Chapter 1 Folate‐Mediated One‐Carbon Metabolism

Homocysteine and Cardiovascular Disease

Refsum, H., Ueland, P. M., Nygård, O., & Vollset, S. E. (1998) · Annual Review of Medicine · doi:10.1146/annurev.med.49.1.31 · Cited by 2,180 · see citing works

Folate deficiency causes uracil misincorporation into human DNA and chromosome breakage: Implications for cancer and neuronal damage

Blount, B. C., Mack, M. M., Wehr, C. M., MacGregor, J. T., Hiatt, R. A., Wang, G., Wickramasinghe, S. N., Everson, R. B., & Ames, B. N. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.7.3290 · Cited by 1,438 · see citing works

Folate, Vitamin B12, and Serum Total Homocysteine Levels in Confirmed Alzheimer Disease

Clarke, R., Smith, A. D., Jobst, K. A., Refsum, H., Sutton, L., & Ueland, P. M. (1998) · Archives of Neurology · doi:10.1001/archneur.55.11.1449 · Cited by 1,408 · see citing works

Relation Between Folate Status, a Common Mutation in Methylenetetrahydrofolate Reductase, and Plasma Homocysteine Concentrations

Jacques, P. F., Bostom, A. G., Williams, R. R., Ellison, R. C., Eckfeldt, J. H., Rosenberg, I. H., Selhub, J., & Rozen, R. R. (1996) · Circulation · doi:10.1161/01.cir.93.1.7 · Cited by 1,380 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

Methylenetetrahydrofolate reductase polymorphism, dietary interactions, and risk of colorectal cancer.

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 · see citing works

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 685 · see citing works

The antiinflammatory mechanism of methotrexate. Increased adenosine release at inflamed sites diminishes leukocyte accumulation in an in vivo model of inflammation.

Cronstein, B. N., Naime, D., & Ostad, E. (1993) · Journal of Clinical Investigation · doi:10.1172/jci116884 · Cited by 683 · see citing works

Molecular genetic analysis in mild hyperhomocysteinemia: a common mutation in the methylenetetrahydrofolate reductase gene is a genetic risk factor for cardiovascular disease.

Kluijtmans, L. A. J., van den Heuvel, L. P., Boers, G. H. J., Frosst, P. D., Stevens, E. M., van Oost, B. A., den Heijer, M., Trijbels, F. J. M., Rozen, R. R., & Blom, H. J. (1996) · PubMed Central · Cited by 653 · see citing works

Homocysteine metabolism in pregnancies complicated by neural-tube defects

Mills, J. L., Lee, Y. J., Conley, M. R., Kirke, P. N., McPartlin, J. M., Weir, D. G., & Scott, J. M. (1995) · The Lancet · doi:10.1016/s0140-6736(95)90165-5 · Cited by 642 · see citing works

Folate in Health and Disease

Bailey, L. B. (2009) · CRC Press eBooks · doi:10.1201/9781420071252 · Cited by 636 · see citing works

How a Protein Binds B 12 : A 3.0 Å X-Ray Structure of B 12 -Binding Domains of Methionine Synthase

Drennan, C. L., Huang, S., Drummond, J. T., Matthews, R. G., & Ludwig, M. L. (1994) · Science · doi:10.1126/science.7992050 · Cited by 626 · see citing works

Thymidylate synthase gene polymorphism determines response and toxicity of 5-FU chemotherapy

Pullarkat, S. T., Stoehlmacher, J., Ghaderi, V. S., Xiong, Y.-P., Ingles, S. A., Sherrod, A., Warren, R. S., Tsao-Wei, D. D., Groshen, S. G., & Lenz, H. J. (2001) · The Pharmacogenomics Journal · doi:10.1038/sj.tpj.6500012 · Cited by 571 · see citing works

DNA damage from micronutrient deficiencies is likely to be a major cause of cancer

Ames, B. N. (2001) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/s0027-5107(01)00070-7 · Cited by 564 · see citing works

Functional Analysis and DNA Polymorphism of the Tandemly Repeated Sequences in the 5'-terminal Regulatory Region of the Human Gene for Thymidylate Synthase.

Horie, N., Aiba, H., Oguro, K., Hojo, H., & Takeishi, K. (1995) · Cell Structure and Function · doi:10.1247/csf.20.191 · Cited by 547 · see citing works

Polymorphisms in the methylenetetrahydrofolate reductase gene are associated with susceptibility to acute leukemia in adults

Skibola, C. F., Smith, M. T., Kane, E. V., Roman, E., Rollinson, S. J., Cartwright, R. A., & Morgan, G. J. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.22.12810 · Cited by 527 · see citing works

A methylenetetrahydrofolate reductase polymorphism and the risk of colorectal cancer.

Chen, J., Giovannucci, E. L., Kelsey, K. T., Rimm, E. B., Stampfer, M. J., Colditz, G. A., Spiegelman, D. L., Willett, W. C., & Hunter, D. J. (1996) · PubMed · Cited by 516 · see citing works

The controversy over homocysteine and cardiovascular risk

Ueland, P. M., Refsum, H. M., Beresford, S. A. A., & Vollset, S. E. (2000) · American Journal of Clinical Nutrition · doi:10.1093/ajcn/72.2.324 · Cited by 514 · see citing works

The structure and properties of methylenetetrahydrofolate reductase from Escherichia coli suggest how folate ameliorates human hyperhomocysteinemia.

Matthews, R. G., Ludwig, M. L., Guenther, B. D., Sheppard, C. A., Tran, P. V., & Rozen, R. R. (1999) · Nature Structural Biology · doi:10.1038/7594 · Cited by 422 · see citing works

Effects of common polymorphisms on the properties of recombinant human methylenetetrahydrofolate reductase

Yamada, K., Chen, Z., Rozen, R. R., & Matthews, R. G. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.261469998 · Cited by 411 · see citing works

Human methionine synthase: cDNA cloning and identification of mutations in patients of the cblG complementation group of folate/cobalamin disorders

Leclerc, D. (1996) · Human Molecular Genetics · doi:10.1093/hmg/5.12.1867 · Cited by 400 · see citing works

The role of the 5′ untranslated region of an mRNA in translation regulation during development

van der Velden, A. W., & Thomas, A. A. M. (1999) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(98)00134-4 · Cited by 397 · see citing works

Cloning and mapping of a cDNA for methionine synthase reductase, a flavoprotein defective in patients with homocystinuria

Leclerc, D., Wilson, A., Dumas, R., Gafuik, C. J., Song, D., Watkins, D., Heng, H. H., Rommens, J. M., Scherer, S. W., Rosenblatt, D. S., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.6.3059 · Cited by 391 · see citing works

Autoregulation of human thymidylate synthase messenger RNA translation by thymidylate synthase.

Chu, E., Koeller, D. M., Casey, J. L., Drake, J. C., Chabner, B. A., Elwood, P. C., Zinn, S., & Allegra, C. J. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.20.8977 · Cited by 382 · see citing works

A novel single nucleotide polymorphism within the 5' tandem repeat polymorphism of the thymidylate synthase gene abolishes USF-1 binding and alters transcriptional activity.

Mandola, M. V., Stoehlmacher, J., Muller‐Weeks, S., Cesarone, G., Yu, M. C., Lenz, H., & Ladner, R. D. (2003) · PubMed · Cited by 363 · see citing works

Multienzyme complex for metabolic channeling in mammalian DNA replication.

Reddy, G. P. V., & Pardee, A. B. (1980) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.77.6.3312 · Cited by 353 · see citing works

Compartmentation of folate‐mediated one‐carbon metabolism in eukaryotes

Appling, D. R. (1991) · The FASEB Journal · doi:10.1096/fasebj.5.12.1916088 · Cited by 350 · see citing works

TREATMENT OF TETANUS SEVERE BONE-MARROW DEPRESSION AFTER PROLONGED NITROUS-OXIDE ANESTHESIA

Lassen, H. C. A. (1956) · The Lancet · doi:10.1016/s0140-6736(56)90593-1 · Cited by 347 · see citing works

Mammalian methylenetetrahydrofolate reductase Partial purification, properties, and inhibition by S-adenosylmethionine

Kutzbach, C., & Stokstad, E. L. R. (1971) · Biochimica et Biophysica Acta (BBA) - Enzymology · doi:10.1016/0005-2744(71)90247-6 · Cited by 342 · see citing works

Thermolabile variant of 5, 10-methylenetetrahydrofolate reductaseassociated with low red-cell folates: implications for folate intake recommendations

Molloy, A. M., Daly, S., Mills, J. L., Kirke, P. N., Whitehead, A. S., Ramsbottom, D., Conley, M. R., Weir, D. G., & Scott, J. M. (1997) · The Lancet · doi:10.1016/s0140-6736(96)12049-3 · Cited by 341 · see citing works

Polyglutamation of methotrexate with common polymorphisms in reduced folate carrier, aminoimidazole carboxamide ribonucleotide transformylase, and thymidylate synthase are associated with methotrexate effects in rheumatoid arthritis

Dervieux, T., Furst, D. E., Lein, D. O., Capps, R., Smith, K., Walsh, M. W., & Kremer, J. M. (2004) · Arthritis & Rheumatism · doi:10.1002/art.20460 · Cited by 337 · see citing works

Methylenetetrahydrofolate reductase (MTHFR) polymorphisms and risk of molecularly defined subtypes of childhood acute leukemia

Wiemels, J. L., Smith, R., Taylor, G. M., Eden, O. B., Alexander, F. E., Greaves, M. F., & United Kingdom Childhood Cancer Study Investigators (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.061408298 · Cited by 337 · see citing works

STRUCTURE-BASED PERSPECTIVES ON B12-DEPENDENT ENZYMES

Ludwig, M. L., & Matthews, R. G. (1997) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.66.1.269 · Cited by 328 · see citing works

Folylpolyglutamate Synthesis and Role in the Regulation of One-Carbon Metabolism

Shane, B. (1989) · Vitamins and hormones · doi:10.1016/s0083-6729(08)60397-0 · Cited by 322 · see citing works

Vitamin B ₁₂ -Folate Interrelationships

Shane, B., & Stokstad, E. L. R. (1985) · Annual Review of Nutrition · doi:10.1146/annurev.nu.05.070185.000555 · Cited by 311 · see citing works

Folate in Health and Disease

Bowman, B. A. (1995) · American Journal of Clinical Nutrition · doi:10.1093/ajcn/62.5.1029 · Cited by 308 · see citing works

Breaks in genomic DNA and within the p53 gene are associated with hypomethylation in livers of folate/methyl-deficient rats.

Pogribny, I. P., Basnakian, A. G., Miller, B., Lopatina, N., Poirier, L. A., & James, S. J. (1995) · PubMed · Cited by 308 · see citing works

A 6 bp polymorphism in the thymidylate synthase gene causes message instability and is associated with decreased intratumoral TS mRNA levels

Mandola, M. V., Stoehlmacher, J., Zhang, W., Groshen, S. G., Yu, M. C., Iqbal, S., Lenz, H., & Ladner, R. D. (2004) · Pharmacogenetics · doi:10.1097/00008571-200405000-00007 · Cited by 298 · see citing works

Polymorphic tandem repeats in the thymidylate synthase gene is associated with its protein expression in human gastrointestinal cancers.

Kawakami, K., Omura, K., Kanehira, E., & Watanabe, Y. (1999) · PubMed · Cited by 282 · see citing works

BIOCHEMICAL ROLE OF FOLATE IN CELLULAR METABOLISM*

Wagner, C. (2001) · Clinical Research and Regulatory Affairs · doi:10.1081/crp-100108171 · Cited by 270 · see citing works

Cytoplasmic Serine Hydroxymethyltransferase Mediates Competition between Folate-dependent Deoxyribonucleotide andS-Adenosylmethionine Biosyntheses

Herbig, K., Chiang, E. I., Lee, L.-R., Hills, J., Shane, B., & Stover, P. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m205000200 · Cited by 264 · see citing works

N EW P ERSPECTIVES ON F OLATE C ATABOLISM

Suh, J. R., Herbig, A. K., & Stover, P. J. (2001) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.21.1.255 · Cited by 261 · see citing works

Genetic Polymorphism of 5,10-Methylenetetrahydrofolate Reductase (MTHFR) as a Risk Factor for Coronary Artery Disease

HiroyukiMorita, JunichiTaguchi, HirokiKurihara, MasaoKitaoka, HideakiKaneda, YukikoKurihara, KojiMaemura, TohruMinamino, MinoruOhno, KazuhideYamaoki, et al. (1997) · Circulation · Cited by 261 · see citing works

Searching expressed sequence tag databases: discovery and confirmation of a common polymorphism in the thymidylate synthase gene.

Ulrich, C. M., Bigler, J., Velicer, C. M., Greene, E. A., Farin, F. M., & Potter, J. D. (2000) · PubMed · Cited by 259 · see citing works

... AND ANOTHER

Al-Fallouji, M. A. R. (1983) · The Lancet · doi:10.1016/s0140-6736(83)90305-7 · Cited by 256 · see citing works

PATHOGENESIS OF SUBACUTE COMBINED DEGENERATION: A RESULT OF METHYL GROUP DEFICIENCY

SCOTT, J. (1981) · The Lancet · doi:10.1016/s0140-6736(81)90649-8 · Cited by 254 · see citing works

Genetic Polymorphism of 5,10-Methylenetetrahydrofolate Reductase (MTHFR) as a Risk Factor for Coronary Artery Disease

Morita, H., Taguchi, J., Kurihara, H., Kitaoka, M., Kaneda, H., Kurihara, Y., Maemura, K., Minamino, T., Ohno, M., Yamaoki, K., et al. (1997) · Circulation · doi:10.1161/01.cir.95.8.2032 · Cited by 252 · see citing works

Germ-line variants in methyl-group metabolism genes and susceptibility to DNA methylation in normal tissues and human primary tumors.

Paz, M. F., Avila, S., Fraga, M. F., Pollán, M., Capellá, G., Peinado, M. A., Sánchez‐Céspedes, M., Herman, J. G., & Esteller, M. (2002) · PubMed · Cited by 244 · see citing works

Homocysteine, methylenetetrahydrofolate reductase and risk of schizophrenia: a meta-analysis

Muntjewerff, J.-W., Kahn, R. S., Blom, H. J., & den Heijer, M. (2005) · Molecular Psychiatry · doi:10.1038/sj.mp.4001746 · Cited by 241 · see citing works

Identification and functional analysis of single nucleotide polymorphism in the tandem repeat sequence of thymidylate synthase gene.

Kawakami, K., & Watanabe, G. (2003) · PubMed · Cited by 240 · see citing works

A Polymorphism, R653Q, in the Trifunctional Enzyme Methylenetetrahydrofolate Dehydrogenase/Methenyltetrahydrofolate Cyclohydrolase/Formyltetrahydrofolate Synthetase Is a Maternal Genetic Risk Factor for Neural Tube Defects: Report of the Birth Defects Research Group

Brody, L. C., Conley, M. R., Cox, C., Kirke, P. N., McKeever, M., Mills, J. L., Molloy, A. M., O’Leary, V. B., Parle‐McDermott, A., Scott, J. M., et al. (2002) · The American Journal of Human Genetics · doi:10.1086/344213 · Cited by 234 · see citing works

Folates and pterins

Blakley, R. L., & Benkovic, S. J. (1984) · Wiley eBooks · Cited by 234 · see citing works

Polymorphisms in the thymidylate synthase and serine hydroxymethyltransferase genes and risk of adult acute lymphocytic leukemia

Skibola, C. F., Smith, M. T., Hubbard, A., Shane, B., Roberts, A. C., Law, G. R., Rollinson, S. J., Roman, E., Cartwright, R. A., & Morgan, G. J. (2002) · Blood · doi:10.1182/blood.v99.10.3786 · Cited by 232 · see citing works

A new folate antimetabolite, 5,10-dideaza-5,6,7,8-tetrahydrofolate is a potent inhibitor of de novo purine synthesis

Beardsley, G. P., Moroson, B. A., Taylor, E. C., & Moran, R. G. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31261-9 · Cited by 231 · see citing works

Cell cycle regulation of thymidylate synthetase gene expression in cultured mouse fibroblasts.

Navalgund, L. G., Rossana, C., Muench, A. J., & Johnson, L. F. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)79715-2 · Cited by 225 · see citing works

E2F-1 accumulation bypasses a G1 arrest resulting from the inhibition of G1 cyclin-dependent kinase activity.Preprint

DeGregori, J. V., Leone, G. W., Ohtani, K., Miron, A., & Nevins, J. R. (1995) · Genes & Development · doi:10.1101/gad.9.23.2873 · Cited by 209 · see citing works

Migraine and MTHFR C677T genotype in a population‐based sample

Scher, I., Terwindt, G. M., Verschuren, W. M. M., Kruit, M. C., Blom, H. J., Kowa, H., Frants, R. R., van den Maagdenberg, A. M. J. M., van Buchem, M. A., Ferrari, M. D., et al. (2005) · Annals of Neurology · doi:10.1002/ana.20755 · Cited by 208 · see citing works

A Functional Screen for Myc-Responsive Genes Reveals Serine Hydroxymethyltransferase, a Major Source of the One-Carbon Unit for Cell Metabolism

Nikiforov, M. A., Chandriani, S. J., O’Connell, B. C., Petrenko, O., Kotenko, I., Beavis, A. J., Sedivy, J. M., & Cole, M. D. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.16.5793-5800.2002 · Cited by 201 · see citing works

Role of linkers in communication between protein modules

Gokhale, R. S., & Khosla, C. (2000) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(99)00046-0 · Cited by 196 · see citing works

The anti-inflammatory mechanism of sulfasalazine is related to adenosine release at inflamed sites

Gadangi, P. K., Longaker, M. T., Naime, D., Levin, R. I., Recht, P. A., Montesinos, M. C., Buckley, M. T., Carlin, G., & Cronstein, B. N. (1996) · The Journal of Immunology · doi:10.4049/jimmunol.156.5.1937 · Cited by 196 · see citing works

FOLATE CHEMISTRY AND METABOLISM*

Shane, B. (2001) · Clinical Research and Regulatory Affairs · doi:10.1081/crp-100108170 · Cited by 190 · see citing works

Human Methionine Synthase

Chen, L. H., Liu, M., Hwang, H., Chen, S. L., Korenberg, J. R., & Shane, B. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.6.3628 · Cited by 183 · see citing works

Cloning of human cDNAs encoding mitochondrial and cytosolic serine hydroxymethyltransferases and chromosomal localization

Garrow, T. A., Brenner, A., Whitehead, V. M., Chen, X. N., Duncan, R., Korenberg, J. R., & Shane, B. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)50286-1 · Cited by 179 · see citing works

The crystal structure of human cytosolic serine hydroxymethyltransferase: a target for cancer chemotherapy

RENWICK, S. B., Snell, K., & Baumann, U. (1998) · Structure · doi:10.1016/s0969-2126(98)00112-9 · Cited by 178 · see citing works

Polymorphism of the thymidylate synthase gene and outcome of acute lymphoblastic leukaemia

Krajinović, M., Costea, I., & Chiasson, S. (2002) · The Lancet · doi:10.1016/s0140-6736(02)08065-0 · Cited by 173 · see citing works

Thermolabile methylenetetrahydrofolate reductase in patients with coronary artery disease

Kang, S., WONG, P. W. K., Zhou, J., Sora, J., Lessick, M. L., Ruggie, N., & Grcevich, G. (1988) · Metabolism · doi:10.1016/0026-0495(88)90076-5 · Cited by 171 · see citing works

Cobalamin-Dependent Methionine Synthase Is a Modular Protein with Distinct Regions for Binding Homocysteine, Methyltetrahydrofolate, Cobalamin, and Adenosylmethionine

Goulding, C. W., Postigo, D., & Matthews, R. G. (1997) · Biochemistry · doi:10.1021/bi9705164 · Cited by 167 · see citing works

Homocysteine and atherosclerosis

Gerhard, G. T., & Duell, P. B. (1999) · Current Opinion in Lipidology · doi:10.1097/00041433-199910000-00006 · Cited by 167 · see citing works

Rapid incorporation of label from ribonucleoside disphosphates into DNA by a cell-free high molecular weight fraction from animal cell nuclei

Noguchi, H., Reddy, G. P. V., & Pardee, A. B. (1983) · Cell · doi:10.1016/0092-8674(83)90464-6 · Cited by 165 · see citing works

Targeted Disruption of the Methionine Synthase Gene in Mice

Swanson, D. A., Liu, M., Baker, P. J., Garrett, L. J., Stitzel, M. L., Wu, J., Harris, M., Banerjee, R. V., Shane, B., & Brody, L. C. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.4.1058-1065.2001 · Cited by 162 · see citing works

Folate and Cancer Prevention: A New Medical Application of Folate Beyond Hyperhomocysteinemia and Neural Tube Defects

Kim, Y. I. (2009) · Nutrition Reviews · doi:10.1111/j.1753-4887.1999.tb06905.x · Cited by 162 · see citing works

AICA-Ribosiduria: A Novel, Neurologically Devastating Inborn Error of Purine Biosynthesis Caused by Mutation of ATIC

Marie, S., Héron, B., Bitoun, P., Timmerman, T., Berghe, G., & Vincent, M. (2004) · The American Journal of Human Genetics · doi:10.1086/421475 · Cited by 159 · see citing works

Serine hydroxymethyltransferase revisited

Schirch, V., & Szebenyi, D. M. E. (2005) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2005.08.017 · Cited by 156 · see citing works

Allosteric inhibition of methylenetetrahydrofolate reductase by adenosylmethionine. Effects of adenosylmethionine and NADPH on the equilibrium between active and inactive forms of the enzyme and on the kinetics of approach to equilibrium.

Jencks, D. A., & Mathews, R. G. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)61530-3 · Cited by 153 · see citing works

Interaction of folylpolyglutamates with enzymes in one-carbon metabolism

Schirch, V., & Strong, W. B. (1989) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(89)90120-3 · Cited by 152 · see citing works

Tracer-derived total and folate-dependent homocysteine remethylation and synthesis rates in humans indicate that serine is the main one-carbon donor

Davis, S. R., Stacpoole, P. W., Williamson, J., Kick, L. S., Quinlivan, E. P., Coats, B. S., Shane, B., Bailey, L. B., & Gregory, J. F. (2004) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00351.2003 · Cited by 149 · see citing works

Targeting Ras signaling through inhibition of carboxyl methylation: An unexpected property of methotrexate

Winter-Vann, A. M., Kamen, B. A., Bergö, M. O., Young, S. G., Melnyk, S., James, S. J., & Casey, P. J. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1135239100 · Cited by 146 · see citing works

Mechanism of reductive activation of cobalamin-dependent methionine synthase: an electron paramagnetic resonance spectroelectrochemical study

Banerjee, R. V., Harder, S. R., Ragsdale, S. W., & Matthews, R. G. (1990) · Biochemistry · doi:10.1021/bi00457a005 · Cited by 146 · see citing works

Methionine synthase (MTR) 2756 (A → G) polymorphism, double heterozygosity methionine synthase 2756 AG/methionine synthase reductase (MTRR) 66 AG, and elevated homocysteinemia are three risk factors for having a child with Down syndrome

Bosco, P., Guéant‐Rodriguez, R., Anello, G., Barone, C., Namour, F., Caraci, F., Romano, A. G., Romano, C., & Guéant, J. (2003) · American Journal of Medical Genetics Part A · doi:10.1002/ajmg.a.20234 · Cited by 145 · see citing works

Maternal Genetic Effects, Exerted by Genes Involved in Homocysteine Remethylation, Influence the Risk of Spina Bifida

Doolin, M.-T., Barbaux, S., McDonnell, M., Hoess, K., Whitehead, A. S., & Mitchell, L. E. (2002) · The American Journal of Human Genetics · doi:10.1086/344209 · Cited by 143 · see citing works

Gene–gene interaction in folate-related genes and risk of neural tube defects in a UK population

Relton, C. L., Wilding, C. S., Pearce, M. S., Laffling, A. J., Jonas, P. A., Lynch, S. A., Tawn, E. J., & Burn, J. (2004) · Journal of Medical Genetics · doi:10.1136/jmg.2003.010694 · Cited by 143 · see citing works

Serine hydroxymethyltransferase catalyzes the hydrolysis of 5,10-methenyltetrahydrofolate to 5-formyltetrahydrofolate

Stover, P., & Schirch, V. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)77290-6 · Cited by 139 · see citing works

Nucleotide sequence of a functional cDNA for human thymidylate synthase

Takeishi, K., Kaneda, S., Ayusawa, D., Shimizu, K., Gotoh, O., & Seno, T. (1985) · Nucleic Acids Research · doi:10.1093/nar/13.6.2035 · Cited by 139 · see citing works

Thymidylate synthase: a novel genetic determinant of plasma homocysteine and folate levels

Trinh, B. N., Ong, C. N., Coetzee, G. A., Yu, M. C., & Laird, P. W. (2002) · Human Genetics · doi:10.1007/s00439-002-0779-2 · Cited by 139 · see citing works

The effect of methotrexate on intracellular folate pools in human MCF-7 breast cancer cells. Evidence for direct inhibition of purine synthesis.

Allegra, C. J., Fine, R. L., Drake, J. C., & Chabner, B. A. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)84587-8 · Cited by 137 · see citing works

Is Mutated Serine Hydroxymethyltransferase (SHMT) Involved in the Etiology of Neural Tube Defects?

Heil, S. G., van der Put, N. M. J., Waas, E. T., den Heijer, M., Trijbels, F. J. M., & Blom, H. J. (2001) · Molecular Genetics and Metabolism · doi:10.1006/mgme.2001.3175 · Cited by 135 · see citing works

5-Formyltetrahydrofolate polyglutamates are slow tight binding inhibitors of serine hydroxymethyltransferase

Stover, P. J., & Schirch, V. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)52328-0 · Cited by 132 · see citing works

The metabolic role of leucovorin

Stover, P. J., & Schirch, V. (1993) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(93)90162-g · Cited by 131 · see citing works

Retrovirally Mediated Complementation of the glyBPhenotype

Titus, S. A., & Moran, R. G. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m005163200 · Cited by 130 · see citing works

Mitochondrial one‐carbon metabolism is adapted to the specific needs of yeast, plants and mammals

Christensen, K. E., & MacKenzie, R. E. (2006) · BioEssays · doi:10.1002/bies.20420 · Cited by 127 · see citing works

Evidence for Small Ubiquitin-like Modifier-dependent Nuclear Import of the Thymidylate Biosynthesis Pathway

Woeller, C. F., Anderson, D. D., Szebenyi, D. M. E., & Stover, P. J. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702526200 · Cited by 123 · see citing works

Characterization of the Zinc Binding Site in Methionine Synthase Enzymes of Escherichia coli: The Role of Zinc in the Methylation of Homocysteine

Peariso, K., Goulding, C. W., Huang, S., Matthews, R. G., & Penner‐Hahn, J. E. (1998) · Journal of the American Chemical Society · doi:10.1021/ja980581g · Cited by 123 · see citing works

Cell-cycle-directed regulation of thymidylate synthase messenger RNA in human diploid fibroblasts stimulated to proliferate

Ayusawa, D., Shimizu, K., Koyama, H., Kaneda, S., Takeishi, K., & Seno, T. (1986) · Journal of Molecular Biology · doi:10.1016/0022-2836(86)90241-x · Cited by 123 · see citing works

Formyl-methyl-methylenetetrahydrofolate synthetase-(combined). An ovine protein with multiple catalytic activities.

Paukert, J. L., Straus, L. D., & Rabinowitz, J. C. (1976) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)33224-6 · Cited by 122 · see citing works

Mitochondrial NAD-Dependent Methylenetetrahydrofolate Dehydrogenase-Methenyltetrahydrofolate Cyclohydrolase Is Essential for Embryonic Development

Pietro, E. D., Sirois, J., Tremblay, M. L., & MacKenzie, R. E. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.12.4158-4166.2002 · Cited by 120 · see citing works

[84] Methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase-formyltetrahydrofolate synthetase: A multifunctional protein from porcine liver

MacKenzie, R. E., & Tan, L. U. L. (1980) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(80)66514-8 · Cited by 118 · see citing works

Associations between polymorphisms in the thymidylate synthase and serine hydroxymethyltransferase genes and susceptibility to malignant lymphoma.

Hishida, A., Matsuo, K., Hamajima, N., Ito, H. M., Ogura, M., Kagami, Y., Taji, H., Morishima, Y., Emi, N., & Tajima, K. (2003) · PubMed · Cited by 118 · see citing works

Elevation of thymidylate synthase following 5-fluorouracil treatment is prevented by the addition of leucovorin in murine colon tumors.

van der Wilt, C. L., Pinedo, H. M., Smid, K., & Peters, G. J. (1992) · PubMed · Cited by 118 · see citing works

Cloning of three human multifunctional de novo purine biosynthetic genes by functional complementation of yeast mutations.

Schild, D., Brake, A. J., Kiefer, M. C., Young, D., & Barr, P. J. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.8.2916 · Cited by 116 · see citing works

5-Formyltetrahydrofolate Regulates Homocysteine Remethylation in Human Neuroblastoma

Girgis, S., Suh, J. R., Jolivet, J., & Stover, P. J. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.8.4729 · Cited by 109 · see citing works

Control of Thymidylate Synthase mRNA Content and Gene Transcription in an Overproducing Mouse Cell Line

Jenh, C., Geyer, P., & Johnson, L. F. (1985) · Molecular and Cellular Biology · doi:10.1128/mcb.5.10.2527-2532.1985 · Cited by 107 · see citing works

Confirmation of the R653Q polymorphism of the trifunctional C1-synthase enzyme as a maternal risk for neural tube defects in the Irish population

Parle‐McDermott, A., Kirke, P. N., Mills, J. L., Molloy, A. M., Cox, C., O’Leary, V. B., Pangilinan, F., Conley, M. R., Cleary, L., Brody, L. C., et al. (2006) · European Journal of Human Genetics · doi:10.1038/sj.ejhg.5201603 · Cited by 107 · see citing works

Effect of nitrous oxide inactivation of vitamin B12-dependent methionine synthetase on the subcellular distribution of folate coenzymes in rat liver

Horne, D. W., Patterson, D., & Cook, R. J. (1989) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(89)90556-0 · Cited by 107 · see citing works

Regulation of Folate-mediated One-carbon Metabolism by 10-Formyltetrahydrofolate Dehydrogenase

Anguera, M. C., Field, M. S., Perry, C. A., Ghandour, H., Chiang, E. I., Selhub, J., Shane, B., & Stover, P. J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m510623200 · Cited by 106 · see citing works

Higher levels of thymidylate synthase gene expression are observed in pulmonary as compared with hepatic metastases of colorectal adenocarcinoma.

Gorlick, R. G., Metzger, R., Danenberg, K. D., Salonga, D. S., Miles, J. S., Longo, G., Fu, J. P., Banerjee, D., Klimstra, D. S., Jhanwar, S. C., et al. (1998) · Journal of Clinical Oncology · doi:10.1200/jco.1998.16.4.1465 · Cited by 106 · see citing works

Molecular cloning, characterization and alternative splicing of the human cytoplasmic serine hydroxymethyltransferase gene

Girgis, S., Nasrallah, I. M., Suh, J. R., Oppenheim, E. W., Zanetti, K. A., Mastri, M. G., & Stover, P. J. (1998) · Gene · doi:10.1016/s0378-1119(98)00085-7 · Cited by 105 · see citing works

Enzymatic properties of dimethylglycine dehydrogenase and sarcosine dehydrogenase from rat liver

Porter, D. H., Cook, R., & Wagner, C. (1985) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(85)90516-8 · Cited by 103 · see citing works

Atypical variants of nonketotic hyperglycinemia

Dinopoulos, A., Matsubara, Y., & Kure, S. (2005) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2005.07.016 · Cited by 103 · see citing works

Association of Polymorphisms in One-Carbon Metabolism Genes and Postmenopausal Breast Cancer Incidence

Stevens, V. L., McCullough, M. L., Pavluck, A., Talbot, J. T., Feigelson, H. S., Thun, M. J., & Calle, E. E. (2007) · Cancer Epidemiology Biomarkers & Prevention · doi:10.1158/1055-9965.epi-06-1037 · Cited by 103 · see citing works

Methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase-formyltetrahydrofolate synthetase. A multifunctional protein from porcine liver.

Tan, L. U. L., Drury, E. J., & MacKenzie, R. E. (1977) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)75214-4 · Cited by 101 · see citing works

A meta‐analysis of the MTHFR C677T polymorphism and schizophrenia risk

Lewis, S. J., Zammit, S., Gunnell, D., & Smith, G. D. (2005) · American Journal of Medical Genetics Part B Neuropsychiatric Genetics · doi:10.1002/ajmg.b.30170 · Cited by 100 · see citing works

Regulation of folate and one-carbon metabolism in mammalian cells. III. Role of mitochondrial folylpoly-gamma-glutamate synthetase.

Lin, B., Huang, R., & Shane, B. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)80594-8 · Cited by 95 · see citing works

Low erythrocyte folate status and polymorphic variation in folate-related genes are associated with risk of neural tube defect pregnancy

Relton, C. L., Wilding, C. S., Laffling, A. J., Jonas, P. A., Burgess, T., Binks, K., Tawn, E. J., & Burn, J. (2004) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2003.12.010 · Cited by 95 · see citing works

Isolation and characterization of cDNA clones for rat liver 10-formyltetrahydrofolate dehydrogenase.

Cook, R., Lloyd, R. S., & Wagner, C. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)67743-4 · Cited by 93 · see citing works

Red blood cell methylfolate and plasma homocysteine as risk factors for venous thromboembolism: a matched case-control study

Quéré, I., Perneger, T., Zittoun, J., Bellet, H., Gris, J., Daurès, J., Schved, J., Mercier, É., Laroche, J.-P., Dauzat, M., et al. (2002) · The Lancet · doi:10.1016/s0140-6736(02)07876-5 · Cited by 92 · see citing works

Regulation of human methylenetetrahydrofolate reductase by phosphorylation

Yamada, K., Strahler, J. R., Andrews, P., & Matthews, R. G. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0504786102 · Cited by 90 · see citing works

Retinoblastoma Tumor Suppressor Targets dNTP Metabolism to Regulate DNA Replication

Angus, S. P., Wheeler, L. J., Ranmal, S. A., Zhang, X., Markey, M. P., Mathews, C. K., & Knudsen, E. S. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m205911200 · Cited by 87 · see citing works

Maternal MTR genotype contributes to the risk of non‐syndromic cleft lip and palate in the Polish population

Mostowska, A., Hozyasz, K. K., & Jagodziński, P. P. (2006) · Clinical Genetics · doi:10.1111/j.1399-0004.2006.00618.x · Cited by 86 · see citing works

Interaction Between Hyperhomocysteinemia, Mutated Methylenetetrahydrofolatereductase (MTHFR) and Inherited Thrombophilic Factors in Recurrent Venous Thrombosis

Keijzer, M. B. A. J., Blom, H. J., Bos, G. M. J., Willems, H., Gerrits, W. B. J., Rosendaal, F. R., & den Heijer, M. (2002) · Thrombosis and Haemostasis · doi:10.1055/s-0037-1613292 · Cited by 85 · see citing works

Neural tube defects and a disturbed folate dependent homocysteine metabolism

van der Put, N. M. J., & Blom, H. J. (2000) · European Journal of Obstetrics & Gynecology and Reproductive Biology · doi:10.1016/s0301-2115(00)00426-7 · Cited by 84 · see citing works

Crystal Structure of Binary and Ternary Complexes of Serine Hydroxymethyltransferase from Bacillus stearothermophilus

Trivedi, V., Gupta, A., Jala, V. R., Saravanan, P., Rao, G. S. J., Rao, N. A., Savithri, H. S., & Subramanya, H. S. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m111976200 · Cited by 83 · see citing works

Reversion of a Chinese Hamster Cell Auxotrophic Mutant

Chasin, L. A., Feldman, A., Konstam, M., & Urlaub, G. (1974) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.71.3.718 · Cited by 81 · see citing works

Lung cancer risk in families of nonsmoking probands: Heterogeneity by age at diagnosis

Yang, P., Schwartz, A. G., McAllister, A. E., Swanson, G. M., & Aston, C. E. (1999) · Genetic Epidemiology · doi:10.1002/(sici)1098-2272(199911)17:4 · Cited by 80 · see citing works

Ligand-mediated Induction of Thymidylate Synthase Occurs by Enzyme Stabilization

Kitchens, M. E., Forsthoefel, A. M., Rafique, Z., Spencer, H. T., & Berger, F. G. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.18.12544 · Cited by 79 · see citing works

De novopurine nucleotide biosynthesis: cloning of human and avian cDNAs encoding the trifunctional glycinamide ribonucleotide synthetase-aminoimidazole ribonucleotide synthetase-glycinamide ribonucleotide transformylase by functional complementation inE.coli

Aimi, J., Qiu, H., Williams, J. S., Zalkin, H., & Dixon, J. E. (1990) · Nucleic Acids Research · doi:10.1093/nar/18.22.6665 · Cited by 79 · see citing works

Tetrahydropteroylpolyglutamate derivatives as substrates of two multifunctional proteins with folate-dependent enzyme activities

MacKenzie, R. E., & Baugh, C. M. (1980) · Biochimica et Biophysica Acta (BBA) - Enzymology · doi:10.1016/0005-2744(80)90054-6 · Cited by 78 · see citing works

Roles of folylpoly-gamma-glutamate synthetase in therapeutics with tetrahydrofolate antimetabolites: an overview.

Rg, M. (1999) · PubMed · Cited by 78 · see citing works

Structure of a Murine Cytoplasmic Serine Hydroxymethyltransferase Quinonoid Ternary Complex: Evidence for Asymmetric Obligate Dimers

Szebenyi, D. M. E., Liu, X., Kriksunov, I. A., Stover, P. J., & Thiel, D. J. (2000) · Biochemistry · doi:10.1021/bi000635a · Cited by 77 · see citing works

The Human GARS-AIRS-GART Gene Encodes Two Proteins Which Are Differentially Expressed during Human Brain Development and Temporally Overexpressed in Cerebellum of Individuals with Down Dyndrome

Brodsky, G. L., Barnes, T. S., Bleskan, J. H., Becker, L. E., Cox, M., & Patterson, D. (1997) · Human Molecular Genetics · doi:10.1093/hmg/6.12.2043 · Cited by 76 · see citing works

UROCANIC ACID AS AN INTERMEDIATE IN THE ENZYMATIC CONVERSION OF HISTIDINE TO GLUTAMIC AND FORMIC ACIDS

Tabor, H., Mehler, A. H., Hayaishi, O., & White, J. (1952) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)55711-2 · Cited by 75 · see citing works

Serine Hydroxymethyltransferase: Role of Glu75 and Evidence that Serine Is Cleaved by a Retroaldol Mechanism

Szebenyi, D. M. E., Musayev, F. N., di Salvo, M. L., Safo, M. K., & Schirch, V. (2004) · Biochemistry · doi:10.1021/bi049791y · Cited by 74 · see citing works

Formyl-methenyl-methylenetetrahydrofolate synthetase from rabbit liver (combined)

Schirch, L. (1978) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(78)90214-x · Cited by 74 · see citing works

Inhibition of the mammalian transcription factor LSF induces S‐phase‐dependent apoptosis by downregulating thymidylate synthase expression

Powell, C. M. H., Rudge, T. L., Zhu, Q., Johnson, L. F., & Hansen, U. M. (2000) · The EMBO Journal · doi:10.1093/emboj/19.17.4665 · Cited by 72 · see citing works

Towards Structure-based Drug Design: Crystal Structure of a Multisubstrate Adduct Complex of Glycinamide Ribonucleotide Transformylase at 1.96 Å Resolution

Klein, C., Chen, P., Arevalo, J. H., Stura, E. A., Marolewski, A. E., Warren, M. S., Benkovic, S. J., & Wilson, I. A. (1995) · Journal of Molecular Biology · doi:10.1006/jmbi.1995.0286 · Cited by 71 · see citing works

Folate-based thymidylate synthase inhibitors in cancer chemotherapy

Takemura, Y., & Jackman, A. L. (1997) · Anti-Cancer Drugs · doi:10.1097/00001813-199701000-00001 · Cited by 71 · see citing works

Evaluation of a methylenetetrahydrofolate-dehydrogenase 1958G>A polymorphism for neural tube defect risk

Marco, P. D., Merello, E., Calevo, M. G., Mascelli, S., Raso, A., Cama, A., & Capra, V. (2005) · Journal of Human Genetics · doi:10.1007/s10038-005-0329-6 · Cited by 70 · see citing works

Cloning of Dimethylglycine Dehydrogenase and a New Human Inborn Error of Metabolism, Dimethylglycine Dehydrogenase Deficiency

Binzak, B. A., Wevers, R. A., Moolenaar, S. H., Lee, Y., Hwu, W., Poggi-Bach, J., Engelke, U. F. H., Hoard-Fruchey, H. M., Vockley, J. G., & Vockley, J. (2001) · The American Journal of Human Genetics · doi:10.1086/319520 · Cited by 70 · see citing works

Hyperhomocysteinemia, methylenetetrahydrofolate reductase 677TT genotype, and the risk for schizophrenia: A dutch population based case‐control study

Muntjewerff, J.-W., Hoogendoorn, M. L. C., Kahn, R. S., Sinke, R. J., den Heijer, M., Kluijtmans, L. A. J., & Blom, H. J. (2005) · American Journal of Medical Genetics Part B Neuropsychiatric Genetics · doi:10.1002/ajmg.b.30179 · Cited by 70 · see citing works

A polymorphism in the MTHFD1 gene increases a mother’s risk of having an unexplained second trimester pregnancy loss

Parle‐McDermott, A., Pangilinan, F., Mills, J. L., Signore, C. C., Molloy, A. M., Cotter, A. M., Conley, M. R., Cox, C., Kirke, P. N., Scott, J. M., et al. (2005) · Molecular Human Reproduction · doi:10.1093/molehr/gah204 · Cited by 69 · see citing works

Glycine Turnover and Decarboxylation Rate Quantified in Healthy Men and Women Using Primed, Constant Infusions of [1,2-13C2]Glycine and [2H3]Leucine ,

Lamers, Y., Williamson, J., Gilbert, L. R., Stacpoole, P. W., & Gregory, J. F. (2007) · Journal of Nutrition · doi:10.1093/jn/137.12.2647 · Cited by 66 · see citing works

PURINE FERMENTATION BY CLOSTRIDIUM CYLINDROSPORUM

Rabinowitz, J. C., & Pricer, W. E. (1956) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)89914-1 · Cited by 66 · see citing works

Crystal Structures of the Carboxyl Terminal Domain of Rat 10-Formyltetrahydrofolate Dehydrogenase: Implications for the Catalytic Mechanism of Aldehyde Dehydrogenases

Tsybovsky, Y., DONATO, H. J., Krupenko, N. I., Davies, C., & Krupenko, S. A. (2007) · Biochemistry · doi:10.1021/bi0619573 · Cited by 66 · see citing works

The molecular basis of glutamate formiminotransferase deficiency

Hilton, J. F., Christensen, K. E., Watkins, D., Raby, B. A., Renaud, Y., de la Luna, S., Estivill, X., MacKenzie, R. E., Hudson, T. J., & Rosenblatt, D. S. (2003) · Human Mutation · doi:10.1002/humu.10236 · Cited by 66 · see citing works

Chromosome breakage induced by thymidylate stress in thymidylate synthase-negative mutants of mouse FM3A cells.

Hori, T.-A., Ayusawa, D., Shimizu, K., Koyama, H., & Seno, T. (1984) · PubMed · Cited by 66 · see citing works

Structural Perturbations in the Ala → Val Polymorphism of Methylenetetrahydrofolate Reductase: How Binding of Folates May Protect against Inactivation,

Pejchal, R., Campbell, E. A., Guenther, B. D., Lennon, B. W., Matthews, R. G., & Ludwig, M. L. (2006) · Biochemistry · doi:10.1021/bi052294c · Cited by 65 · see citing works

Heavy Chain Ferritin Enhances Serine Hydroxymethyltransferase Expression and de Novo Thymidine Biosynthesis

Oppenheim, E. W., Adelman, C. A., Liu, X., & Stover, P. J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100039200 · Cited by 65 · see citing works

Methenyltetrahydrofolate Synthetase Regulates Folate Turnover and Accumulation

Anguera, M. C., Suh, J. R., Ghandour, H., Nasrallah, I. M., Selhub, J., & Stover, P. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302883200 · Cited by 65 · see citing works

Thymidylate Synthetase Activity in Cultured Mammalian Cells

Conrad, A. H. (1971) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)76977-4 · Cited by 65 · see citing works

The human and mouse methylenetetrahydrofolate reductase (MTHFR) genes: genomic organization, mRNA structure and linkage to the CLCN6 gene

Gaughan, D. J., Barbaux, S., Kluijtmans, L. A. J., & Whitehead, A. S. (2000) · Gene · doi:10.1016/s0378-1119(00)00392-9 · Cited by 65 · see citing works

Small ubiquitin-like modifier-1 (SUMO-1) modification of thymidylate synthase and dihydrofolate reductase

Anderson, D. D., Woeller, C. F., & Stover, P. J. (2007) · Clinical Chemistry and Laboratory Medicine (CCLM) · doi:10.1515/cclm.2007.355 · Cited by 63 · see citing works

Interaction of mitochondrial initiation factor 2 with mitochondrial fMet-tRNA

Spencer, A. C. (2004) · Nucleic Acids Research · doi:10.1093/nar/gkh886 · Cited by 61 · see citing works

Multiple transcription start sites and alternative splicing in the methylenetetrahydrofolate reductase gene result in two enzyme isoforms

Tran, P. V., Leclerc, D., Chan, M., Pai, A., Hiou-Tim, F., Wu, Q. H., Goyette, P., Artigas, C., Milos, R., & Rozen, R. R. (2002) · Mammalian Genome · doi:10.1007/s00335-002-2167-6 · Cited by 61 · see citing works

Human Mitochondrial C1-Tetrahydrofolate Synthase

Prasannan, P., Pike, S., Peng, K., Shane, B., & Appling, D. R. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304319200 · Cited by 60 · see citing works

In silico experimentation with a model of hepatic mitochondrial folate metabolism

Nijhout, H. F., Reed, M. C., Lam, S.-L., Shane, B., Gregory, J. F., & Ulrich, C. M. (2006) · Theoretical Biology and Medical Modelling · doi:10.1186/1742-4682-3-40 · Cited by 59 · see citing works

Metabolic Compartmentation

Spivey, H. O., & Merz, J. M. (1989) · BioEssays · doi:10.1002/bies.950100409 · Cited by 59 · see citing works

On the cofactor specificity of glycinamide ribonucleotide and 5-aminoimidazole-4-carboxamide ribonucleotide transformylase from chicken liver

Smith, G. K., Mueller, W. T., Benkovic, P. A., & Benkovic, S. J. (1981) · Biochemistry · doi:10.1021/bi00508a029 · Cited by 59 · see citing works

In vitro conversion of formate to serine: effect of tetrahydropteroylpolyglutamates and serine hydroxymethyltransferase on the rate of 10-formyltetrahydrofolate synthetase

Strong, W. B., & Schirch, V. (1989) · Biochemistry · doi:10.1021/bi00450a028 · Cited by 59 · see citing works

A common insertion/deletion polymorphism of the thymidylate synthase (TYMS) gene is a determinant of red blood cell folate and homocysteine concentrations

Kealey, C., Brown, K. S., Woodside, J. V., Young, I. S., Murray, L., Boreham, C. A., McNulty, H., Strain, J., McPartlin, J. M., Scott, J. M., et al. (2005) · Human Genetics · doi:10.1007/s00439-004-1243-2 · Cited by 58 · see citing works

MTHFD1 R653Q polymorphism is a maternal genetic risk factor for severe abruptio placentae

Parle‐McDermott, A., Mills, J. L., Kirke, P. N., Cox, C., Signore, C. C., Kirke, S., Molloy, A. M., O’Leary, V. B., Pangilinan, F., O’Herlihy, C., et al. (2005) · American Journal of Medical Genetics Part A · doi:10.1002/ajmg.a.30354 · Cited by 58 · see citing works

Regulation of de Novo Purine Biosynthesis by Methenyltetrahydrofolate Synthetase in Neuroblastoma

Field, M. S., Szebenyi, D. M. E., & Stover, P. J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m510624200 · Cited by 57 · see citing works

Mammalian Mitochondrial Methionyl-tRNA Transformylase from Bovine Liver

Takeuchi, N., Kawakami, M., Omori, A., Ueda, T., Spremulli, L. L., & Watanabe, K. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.24.15085 · Cited by 57 · see citing works

Characterization of the folate-dependent mitochondrial oxidation of carbon 3 of serine

Garcı́a-Martı́nez, L. F., & Appling, D. R. (1993) · Biochemistry · doi:10.1021/bi00068a027 · Cited by 56 · see citing works

Effect of vitamin B6 availability on serine hydroxymethyltransferase in MCF-7 cells

Perry, C. A., Yu, S., Chen, J., Matharu, K., & Stover, P. J. (2007) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2007.04.005 · Cited by 56 · see citing works

Glycine cleavage system in neurogenic regions

Ichinohe, A., Kure, S., Mikawa, S., Ueki, T., Kojima, K., Fujiwara, K., Iinuma, K., Matsubara, Y., & Sato, K. (2004) · European Journal of Neuroscience · doi:10.1111/j.0953-816x.2004.03345.x · Cited by 55 · see citing works

Intracellular Location of Thymidylate Synthase and Its State of Phosphorylation

Samsonoff, W. A., Reston, J. T., McKee, M. L., O'Connor, B. M., Galivan, J. H., Maley, G. F., & Maley, F. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.20.13281 · Cited by 55 · see citing works

Inhibition of progression of aberrant crypt foci and colon tumor development by vitamin E and β-carotene in rats on a high-risk diet

Shivapurkar, N., Tang, Z., Frost, A. R., & Alabaster, O. (1995) · Cancer Letters · doi:10.1016/0304-3835(95)03729-g · Cited by 53 · see citing works

The MTHFR 1298CC and 677TT genotypes have opposite associations with red cell folate levels

Parle‐McDermott, A., Mills, J. L., Molloy, A. M., Carroll, N., Kirke, P. N., Cox, C., Conley, M. R., Pangilinan, F., Brody, L. C., & Scott, J. M. (2006) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2006.02.011 · Cited by 53 · see citing works

Dependence of mitochondrial protein synthesis initiation on formylation of the initiator methionyl-tRNAf.

Bianchetti, R., Lucchini, G., Crosti, P., & Tortora, P. (1977) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)40489-3 · Cited by 53 · see citing works

Disruption of the Mthfd1 Gene Reveals a Monofunctional 10-Formyltetrahydrofolate Synthetase in Mammalian Mitochondria

Christensen, K. E., Patel, H., Kuzmanov, U., Mejia, N. R., & MacKenzie, R. E. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m409380200 · Cited by 52 · see citing works

Variable contribution of the MTHFR C677T polymorphism to non‐syndromic cleft lip and palate risk in China

Zhu, J., Ren, A., Hao, L., Lijun, P., Liu, J., Zhu, H., Li, S., Finnell, R. H., & Li, Z. (2006) · American Journal of Medical Genetics Part A · doi:10.1002/ajmg.a.31115 · Cited by 50 · see citing works

The metabolism of serine and glycine in mutant lines of Chinese hamster ovary cells

Pfendner, W., & Pizer, L. I. (1980) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(80)90382-3 · Cited by 50 · see citing works

Methylation demand and homocysteine metabolism

Stead, L. M., Jacobs, R. L., Brosnan, M. E., & Brosnan, J. T. (2004) · Advances in Enzyme Regulation · doi:10.1016/j.advenzreg.2003.11.012 · Cited by 49 · see citing works

Structural Determinants for the Intracellular Degradation of Human Thymidylate Synthase

Forsthoefel, A. M., Peña, M. M. O., Xing, Y., Rafique, Z., & Berger, F. G. (2004) · Biochemistry · doi:10.1021/bi035894p · Cited by 49 · see citing works

Natural antisense (rTSalpha) RNA induces site-specific cleavage of thymidylate synthase mRNA.

Chu, J., & Dolnick, B. (2002) · Biochimica et Biophysica Acta · doi:10.1016/s0925-4439(02)00081-9 · Cited by 49 · see citing works

Activities of Hepatic Cytosolic and Mitochondrial Forms of Serine Hydroxymethyltransferase and Hepatic Glycine Concentration Are Affected by Vitamin B-6 Intake in Rats

Scheer, J. B., Mackey, A. D., & Gregory, J. F. (2005) · Journal of Nutrition · doi:10.1093/jn/135.2.233 · Cited by 48 · see citing works

Associations between polymorphisms within the thymidylate synthase gene and spina bifida

Volcik, K. A., Shaw, G. M., Zhu, H., Lammer, E. J., Laurent, C. A., & Finnell, R. H. (2003) · Birth Defects Research Part A Clinical and Molecular Teratology · doi:10.1002/bdra.10029 · Cited by 48 · see citing works

Cloning the full-length cDNA for rat connective tissue growth factor: Implications for skeletal development

Xu, J., Smock, S. L., Safadi, F. F., Rosenzweig, A. B., Odgren, P. R., Marks, S. C., Owen, T. A., & Popoff, S. N. (2000) · Journal of Cellular Biochemistry · doi:10.1002/(sici)1097-4644(20000401)77:1 · Cited by 48 · see citing works

Identification of folate binding protein of mitochondria as dimethylglycine dehydrogenase.

Wittwer, A. J., & Wagner, C. (1980) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.77.8.4484 · Cited by 47 · see citing works

Polymorphisms in Cytoplasmic Serine Hydroxymethyltransferase and Methylenetetrahydrofolate Reductase Affect the Risk of Cardiovascular Disease in Men

Lim, U., Peng, K., Shane, B., Stover, P. J., Litonjua, A. A., Weiss, S. T., Gaziano, J. M., Strawderman, R. L., Raiszadeh, F., Selhub, J., et al. (2005) · Journal of Nutrition · doi:10.1093/jn/135.8.1989 · Cited by 46 · see citing works

Purification and properties of serine hydroxymethyltransferase and C1-tetrahydrofolate synthase from L1210 cells.

Strong, W. B., Tendler, S. J. B., Seither, R. L., Goldman, I. D., & Schirch, V. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)38324-3 · Cited by 45 · see citing works

Nuclear thymidylate synthase expression, p53 expression and 5FU response in colorectal carcinoma

Wong, N. A. C. S., Brett, L., Stewart, M., Leitch, A., Longley, D. B., Dunlop, M. G., Johnston, P. G., Lessells, A. M., & Jodrell, D. I. (2001) · British Journal of Cancer · doi:10.1054/bjoc.2001.2175 · Cited by 45 · see citing works

MTHFD 1958G>A and MTR 2756A>G polymorphisms are associated with bipolar disorder and schizophrenia

Kempisty, B., Sikora, J., Lianeri, M., Szczepankiewicz, A., Czerski, P. M., Hauser, J., & Jagodziński, P. P. (2007) · Psychiatric Genetics · doi:10.1097/ypg.0b013e328029826f · Cited by 44 · see citing works

Exclusion of angiotensinogen gene in molecular basis of human hypertension: Sibpair linkage and association analyses in Australian Anglo-Caucasians

Wang, W. Y. S., Glenn, C. L., Zhang, W., Benjafield, A., Nyholt, D. R., & Morris, B. J. (1999) · American Journal of Medical Genetics · doi:10.1002/(sici)1096-8628(19991105)87:1 · Cited by 44 · see citing works

Folate requirements for health in different population groups.

McNulty, H. (1995) · PubMed · Cited by 43 · see citing works

Mimosine Attenuates Serine Hydroxymethyltransferase Transcription by Chelating Zinc

Perry, C. A., Sastry, R., Nasrallah, I. M., & Stover, P. J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m410467200 · Cited by 43 · see citing works

The Kinetic Mechanism of the Human Bifunctional Enzyme ATIC (5-Amino-4-imidazolecarboxamide Ribonucleotide Transformylase/Inosine 5′-Monophosphate Cyclohydrolase)

Bulock, K. G., Beardsley, G. P., & Anderson, K. S. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m111964200 · Cited by 43 · see citing works

The Enzymatic Degradation of Urocanic Acid

Revel, H. R. B., & Magasanik, B. (1958) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)64681-2 · Cited by 43 · see citing works

Formyltetrahydrofolate Synthetase

Himes, R. H., & Rabinowitz, J. C. (1962) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)60250-9 · Cited by 42 · see citing works

Gonadal (ovarian) dysgenesis in 46,XX individuals: Frequency of the autosomal recessive form

Meyers, C. M., Boughman, J. A., Rivas, M. L., Wilroy, R. S., & Simpson, J. L. (1996) · American Journal of Medical Genetics · doi:10.1002/(sici)1096-8628(19960628)63:4 · Cited by 42 · see citing works

Molecular genetic analysis of Saccharomyces cerevisiae C1-tetrahydrofolate synthase mutants reveals a noncatalytic function of the ADE3 gene product and an additional folate-dependent enzyme.

Barlowe, C. K., & Appling, D. R. (1990) · Molecular and Cellular Biology · doi:10.1128/mcb.10.11.5679 · Cited by 42 · see citing works

10-Formyltetrahydrofolate Dehydrogenase Requires a 4′-Phosphopantetheine Prosthetic Group for Catalysis

DONATO, H. J., Krupenko, N. I., Tsybovsky, Y., & Krupenko, S. A. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m707627200 · Cited by 41 · see citing works

Properties of Tetrahydropteroylpentaglutamate Bound to 10-Formyltetrahydrofolate Dehydrogenase

Kim, D. W., Huang, T. H., Schirch, D. M., & Schirch, V. (1996) · Biochemistry · doi:10.1021/bi9619684 · Cited by 41 · see citing works

A B12-responsive Internal Ribosome Entry Site (IRES) Element in Human Methionine Synthase

Oltean, S., & Banerjee, R. V. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501964200 · Cited by 41 · see citing works

Methenyltetrahydrofolate Synthetase Prevents the Inhibition of Phosphoribosyl 5-Aminoimidazole 4-Carboxamide Ribonucleotide Formyltransferase by 5-Formyltetrahydrofolate Polyglutamates

Bertrand, R., & Jolivet, J. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)81870-1 · Cited by 41 · see citing works

The association-dissociation of formyltetrahydrofolate synthetase and its relation to monovalent cation activation of catalytic activity

Scott, J. M., & Rabinowitz, J. C. (1967) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(67)90473-1 · Cited by 40 · see citing works

Formyltetrahydrofolate Synthetase

Himes, R. H., & Cohn, M. (1967) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)95855-2 · Cited by 40 · see citing works

Enzymatic characterization of human mitochondrial C1-tetrahydrofolate synthase

Walkup, A. S., & Appling, D. R. (2005) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2005.08.007 · Cited by 39 · see citing works

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 · see citing works

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 1,147 · see citing works

Compartmentalization 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 · see citing works

ESPEN micronutrient guideline

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 · see citing works

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 435 · see citing works

Mitochondrial Biogenesis and Proteome Remodeling Promote One-Carbon Metabolism for T Cell Activation

Ron-Harel, N., Santos, D., Ghergurovich, J. M., Sage, P. T., Reddy, A., Lovitch, S. B., Dephoure, N., Satterstrom, F. K., Sheffer, M., Spinelli, J. B., et al. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.06.007 · Cited by 429 · see citing works

Mitochondrial translation requires folate-dependent tRNA methylation

Morscher, R. J., Ducker, G. S., Li, H., Mayer, J., Gitai, Z., Sperl, W., & Rabinowitz, J. D. (2018) · Nature · doi:10.1038/nature25460 · Cited by 278 · see citing works

One-Carbon Metabolism–Genome Interactions in Folate-Associated Pathologies ,

Stover, P. J. (2009) · The Journal of Nutrition · doi:10.3945/jn.109.113670 · Cited by 276 · see citing works

Maternal plasma folate impacts differential DNA methylation in an epigenome-wide meta-analysis of newborns

Joubert, B. R., den Dekker, H. T., Felix, J. F., Bohlin, J., Ligthart, S., Beckett, E., Tiemeier, H. W., van Meurs, J. B. J., Uitterlinden, A. G., Albert Hofman, D., et al. (2016) · Nature Communications · doi:10.1038/ncomms10577 · Cited by 262 · see citing works

The many roles of glutamate in metabolism

Walker, M. C., & van der Donk, W. A. (2015) · Journal of Industrial Microbiology & Biotechnology · doi:10.1007/s10295-015-1665-y · Cited by 245 · see citing works

Betaine chemistry, roles, and potential use in liver disease

Day, C. R., & Kempson, S. A. (2016) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2016.02.001 · Cited by 233 · see citing works

The Intestinal Absorption of Folates

Visentin, M., Diop-Bove, N., Zhao, R., & Goldman, I. D. (2011) · Annual Review of Physiology · doi:10.1146/annurev-physiol-020911-153251 · Cited by 223 · see citing works

SHMT1 and SHMT2 Are Functionally Redundant in Nuclear De novo Thymidylate Biosynthesis

Anderson, D. D., & Stover, P. J. (2009) · PLoS ONE · doi:10.1371/journal.pone.0005839 · Cited by 199 · see citing works

The epigenetics of autoimmunity

Meda, F., Folci, M., Baccarelli, A., & Selmi, C. F. (2011) · Cellular and Molecular Immunology · doi:10.1038/cmi.2010.78 · Cited by 195 · see citing works

Identification of a de novo thymidylate biosynthesis pathway in mammalian mitochondria

Anderson, D. D., Quintero, C. M., & Stover, P. J. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1103623108 · Cited by 186 · see citing works

β-Lactoglobulin/Folic Acid Complexes: Formation, Characterization, and Biological Implication

Liang, L., & Subirade, M. (2010) · The Journal of Physical Chemistry B · doi:10.1021/jp101096r · Cited by 182 · see citing works

One-carbon metabolism and nucleotide biosynthesis as attractive targets for anticancer therapy

Shuvalov, O., Petukhov, A., Daks, A., Fedorova, O., Vasileva, E., & Barlev, N. A. (2017) · Oncotarget · doi:10.18632/oncotarget.15053 · Cited by 168 · see citing works

Molecular Basis of Alcohol-Related Gastric and Colon Cancer

Na, H., & Lee, J. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18061116 · Cited by 160 · see citing works

Safety of folic acid

Field, M. S., & Stover, P. J. (2017) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.13499 · Cited by 160 · see citing works

Folic acid‐induced animal model of kidney disease

Yan, L. (2021) · Animal Models and Experimental Medicine · doi:10.1002/ame2.12194 · Cited by 144 · see citing works

Folic Acid and the Prevention of Birth Defects: 30 Years of Opportunity and Controversies

Crider, K. S., Qi, Y., Yeung, L. F., Mai, C. T., Zauche, L. H., Wang, A., Daniels, K., & Williams, J. L. (2022) · Annual Review of Nutrition · doi:10.1146/annurev-nutr-043020-091647 · Cited by 137 · see citing works

Trafficking of Intracellular Folates

Stover, P. J., & Field, M. S. (2011) · Advances in Nutrition · doi:10.3945/an.111.000596 · Cited by 135 · see citing works

One carbon metabolism in pregnancy: Impact on maternal, fetal and neonatal health

Kalhan, S. C. (2016) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2016.06.006 · Cited by 135 · see citing works

Recent Developments in Folate Nutrition

Naderi, N., & House, J. D. (2018) · Advances in food and nutrition research · doi:10.1016/bs.afnr.2017.12.006 · Cited by 131 · see citing works

Possible Roles for Folic Acid in the Regulation of Trophoblast Invasion and Placental Development in Normal Early Human Pregnancy1

Williams, P. J., Bulmer, J. N., Innes, B. A., & Pipkin, F. B. (2011) · Biology of Reproduction · doi:10.1095/biolreprod.110.088351 · Cited by 127 · see citing works

Protective effects of N-acetyl-cysteine in mitochondria bioenergetics, oxidative stress, dynamics and S-glutathionylation alterations in acute kidney damage induced by folic acid

Aparicio‐Trejo, O. E., Reyes-Fermín, L. M., Briones‐Herrera, A., Tapia, E., León‐Contreras, J. C., Hernández‐Pando, R., Sánchez‐Lozada, L. G., & Pedraza‐Chaverrí, J. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.11.005 · Cited by 125 · see citing works

Serine Hydroxymethyltransferase Anchors de Novo Thymidylate Synthesis Pathway to Nuclear Lamina for DNA Synthesis

Anderson, D. D., Woeller, C. F., Chiang, E. I., Shane, B., & Stover, P. J. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.333120 · Cited by 124 · see citing works

The complexity of the serine glycine one-carbon pathway in cancer

Reina‐Campos, M., Díaz-Meco, M. T., & Moscat, J. (2019) · The Journal of Cell Biology · doi:10.1083/jcb.201907022 · Cited by 123 · see citing works

Folate metabolic pathways in Leishmania

Vickers, T. J., & Beverley, S. M. (2011) · Essays in Biochemistry · doi:10.1042/bse0510063 · Cited by 122 · see citing works

Fluorescent probes for imaging formaldehyde in biological systems

Bruemmer, K. J., Brewer, T. F., & Chang, C. J. (2017) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2017.04.010 · Cited by 122 · see citing works

Copper- or manganese-doped ZnS quantum dots as fluorescent probes for detecting folic acid in aqueous media

Geszke-Moritz, M., Clavier, G. M., Lulek, J., & Schneider, R. (2011) · Journal of Luminescence · doi:10.1016/j.jlumin.2011.12.014 · Cited by 121 · see citing works

More than just a gut instinct–the potential interplay between a baby's nutrition, its gut microbiome, and the epigenome

Mischke, M., & Plösch, T. (2013) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00551.2012 · Cited by 120 · see citing works

Folates: Chemistry, analysis, occurrence, biofortification and bioavailability

Saini, R. K., Nile, S. H., & Keum, Y. (2016) · Food Research International · doi:10.1016/j.foodres.2016.07.013 · Cited by 120 · see citing works

ALDH1L2 Is the Mitochondrial Homolog of 10-Formyltetrahydrofolate Dehydrogenase

Krupenko, N. I., Dubard, M. E., Strickland, K. C., Moxley, K. M., Oleinik, N. V., & Krupenko, S. A. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.128843 · Cited by 114 · see citing works

Mechanisms of quantitative disease resistance in plants

French, E., Kim, B.-S., & Iyer‐Pascuzzi, A. S. (2016) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2016.05.015 · Cited by 113 · see citing works

Cell cycle regulation of folate‐mediated one‐carbon metabolism

Lan, X., Field, M. S., & Stover, P. J. (2018) · WIREs Systems Biology and Medicine · doi:10.1002/wsbm.1426 · Cited by 113 · see citing works

Production of germ-free mosquitoes via transient colonisation allows stage-specific investigation of host–microbiota interactions

Romoli, O., Schönbeck, J. C., Hapfelmeier, S., & Gendrin, M. (2021) · Nature Communications · doi:10.1038/s41467-021-21195-3 · Cited by 107 · see citing works

Polymorphisms in 1-carbon metabolism, epigenetics and folate-related pathologies

Stover, P. J. (2011) · Lifestyle Genomics · doi:10.1159/000334586 · Cited by 109 · see citing works

Emerging therapeutic targets for treatment of leishmaniasis

Sundar, S., & Singh, B. (2018) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2018.1472241 · Cited by 105 · see citing works

The purinosome, a multi-protein complex involved in the de novo biosynthesis of purines in humans

Zhao, H., French, J. B., Ye, F., & Benkovic, S. J. (2013) · Chemical Communications · doi:10.1039/c3cc41437j · Cited by 103 · see citing works

The metabolic basis for developmental disorders due to defective folate transport

Desai, A., Sequeira, J. M., & Quadros, E. V. (2016) · Biochimie · doi:10.1016/j.biochi.2016.02.012 · Cited by 98 · see citing works

Is 5-methyltetrahydrofolate an alternative to folic acid for the prevention of neural tube defects?

Obeid, R., Holzgreve, W., & Pietrzik, K. F. (2013) · Journal of Perinatal Medicine · doi:10.1515/jpm-2012-0256 · Cited by 96 · see citing works

Methylenetetrahydrofolate Reductase: Biochemical Characterization and Medical Significance

Trimmer, E. E. (2013) · Current Pharmaceutical Design · doi:10.2174/1381612811319140008 · Cited by 94 · see citing works

The toxic side of one-carbon metabolism and epigenetics

Morellato, A. E., Umansky, C., & Pontel, L. B. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101850 · Cited by 92 · see citing works

Folic Acid Protects against Lipopolysaccharide-Induced Preterm Delivery and Intrauterine Growth Restriction through Its Anti-Inflammatory Effect in Mice

Zhao, M., Chen, Y., Dong, X.-T., Zhou, J. F., Chen, X., Wang, H., Wu, S., Xia, M., Zhang, C., & Xu, D. (2013) · PLoS ONE · doi:10.1371/journal.pone.0082713 · Cited by 96 · see citing works

Relationship between Maternal Vitamin D Levels and Adverse Outcomes

Zhang, H., Wang, S., Tuo, L., Zhai, Q., Cui, J., Chen, D., & Xu, D. (2022) · Nutrients · doi:10.3390/nu14204230 · Cited by 90 · see citing works

Evidence for the Role of Mitochondrial DNA Release in the Inflammatory Response in Neurological Disorders

Moya, G. E., Rivera, P. D., & Dittenhafer‐Reed, K. E. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22137030 · Cited by 88 · see citing works

Nuclear Folate Metabolism

Field, M. S., Kamynina, E., Chon, J., & Stover, P. J. (2018) · Annual Review of Nutrition · doi:10.1146/annurev-nutr-071714-034441 · Cited by 85 · see citing works

Rice Intake and Emerging Concerns on Arsenic in Rice: a Review of the Human Evidence and Methodologic Challenges

Karagas, M. R., Punshon, T., Davis, M. M., Bulka, C. M., Slaughter, F. A., Karalis, D., Argos, M., & Ahsan, H. (2019) · Current Environmental Health Reports · doi:10.1007/s40572-019-00249-1 · Cited by 85 · see citing works

Folate metabolism in human malaria parasites—75 years on

Müller, I. B., & Hyde, J. E. (2013) · Molecular and Biochemical Parasitology · doi:10.1016/j.molbiopara.2013.02.008 · Cited by 85 · see citing works

Targeting nuclear thymidylate biosynthesis

Chon, J., Stover, P. J., & Field, M. S. (2016) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2016.11.005 · Cited by 84 · see citing works

Effect of in ovo feeding of folic acid on the folate metabolism, immune function and epigenetic modification of immune effector molecules of broiler

Li, S., LiHui, Z., Liu, Y., Shen, J., Liu, L., Yao, J., & Yang, X. (2015) · British Journal Of Nutrition · doi:10.1017/s0007114515004511 · Cited by 86 · see citing works

PHGDH: a novel therapeutic target in cancer

Lee, C. M., Hwang, Y., Kim, M., Park, Y.-C., Kim, H., & Fang, S. (2024) · Experimental & Molecular Medicine · doi:10.1038/s12276-024-01268-1 · Cited by 81 · see citing works

Folylpoly-γ-glutamate synthetase: A key determinant of folate homeostasis and antifolate resistance in cancer

Raz, S., Stark, M., & Assaraf, Y. G. (2016) · Drug Resistance Updates · doi:10.1016/j.drup.2016.06.004 · Cited by 80 · see citing works

ALDH1L1 inhibits cell motility via dephosphorylation of cofilin by PP1 and PP2A

Oleinik, N. V., Krupenko, N. I., & Krupenko, S. A. (2010) · Oncogene · doi:10.1038/onc.2010.356 · Cited by 80 · see citing works

Nuclear Enrichment of Folate Cofactors and Methylenetetrahydrofolate Dehydrogenase 1 (MTHFD1) Protect de Novo Thymidylate Biosynthesis during Folate Deficiency

Field, M. S., Kamynina, E., Agunloye, O. C., Liebenthal, R. P., Lamarre, S. G., Brosnan, M. E., Brosnan, J. T., & Stover, P. J. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.599589 · Cited by 77 · see citing works

One-Carbon Metabolism, Spermatogenesis, and Male Infertility

Singh, K., & Jaiswal, D. (2012) · Reproductive Sciences · doi:10.1177/1933719112459232 · Cited by 76 · see citing works

Metabolic characterization of asthenozoospermia using nontargeted seminal plasma metabolomics

Zhang, X., Diao, R., Zhu, X., Li, Z., & Cai, Z. (2015) · Clinica Chimica Acta · doi:10.1016/j.cca.2015.09.001 · Cited by 75 · see citing works

Epigenetics: deciphering how environmental factors may modify autoimmune type 1 diabetes

MacFarlane, A. J., Strom, A., & Scott, F. W. (2009) · Mammalian Genome · doi:10.1007/s00335-009-9213-6 · Cited by 75 · see citing works

Methionine synthase supports tumour tetrahydrofolate pools

Ghergurovich, J. M., Xu, X., Wang, J. Z., Yang, L., Ryseck, R.-P., Wang, L., & Rabinowitz, J. D. (2021) · Nature Metabolism · doi:10.1038/s42255-021-00465-w · Cited by 74 · see citing works

The clinical presentation of cobalamin‐related disorders: From acquired deficiencies to inborn errors of absorption and intracellular pathways

Huemer, M., & Baumgartner, M. R. (2019) · Journal of Inherited Metabolic Disease · doi:10.1002/jimd.12012 · Cited by 75 · see citing works

Folate Stress Induces Apoptosis via p53-dependent de Novo Ceramide Synthesis and Up-regulation of Ceramide Synthase 6

Hoeferlin, L. A., Fekry, B., Öğretmen, B., Krupenko, S. A., & Krupenko, N. I. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.461798 · Cited by 72 · see citing works

Molecular mechanisms underlying the potentially adverse effects of folate

Strickland, K. C., Krupenko, N. I., & Krupenko, S. A. (2012) · Clinical Chemistry and Laboratory Medicine (CCLM) · doi:10.1515/cclm-2012-0561 · Cited by 70 · see citing works

Chronic impairment of mitochondrial bioenergetics and β-oxidation promotes experimental AKI-to-CKD transition induced by folic acid

Aparicio‐Trejo, O. E., Avila-Rojas, S. H., Tapia, E., Rojas‐Morales, P., León‐Contreras, J. C., Martínez‐Klimova, E., Hernández‐Pando, R., Sánchez‐Lozada, L. G., & Pedraza‐Chaverrí, J. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.04.016 · Cited by 70 · see citing works

Therapeutic targeting of the mitochondrial one-carbon pathway: perspectives, pitfalls, and potential

Zhao, L. N., Björklund, M., Caldez, M. J., Zheng, J., & Kaldis, P. (2021) · Oncogene · doi:10.1038/s41388-021-01695-8 · Cited by 70 · see citing works

A comprehensive review on the efficacy of S-Adenosyl-L-methionine in Major Depressive Disorder.

Berardis, D. D., Orsolini, L., Serroni, N., Girinelli, G., Iasevoli, F., Tomasetti, C., de Bartolomeis, A., Mazza, M., Valchera, A., Fornaro, M., et al. (2016) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/1871527314666150821103825 · Cited by 71 · see citing works

Nanomaterials for sensing of formaldehyde in air: Principles, applications, and performance evaluation

Kukkar, D., Vellingiri, K., Kaur, R., Bhardwaj, S. K., Deep, A., & Kim, K. (2018) · Nano Research · doi:10.1007/s12274-018-2207-5 · Cited by 70 · see citing works

Mito-Nuclear Communication by Mitochondrial Metabolites and Its Regulation by B-Vitamins

Janssen, J. J. E., Grefte, S., Keijer, J., & de Boer, V. C. J. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.00078 · Cited by 68 · see citing works

Human mutations in methylenetetrahydrofolate dehydrogenase 1 impair nuclear de novo thymidylate biosynthesis

Field, M. S., Kamynina, E., Watkins, D., Rosenblatt, D. S., & Stover, P. J. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1414555112 · Cited by 63 · see citing works

Is the Measurement of Serum Formate Concentration Useful in the Diagnostics of Acute Methanol Poisoning? A Prospective Study of 38 Patients

Zakharov, S., Kurcová, I., Navrátil, T., Šálek, T., Komarc, M., & Pelclová, D. (2014) · Basic & Clinical Pharmacology & Toxicology · doi:10.1111/bcpt.12338 · Cited by 63 · see citing works

Maximizing the Therapeutic Window of an Antimicrobial Drug by Imparting Mitochondrial Sequestration in Human Cells

Pereira, M. P., & Kelley, S. O. (2011) · Journal of the American Chemical Society · doi:10.1021/ja110246u · Cited by 63 · see citing works

ALDH1L1 and ALDH1L2 Folate Regulatory Enzymes in Cancer

Krupenko, S. A., & Krupenko, N. I. (2018) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-98788-0_10 · Cited by 63 · see citing works

One-Carbon Metabolism in Prostate Cancer: The Role of Androgen Signaling

Corbin, J. M., & Ruiz-Echevarría, M. J. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17081208 · Cited by 62 · see citing works

Potential Links between Impaired One-Carbon Metabolism Due to Polymorphisms, Inadequate B-Vitamin Status, and the Development of Alzheimer’s Disease

Troesch, B., Weber, P., & Mohajeri, M. H. (2016) · Nutrients · doi:10.3390/nu8120803 · Cited by 61 · see citing works

Development of chemically defined media supporting high cell density growth of Ketogulonicigenium vulgare and Bacillus megaterium

Zhang, J., Zhou, J., Liu, J., Chen, K., Liu, L., & Chen, J. (2010) · Bioresource Technology · doi:10.1016/j.biortech.2010.10.124 · Cited by 61 · see citing works

Folate and folate receptor alpha antagonists mechanism of action in ovarian cancer

Walters, C. L., Arend, R. C., Armstrong, D. K., Naumann, R. W., & Alvarez, R. D. (2013) · Gynecologic Oncology · doi:10.1016/j.ygyno.2013.07.080 · Cited by 60 · see citing works

Brain structure, working memory and response inhibition in childhood leukemia survivors

van der Plas, E., Schachar, R. J., Hitzler, J., Crosbie, J., Guger, S. L., Spiegler, B. J., Ito, S., & Nieman, B. J. (2017) · Brain and Behavior · doi:10.1002/brb3.621 · Cited by 59 · see citing works

Subinhibitory Concentrations of Trimethoprim and Sulfamethoxazole Prevent Biofilm Formation by Acinetobacter baumannii through Inhibition of Csu Pilus Expression

Moon, K. H., Weber, B. S., & Feldman, M. F. (2017) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00778-17 · Cited by 59 · see citing works

Folate nutrition and blood–brain barrier dysfunction

Stover, P. J., Durga, J., & Field, M. S. (2017) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2017.01.006 · Cited by 59 · see citing works

Shmt1 Heterozygosity Impairs Folate-Dependent Thymidylate Synthesis Capacity and Modifies Risk of Apcmin -Mediated Intestinal Cancer Risk

MacFarlane, A. J., Perry, C. A., McEntee, M. F., Lin, D. M., & Stover, P. J. (2011) · Cancer Research · doi:10.1158/0008-5472.can-10-1886 · Cited by 57 · see citing works

Genetic modifiers of folate, vitamin B-12, and homocysteine status in a cross-sectional study of the Canadian population

Zinck, J. W. R., de Groh, M., & MacFarlane, A. J. (2015) · American Journal of Clinical Nutrition · doi:10.3945/ajcn.115.107219 · Cited by 57 · see citing works

Dietary folate, but not choline, modifies neural tube defect risk in Shmt1 knockout mice

Beaudin, A. E., Abarinov, E. V., Malysheva, O., Perry, C. A., Caudill, M. A., & Stover, P. J. (2011) · American Journal of Clinical Nutrition · doi:10.3945/ajcn.111.020305 · Cited by 54 · see citing works

Characterization and review of MTHFD1 deficiency: four new patients, cellular delineation and response to folic and folinic acid treatment

Burda, P., Küster, A., Hjalmarson, O., Suormala, T., Bürer, C., Lutz, S., Roussey, G., Christa, L., Asin-Cayuela, J., Kollberg, G., et al. (2015) · Journal of Inherited Metabolic Disease · doi:10.1007/s10545-015-9810-3 · Cited by 53 · see citing works

Investigating the effects of dietary folic acid on sperm count, DNA damage and mutation in Balb/c mice

Swayne, B. G., Kawata, A., Behan, N. A., Williams, A., Wade, M. G., MacFarlane, A. J., & Yauk, C. L. (2012) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2012.07.002 · Cited by 53 · see citing works

Loss of ALDH1L1 folate enzyme confers a selective metabolic advantage for tumor progression

Krupenko, S. A., & Krupenko, N. I. (2019) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2019.02.013 · Cited by 51 · see citing works

Differential proteomic analysis by SWATH-MS unravels the most dominant mechanisms underlying yeast adaptation to non-optimal temperatures under anaerobic conditions

Pinheiro, T., Lip, K. Y. F., García‐Ríos, E., Querol, A., Teixeira, J. A., van Gulik, W. M., Guillamón, J. M., & Domingues, L. (2020) · Scientific Reports · doi:10.1038/s41598-020-77846-w · Cited by 50 · see citing works

Rho GTPases RhoA and Rac1 Mediate Effects of Dietary Folate on Metastatic Potential of A549 Cancer Cells through the Control of Cofilin Phosphorylation

Oleinik, N. V., Helke, K. L., Kistner‐Griffin, E., Krupenko, N. I., & Krupenko, S. A. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.569657 · Cited by 50 · see citing works

Reaction-based fluorescent and chemiluminescent probes for formaldehyde detection and imaging

Huang, S., Li, Z., Liu, M., Zhou, M., Weng, J., He, Y., Jiang, Y., Zhang, H., & Sun, H. (2022) · Chemical Communications · doi:10.1039/d1cc05644a · Cited by 48 · see citing works

Mitochondrial NAD(P) + Transhydrogenase: From Molecular Features to Physiology and Disease

Francisco, A., Figueira, T. R., & Castilho, R. F. (2021) · Antioxidants and Redox Signaling · doi:10.1089/ars.2021.0111 · Cited by 48 · see citing works

Modeling cellular compartmentation in one‐carbon metabolism

Scotti, M., Stella, L., Shearer, E. J., & Stover, P. J. (2013) · WIREs Systems Biology and Medicine · doi:10.1002/wsbm.1209 · Cited by 46 · see citing works

Nutrient-Gene Interaction in Colon Cancer, from the Membrane to Cellular Physiology

Hou, T. Y., Davidson, L. A., Kim, E., Fan, Y., Fuentes, N. R., Triff, K., & Chapkin, R. S. (2016) · Annual Review of Nutrition · doi:10.1146/annurev-nutr-071715-051039 · Cited by 45 · see citing works

The Role of Metabolic Enzymes in the Regulation of Inflammation

Godfrey, W. H., & Kornberg, M. D. (2020) · Metabolites · doi:10.3390/metabo10110426 · Cited by 46 · see citing works

Enzymatic properties of ALDH1L2, a mitochondrial 10-formyltetrahydrofolate dehydrogenase

Strickland, K. C., Krupenko, N. I., Dubard, M. E., Hu, C. J., Tsybovsky, Y., & Krupenko, S. A. (2011) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2011.01.008 · Cited by 45 · see citing works

Genetic impairments in folate enzymes increase dependence on dietary choline for phosphatidylcholine production at the expense of betaine synthesis

Ganz, A. B., Shields, K. S., Fomin, V. G., Lopez, Y. S., Mohan, S., Lovesky, J., Chuang, J. C., Ganti, A., Carrier, B., Yan, J., et al. (2016) · The FASEB Journal · doi:10.1096/fj.201500138rr · Cited by 45 · see citing works

Finding the genetic mechanisms of folate deficiency and neural tube defects—Leaving no stone unturned

Au, K. S., Findley, T. O., & Northrup, H. (2017) · American Journal of Medical Genetics Part A · doi:10.1002/ajmg.a.38478 · Cited by 45 · see citing works

Reverse engineering the cancer metabolic network using flux analysis to understand drivers of human disease

Badur, M. G., & Metallo, C. M. (2017) · Metabolic Engineering · doi:10.1016/j.ymben.2017.11.013 · Cited by 44 · see citing works

A New 18F-Labeled Folic Acid Derivative with Improved Properties for the PET Imaging of Folate Receptor–Positive Tumors

Roß, T. L., Honer, M., Müller, C., Groehn, V., Schibli, R., & Ametamey, S. M. (2010) · Journal of Nuclear Medicine · doi:10.2967/jnumed.110.079756 · Cited by 44 · see citing works

Effect of supplementation with methyl-donor nutrients on neurodevelopment and cognition: considerations for future research

McKee, S. E., & Reyes, T. M. (2018) · Nutrition Reviews · doi:10.1093/nutrit/nuy007 · Cited by 44 · see citing works

Maternal smoking during pregnancy and cord blood DNA methylation: new insight on sex differences and effect modification by maternal folate levels

Zhang, B., Hong, X., Ji, H., Tang, W., Kimmel, M., Ji, Y., Pearson, C., ZUCKERMAN, B. S., Surkan, P. J., & Wang, X. (2018) · Epigenetics · doi:10.1080/15592294.2018.1475978 · Cited by 44 · see citing works

Systematic investigation of the aza-Cope reaction for fluorescence imaging of formaldehyde in vitro and in vivo

Du, Y. L., Zhang, Y., Huang, M., Wang, S., Wang, J., Liao, K., Wu, X., Zhou, Q., Zhang, X., Wu, Y., et al. (2021) · Chemical Science · doi:10.1039/d1sc04387k · Cited by 44 · see citing works

The association-dissociation of formyltetrahydrofolate synthetase and its relation to monovalent cation activation of catalytic activity

Scott, J. M., & Rabinowitz, J. C. (1967) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(67)90473-1 · Cited by 40 · see citing works

One-Carbon Metabolism in Health and Disease

Ducker, G. S., & Rabinowitz, J. D. (2017) · Cell Metabolism · doi:10.1016/j.cmet.2016.08.009 · Cited by 2,239 · see citing works

The Roles of Mitochondrial Folate Metabolism in Supporting Mitochondrial DNA Synthesis, Oxidative Phosphorylation, and Cellular Function

Xiu, Y., & Field, M. S. (2020) · Current Developments in Nutrition · doi:10.1093/cdn/nzaa153 · Cited by 74 · see citing works

In vitro evidence for the involvement of mitochondrial folate metabolism in the supply of cytoplasmic one-carbon units.

Barlowe, C. K., & Appling, D. R. (1988) · PubMed · Cited by 110 · see citing works

Compartmentation of folate‐mediated one‐carbon metabolism in eukaryotes

Appling, D. R. (1991) · The FASEB Journal · doi:10.1096/fasebj.5.12.1916088 · Cited by 350 · see citing works