. F., Mills, J. L., Pfeiffer, C. M., Fazili, Z., Zhang, M., Ueland, P. M., et al. (2015) · Journal of Nutrition · doi:10.3945/jn.114.206599 · Cited by 1,170
Self-citationCompartmentalization of Mammalian Folate-Mediated One-Carbon Metabolism
Tibbetts, A. S., & Appling, D. R. (2010) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.012809.104810 · Cited by 692
Berger, M. M., Shenkin, A., Schweinlin, A., Amrein, K., Augsburger, M., Biesalski, H.-K., Bischoff, S. C., Casaer, M. P., Gundogan, K., Lepp, H.-L., et al. (2022) · Clinical Nutrition · doi:10.1016/j.clnu.2022.02.015 · Cited by 615
Antifolates in cancer therapy: Structure, activity and mechanisms of drug resistance
Gonen, N., & Assaraf, Y. G. (2012) · Drug Resistance Updates · doi:10.1016/j.drup.2012.07.002 · Cited by 444
Metadata
- Authors
- Fox, J. T., & Stover, P. J.
- Affiliations
- Cornell University (US)
- Venue
- Vitamins & Hormones
- Publisher
- Elsevier
- Published
- 2008
- Volume
- 79
- Pages
- 1-44
- ISSN
- 0083-6729 (ISSN-L)
- OpenAlex
- W3975443
- Cited by
- 402
- References
- 269
- Citations by year
- 2026: 19 · 2025: 24 · 2024: 22 · 2023: 17 · 2022: 20 · 2021: 25 · 2020: 25 · 2019: 34 · 2018: 25 · 2017: 36 · 2016: 35 · 2015: 16 · 2014: 16 · 2013: 26 · 2012: 18
- FWCI
- 62.82
- Type
- book chapter
- Language
- en
- Open access
- closed
- Locations
- Vitamins and hormones (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of Diabetes and Digestive and Kidney Diseases (DK58144)
- Topics
- Health Sciences › Nursing › Nutrition and Dietetics › Folate and B Vitamins Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Molecular Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Metabolism and Genetic Disorders
- Keywords
- folic acid, one-carbon metabolism, thymidylate synthesis, purine biosynthesis, homocysteine remethylation, methionine biosynthesis, histidine catabolism, mitochondrial metabolism, folate deficiency, developmental anomalies
- MeSH terms
- Animals, Cell Nucleus, Cytoplasm, Folic Acid, Mammals, Mitochondria, One-Carbon Group Transferases
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