Vitamin C. Biosynthesis, recycling and degradation in mammals
Open accessAbstract
Vitamin C, a reducing agent and antioxidant, is a cofactor in reactions catalyzed by Cu(+)-dependent monooxygenases and Fe(2+)-dependent dioxygenases. It is synthesized, in vertebrates having this capacity, from d-glucuronate. The latter is formed through direct hydrolysis of uridine diphosphate (UDP)-glucuronate by enzyme(s) bound to the endoplasmic reticulum membrane, sharing many properties with, and most likely identical to, UDP-glucuronosyltransferases. Non-glucuronidable xenobiotics (aminopyrine, metyrapone, chloretone and others) stimulate the enzymatic hydrolysis of UDP-glucuronate, accounting for their effect to increase vitamin C formation in vivo. Glucuronate is converted to l-gulonate by aldehyde reductase, an enzyme of the aldo-keto reductase superfamily. l-Gulonate is converted to l-gulonolactone by a lactonase identified as SMP30 or regucalcin, whose absence in mice leads to vitamin C deficiency. The last step in the pathway of vitamin C synthesis is the oxidation of l-gulonolactone to l-ascorbic acid by l-gulonolactone oxidase, an enzyme associated with the endoplasmic reticulum membrane and deficient in man, guinea pig and other species due to mutations in its gene. Another fate of glucuronate is its conversion to d-xylulose in a five-step pathway, the pentose pathway, involving identified oxidoreductases and an unknown decarboxylase. Semidehydroascorbate, a major oxidation product of vitamin C, is reconverted to ascorbate in the cytosol by cytochrome b(5) reductase and thioredoxin reductase in reactions involving NADH and NADPH, respectively. Transmembrane electron transfer systems using ascorbate or NADH as electron donors serve to reduce semidehydroascorbate present in neuroendocrine secretory vesicles and in the extracellular medium. Dehydroascorbate, the fully oxidized form of vitamin C, is reduced spontaneously by glutathione, as well as enzymatically in reactions using glutathione or NADPH. The degradation of vitamin C in mammals is initiated by the hydrolysis of dehydroascorbate to 2,3-diketo-l-gulonate, which is spontaneously degraded to oxalate, CO(2) and l-erythrulose. This is at variance with bacteria such as Escherichia coli, which have enzymatic degradation pathways for ascorbate and probably also dehydroascorbate.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Synthesis of vitamin C has been documented in all plant species, including algae and photosynthetic protists.
“So far, the synthesis of vitamin C was documented in all plant species, including algae and photosynthetic protists [1].”
From Vitamin C-Sources, Physiological Role, Kinetics, Deficiency, Use, Toxicity, and Determination (2021) · cites this paper as [1]
Humans are fully dependent on vitamin C intake from the diet.
“They are, therefore, fully dependent on vitamin C intake from the diet [1,2,3].”
From Vitamin C-Sources, Physiological Role, Kinetics, Deficiency, Use, Toxicity, and Determination (2021) · cites this paper as [1]
Humans and several other species (guinea pigs, bats, passeriform birds, and primates) lack L-gulono-1,4-lactone oxidase and cannot synthesize vitamin C.
“In contrast to most of the vertebrates, guinea pigs, bats, passeriform birds, and primates, including humans, lack L-gulono-1,4-lactone oxidase, and, hence, cannot synthesize vitamin C.”
From Vitamin C-Sources, Physiological Role, Kinetics, Deficiency, Use, Toxicity, and Determination (2021) · cites this paper as [1]
The pKa of ascorbic acid is 4.1-4.2, so it is present completely as a monoanion-ascorbate-at physiological pH.
“The pKa of ascorbic acid is 4.1–4.2. Hence, it is present completely as a monoanion—ascorbate at the physiological pH [1,2,4,68].”
From Vitamin C-Sources, Physiological Role, Kinetics, Deficiency, Use, Toxicity, and Determination (2021) · cites this paper as [1]
2,3-diketo-1-gulonic acid can be spontaneously and enzymatically decomposed to erythrulose and oxalate, and this reaction is accelerated by bicarbonate.
“2,3-diketo-1-gulonic acid can be spontaneously, but also enzymatically, decomposed to erythrulose and oxalate. This reaction is accelerated by bicarbonate [1,3].”
From Vitamin C-Sources, Physiological Role, Kinetics, Deficiency, Use, Toxicity, and Determination (2021) · cites this paper as [1]
Redundant pathways mediate reduction of dehydroascorbic acid to ascorbic acid, including direct but slow nonenzymatic reduction by glutathione and enzymatic reduction by glutaredoxin, glutathione transferase omega 2, or thioredoxin reductase; the first two require glutathione.
“There are apparently redundant pathways mediating the reduction of dehydroascorbic acid to ascorbic acid. They include both direct but slow nonenzymatic reduction by glutathione and enzymatic by a couple of enzymes (e.g., glutaredoxin, glutathione transferase omega 2, or thioredoxin reductase). Of note is that the first two enzymes require glutathione for their activity [1,73].”
From Vitamin C-Sources, Physiological Role, Kinetics, Deficiency, Use, Toxicity, and Determination (2021) · cites this paper as [1]
Cites
The Metabolic and Molecular Bases of Inherited Disease
Scriver, R. C. (1995) · Medical Entomology and Zoology · Cited by 12,101 · see citing works
The metabolic and molecular bases of inherited disease
Chen, Y.-T. (2001) · Medical Entomology and Zoology · Cited by 6,928 · see citing works
Predicting subcellular localization of proteins based on their N-terminal amino acid sequence.
Emanuelsson, O., Nielsen, H., Brunak, S., & von Heijne, G. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.3903 · Cited by 4,419 · see citing works
The Pecking Order of Free Radicals and Antioxidants: Lipid Peroxidation, α-Tocopherol, and Ascorbate
Buettner, G. R. (1993) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1993.1074 · Cited by 2,417 · see citing works
Vitamin C as an Antioxidant: Evaluation of Its Role in Disease Prevention
Padayatty, S. J., Katz, A., Wang, Y., Eck, P., Kwon, O., Lee, J.-H., Chen, S., Corpe, C., Dutta, A., Dutta, S. K., et al. (2003) · Journal of the American College of Nutrition · doi:10.1080/07315724.2003.10719272 · Cited by 1,949 · see citing works
Catalytic Metals, Ascorbate and Free Radicals: Combinations to Avoid
Buettner, G. R., & Jurkiewicz, B. A. (1996) · Radiation Research · doi:10.2307/3579271 · Cited by 884 · see citing works
Glutathione-ascorbic acid antioxidant system in animals
Meister, A. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)36891-6 · Cited by 812 · see citing works
Identification, Characterization, and Crystal Structure of the Omega Class Glutathione Transferases
Philip G. Board, Coggan, M., Chelvanayagam, G., Easteal, S., Jermiin, L. S., Schulte, G. K., Danley, D. E., Hoth, L. R., Griffor, M. C., Kamath, A. V., et al. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m001706200 · Cited by 719 · see citing works
The biochemical functions of ascorbic acid
Englard, S., & Seifter, S. (1986) · Annual Review of Nutrition · doi:10.1146/annurev.nu.06.070186.002053 · Cited by 564 · see citing works
Nishikimi, M., Fukuyama, R., Minoshima, S., Shimizu, N., & Yagi, K. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)36884-9 · Cited by 505 · see citing works
ISOLATION OF RAT LIVER PLASMA MEMBRANES
Touster, O., Aronson, N. N., Dulaney, J. T., & Hendrickson, H. (1970) · The Journal of Cell Biology · doi:10.1083/jcb.47.3.604 · Cited by 499 · see citing works
The redox couple between glutathione and ascorbic acid: A chemical and physiological perspective
Winkler, B. S., Orselli, S. M., & Rex, T. S. (1994) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(94)90019-1 · Cited by 491 · see citing works
New insights into copper monooxygenases and peptide amidation: Structure, mechanism and function
Prigge, S. T., Mains, R. E., Eipper, B. A., & Amzel* **, L. M. (2000) · Cellular and Molecular Life Sciences · doi:10.1007/pl00000763 · Cited by 460 · see citing works
The Aldo-Keto Reductase Superfamily
Bohren, K. M., Bullock, B., Wermuth, B., & Gabbay, K. H. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)60566-6 · Cited by 453 · see citing works
Wells, W. W., Xu, D. P., Yang, Y., & Rocque, P. A. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)55401-6 · Cited by 450 · see citing works
Evolution and the Biosynthesis of Ascorbic Acid
Chatterjee, I. (1973) · Science · doi:10.1126/science.182.4118.1271 · Cited by 433 · see citing works
B IOSYNTHESIS OF A SCORBIC A CID IN P LANTS : A Renaissance
Smirnoff, N., Conklin, P. L., & Loewus, F. A. (2001) · Annual Review of Plant Physiology and Plant Molecular Biology · doi:10.1146/annurev.arplant.52.1.437 · Cited by 413 · see citing works
REGULATION OF VITAMIN C TRANSPORT
Wilson, J. X. (2005) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.25.050304.092647 · Cited by 376 · see citing works
Sotiriou, S., Gispert, S., Cheng, J., Wang, Y., Chen, A., Hoogstraten-Miller, S., Miller, G. F., Kwon, O., Levine, M., Guttentag, S. H., et al. (2002) · Nature Medicine · doi:10.1038/0502-514 · Cited by 367 · see citing works
Reduction of Dehydroascorbate to Ascorbate by the Selenoenzyme Thioredoxin Reductase
May, J. M., Mendiratta, S. S., Hill, K. E., & Burk, R. F. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.36.22607 · Cited by 344 · see citing works
Mãrtensson, J., Meister, A., & M�rtensson, J. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.11.4656 · Cited by 287 · see citing works
Aortic wall damage in mice unable to synthesize ascorbic acid
Maeda, N., Hagihara, H., Nakata, Y., Hiller, S., Wilder, J., & Reddick, R. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.2.841 · Cited by 260 · see citing works
Vitamin C transport systems of mammalian cells
Liang, W.-J., Johnson, D., & Jarvis, S. M. (2001) · Molecular Membrane Biology · doi:10.1080/09687680110033774 · Cited by 255 · see citing works
The aldo-keto reductase (AKR) superfamily: an update
Jez, J. M., & Penning, T. M. (2001) · Chemico-Biological Interactions · doi:10.1016/s0009-2797(00)00295-7 · Cited by 239 · see citing works
Regulation of hypoxia-inducible factor 1 by prolyl and asparaginyl hydroxylases
Hirota, K., & Semenza, G. L. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.08.193 · Cited by 231 · see citing works
Kondo, Y., Inai, Y., Sato, Y., Handa, S., Kubo, S., Shimokado, K., Goto, S., Nishikimi, M., Maruyama, N., & Ishigami, A. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0511225103 · Cited by 227 · see citing works
Characterization of the Omega Class of Glutathione Transferases
Whitbread, A. K., Masoumi, A., Tetlow, N., Schmuck, E., Coggan, M., & Philip G. Board (2005) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(05)01005-0 · Cited by 218 · see citing works
Ascorbate Increases Human Oxaluria and Kidney Stone Risk
Massey, L. K., Liebman, M., & Kynast-Gales, S. A. (2005) · Journal of Nutrition · doi:10.1093/jn/135.7.1673 · Cited by 214 · see citing works
Is ascorbic acid an antioxidant for the plasma membrane?
May, J. M. (1999) · The FASEB Journal · doi:10.1096/fasebj.13.9.995 · Cited by 199 · see citing works
Reduction of the Ascorbyl Free Radical to Ascorbate by Thioredoxin Reductase
May, J. M., Cobb, C. E., Mendiratta, S. S., Hill, K. E., & Burk, R. F. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.36.23039 · Cited by 188 · see citing works
Bode, A. M., Cunningham, L., & Rose, R. C. (1990) · Clinical Chemistry · doi:10.1093/clinchem/36.10.1807 · Cited by 177 · see citing works
Role of regucalcin in maintaining cell homeostasis and function (Review)
Yamaguchi, M. (2005) · International Journal of Molecular Medicine · doi:10.3892/ijmm.15.3.371 · Cited by 174 · see citing works
Fujita, T., Uchida, K., & Maruyama, N. (1992) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(92)90108-7 · Cited by 172 · see citing works
Villalba, J. M., Navarro, F., Córdoba, F., Serrano, A., Arroyo, A., Crane, F. L., & Navas, P. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.11.4887 · Cited by 169 · see citing works
Schmuck, E., Philip G. Board, Whitbread, A. K., Tetlow, N., Cavanaugh, J. A., Blackburn, A. C., & Masoumi, A. (2005) · Pharmacogenetics and Genomics · doi:10.1097/01.fpc.0000165725.81559.e3 · Cited by 167 · see citing works
Sodium-dependent ascorbic acid transporter family SLC23
Takanaga, H., Mackenzie, B., & Hediger, M. A. (2004) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-003-1104-1 · Cited by 161 · see citing works
Nucleotide Activation of Liver Microsomal Glucuronidation
Pogell, B. M., & Leloir, L. F. (1961) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)64355-8 · Cited by 159 · see citing works
The non-oxidative degradation of ascorbic acid at physiological conditions
Simpson, G., & ORTWERTH, B. J. (2000) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/s0925-4439(00)00009-0 · Cited by 158 · see citing works
Metabolism of L-ascorbic acid-1-C14 in man
Hellman, L., & Burns, J. J. (1958) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)70515-2 · Cited by 150 · see citing works
Nishikimi, M., Kawai, T., & Yagi, K. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)36707-9 · Cited by 148 · see citing works
Ôba, K., Ishikawa, S., Nishikawa, M., Mizuno, H., & Yamamoto, T. (1995) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a124697 · Cited by 148 · see citing works
Electron transfer across the chromaffin granule membrane.
Njus, D., KNOTH, J., Cook, C., & Kelly, P. M. (1983) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)33212-5 · Cited by 146 · see citing works
Østergaard, J., Persiau, G., Davey, M. W., Bauw, G., & MONTAGU, M. V. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.48.30009 · Cited by 146 · see citing works
Smirnoff, N. (2001) · Vitamins and hormones · doi:10.1016/s0083-6729(01)61008-2 · Cited by 144 · see citing works
Iyanagi, T., & Yamazaki, I. (1969) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(69)90133-9 · Cited by 144 · see citing works
Disorders of oxidised haemoglobin
Percy, M. J., McFerran, N. V., & Lappin, T. R. J. (2004) · Blood Reviews · doi:10.1016/j.blre.2004.02.001 · Cited by 144 · see citing works
Wells, W. W., & Xu, D. P. (1994) · Journal of Bioenergetics and Biomembranes · doi:10.1007/bf00762777 · Cited by 128 · see citing works
Iyanagi, T. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54390-8 · Cited by 126 · see citing works
Yew, W. S., & Gerlt, J. A. (2002) · Journal of Bacteriology · doi:10.1128/jb.184.1.302-306.2002 · Cited by 126 · see citing works
Hollmann, S., & Touster, O. (1962) · Biochimica et Biophysica Acta · doi:10.1016/0006-3002(62)90048-3 · Cited by 124 · see citing works
Nucleotide pyrophosphatase, a sialoglycoprotein located on the hepatocyte surface
Evans, W. H. (1974) · Nature · doi:10.1038/250391a0 · Cited by 124 · see citing works
A rat mutant unable to synthesize vitamin C
Mizushima, Y., Harauchi, T., Yoshizaki, T., & Makino, S. (1984) · Cellular and Molecular Life Sciences · doi:10.1007/bf01952551 · Cited by 120 · see citing works
Purification and characterization of glutathione-dependent dehydroascorbate reductase from rat liver
Maellaro, E., Bello, B. D., Sugherini, L., Santucci, A., Comporti, M., & Casini, A. (1994) · Biochemical Journal · doi:10.1042/bj3010471 · Cited by 116 · see citing works
Siendones, E., González-Reyes, J. A., Santos‐Ocaña, C., Navas, P., & Córdoba, F. (1999) · PLANT PHYSIOLOGY · doi:10.1104/pp.120.3.907 · Cited by 114 · see citing works
Bello, B. D., Maellaro, E., Sugherini, L., Santucci, A., Comporti, M., & Casini, A. (1994) · Biochemical Journal · doi:10.1042/bj3040385 · Cited by 112 · see citing works
Iyanagi, T., Watanabe, T., & Uchiyama, Y. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)30079-1 · Cited by 109 · see citing works
Glutathione deficiency increases hepatic ascorbic acid synthesis in adult mice.
Mårtensson, J., & Meister, A. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.23.11566 · Cited by 109 · see citing works
Missing Step in Guinea Pigs Required for the Biosynthesis of L-Ascorbic Acid
Burns, J. J., Peyser, P., & Moltz, A. (1956) · Science · doi:10.1126/science.124.3232.1148-a · Cited by 105 · see citing works
Diliberto, E. J., Dean, G., Carter, C., & Allen, P. L. (1982) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1982.tb03982.x · Cited by 103 · see citing works
Nakagawa, J., Ishikura, S., Asami, J., Isaji, T., Usami, N., Hara, A., Sakurai, T., Tsuritani, K., Oda, K., Takahashi, M., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m110703200 · Cited by 103 · see citing works
The structure of cytochrome b561, a secretory vesicle‐specific electron transport protein.
Perin, M. S., Fried, V. A., Slaughter, C. A., & Südhof, T. C. (1988) · The EMBO Journal · doi:10.1002/j.1460-2075.1988.tb03123.x · Cited by 103 · see citing works
THE EFFECT OF ORGANIC COMPOUNDS UPON VITAMIN C SYNTHESIS IN THE RAT
Longenecker, H. E., Fricke, H. H., & KING, C. G. (1940) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)73119-0 · Cited by 102 · see citing works
Burns, J. J., Evans, C. D., & Trousof, N. (1957) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)70758-8 · Cited by 102 · see citing works
THE SYNTHESIS OF l-ASCORBIC ACID IN THE RAT FROM d-GLUCURONOLACTONE AND l-GULONOLACTONE
Burns, J. J., & Evans, C. D. (1956) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)65088-4 · Cited by 88 · see citing works
Ito, A., Hayashi, S.-I., & Yoshida, T. (1981) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(81)91300-0 · Cited by 83 · see citing works
ASCORBIC ACID SYNTHESIS IN NORMAL AND DRUG-TREATED RATS, STUDIED WITH l-ASCORBIC-1-C14 ACID
Burns, J. J., Mosbach, E. H., & Schulenberg, S. (1954) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)65685-6 · Cited by 82 · see citing works
A Phospholipid-Dependent NADH-Coenzyme Q Reductase from Liver Plasma Membrane
Navarro, F., Villalba, J. M., Crane, F. L., MacKellar, W. C., & Navas, P. (1995) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1995.1947 · Cited by 82 · see citing works
The secretory-vesicle ascorbate-regenerating system: A chain of concerted H+/e−-transfer reactions
Njus, D., & Kelley, P. M. (1993) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(93)90108-r · Cited by 81 · see citing works
Chatterjee, I., Chatterjee, G. C., Ghosh, N., Ghosh, J. J., & Guha, B. C. (1960) · Biochemical Journal · doi:10.1042/bj0740193 · Cited by 79 · see citing works
Purification and characterization of L-gulonolactone oxidase from chicken kidney microsomes
Kiuchi, K., Nishikimi, M., & Yagi, K. (1982) · Biochemistry · doi:10.1021/bi00263a035 · Cited by 78 · see citing works
Ascorbate is regenerated by HL-60 cells through the transplasmalemma redox system
Alcain, F. J., Burón, M. I., Villalba, J. M., & Navas, P. (1991) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(91)90146-8 · Cited by 78 · see citing works
Enzymatic recycling of oxidized ascorbate in pig heart: One-electron vs two-electron pathway
Coassin, M., Tomasi, A., Vannini, V., & Ursini, F. (1991) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(91)90566-2 · Cited by 77 · see citing works
VanDuijn, M. M., Jolanda Van der, Z. E. E., VanSteveninck, J., & den Broek, P. J. A. V. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.22.13415 · Cited by 77 · see citing works
Enzymic Studies on TPN L-Hexonate Dehydrogenase from Rat Liver
Mano, Y., Suzuki, K., Yamada, K., & Shimazono, N. (1961) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a127352 · Cited by 76 · see citing works
Ishikawa, T., Casini, A., & Nishikimi, M. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.44.28708 · Cited by 75 · see citing works
The Ascorbate Transporter of Escherichia coli
Zhang, Z., Aboulwafa, M., Smith, M. H., & Milton H. Saier (2003) · Journal of Bacteriology · doi:10.1128/jb.185.7.2243-2250.2003 · Cited by 74 · see citing works
Kawai, T., Nishikimi, M., Ozawa, T., & Yagi, K. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)36708-0 · Cited by 73 · see citing works
Koshizaka, T., Nishikimi, M., Ozawa, T., & Yagi, K. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)77923-x · Cited by 73 · see citing works
Moreau, V. H., Castilho, R. F., Ferreira, S. T., & Carvalho-Alves, P. C. (1998) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(98)00084-7 · Cited by 71 · see citing works
Inability of bats to synthesise L-ascorbic acid
Birney, E. C., Jenness, R., & Ayaz, K. L. (1976) · Nature · doi:10.1038/260626a0 · Cited by 71 · see citing works
VanDuijn, M. M., Tijssen, K., VanSteveninck, J., den Broek, P. J. A. V., & Jolanda Van der, Z. E. E. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m910281199 · Cited by 70 · see citing works
Aldose and aldehyde reductases in human tissues
Sk, S., Ansari, N. H., Hair, G. A., & Das, B. (1984) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(84)90399-4 · Cited by 67 · see citing works
Aldono- and Uronolactonases of Animal Tissues
Winkelman, J. W., & Lehninger, A. L. (1958) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)64657-5 · Cited by 63 · see citing works
Effects of Some Xenobiotics on Ascorbic Acid Metabolism in Rats
Horio, F., & Yoshida, A. (1982) · Journal of Nutrition · doi:10.1093/jn/112.3.416 · Cited by 62 · see citing works
Purification and characterization of l-gulono-γ-lactone oxidase from rat and goat liver
Nishikimi, M., Tolbert, B. M., & Udenfriend, S. (1976) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(76)90530-0 · Cited by 62 · see citing works
Xu, D. P., Washburn, M. P., Sun, G., & Wells, W. W. (1996) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1996.0555 · Cited by 59 · see citing works
Senescence marker protein‐30 knockout mouse as a novel murine model of senile lung
Mori, T., Ishigami, A., Seyama, K., Onai, R., Kubo, S., Shimizu, K., Maruyama, N., & Fukuchi, Y. (2004) · Pathology International · doi:10.1111/j.1440-1827.2003.01603.x · Cited by 58 · see citing works
Purification and Properties of β-l-Hydroxy Acid Dehydrogenase
Smiley, J. D., & Ashwell, G. (1961) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)64367-4 · Cited by 57 · see citing works
Borgese, N., & Pietrini, G. (1986) · Biochemical Journal · doi:10.1042/bj2390393 · Cited by 56 · see citing works
Ohta, Y., & Nishikimi, M. (1999) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/s0304-4165(99)00123-3 · Cited by 56 · see citing works
Collard, F., Collet, J., Gerin, I., Veiga‐da‐Cunha, M., & SCHAFTINGEN, E. V. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)01247-8 · Cited by 56 · see citing works
Borgese, N., D’Arrigo, A., Silvestris, M. D., & Pietrini, G. (1993) · FEBS Letters · doi:10.1016/0014-5793(93)81416-w · Cited by 56 · see citing works
Localization of a GSH-Dependent Dehydroascorbate Reductase in Rat Tissues and Subcellular Fractions
Paolicchi, A., Pezzini, A., Saviozzi, M., Piaggi, S., Andreuccetti, M., Chieli, E., Malvaldi, G., & Casini, A. (1996) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1996.0419 · Cited by 55 · see citing works
Role of ascorbate in oxidative protein folding
Bánhegyi, G., Csala, M., Szarka, A., Varsányi, M., Benedetti, A., & Mandl, J. (2003) · BioFactors · doi:10.1002/biof.5520170105 · Cited by 55 · see citing works
Ascorbate synthesis‐dependent glutathione consumption in mouse liver
Bánhegyi, G., Csala, M., Braun, L., Garzó, T., & Mandl, J. (1996) · FEBS Letters · doi:10.1016/0014-5793(96)00077-4 · Cited by 51 · see citing works
Shirabe, K., Landi, M. T., Takeshita, M., Uziel, G., Fedrizzi, E., & Borgese, N. (1995) · Europe PMC (PubMed Central) · Cited by 50 · see citing works
Extracellular Reduction of the Ascorbate Free Radical by Human Erythrocytes
May, J. M., Qu, Z., & Cobb, C. E. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.1906 · Cited by 50 · see citing works
Identification of the covalently bound flavin of L-gulono-γ-lactone oxidase
Kenney, W. C., Edmondson, D. E., Singer, T. P., Nakagawa, H., Asano, A., & Sato, R. (1976) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(76)90780-4 · Cited by 50 · see citing works
Oxygen-Accepting Antioxidants Which Arise during Ascorbate Oxidation
Deutsch, J. C. (1998) · Analytical Biochemistry · doi:10.1006/abio.1998.2940 · Cited by 49 · see citing works
Cytochrome b561, ascorbic acid, and transmembrane electron transfer
Fleming, P., & Kent, U. (1991) · American Journal of Clinical Nutrition · doi:10.1093/ajcn/54.6.1173s · Cited by 48 · see citing works
Chatterjee, I. B., Chatterjee, G. C., Ghosh, N., Ghosh, J. J., & Guha, B. C. (1960) · Biochemical Journal · doi:10.1042/bj0760279 · Cited by 47 · see citing works
Evans, C. D., Conney, A. H., Trousof, N., & Burns, J. J. (1960) · Biochimica et Biophysica Acta · doi:10.1016/0006-3002(60)90362-0 · Cited by 46 · see citing works
Mechanism of Ascorbic Acid Regeneration Mediated by Cytochrome b561a
Njus, D., Kelley, P. M., Harnadek, G. J., & Pacquing, Y. V. (1987) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1987.tb27188.x · Cited by 44 · see citing works
Structure prediction for the di-heme cytochrome b 561 protein family
Bashtovyy, D., B�rczi, A., Asard, H., & Páli, T. (2003) · PROTOPLASMA · doi:10.1007/s00709-002-0065-0 · Cited by 43 · see citing works
Isolation and characterization of the gene encoding gluconolactonase from Zymomonas mobilis
Kanagasundaram, V., & Scopes, R. K. (1992) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/0167-4781(92)90120-o · Cited by 43 · see citing works
Mechanism of stimulation of microsomal UDP-glucuronosyltransferase by UDP-N-acetylglucosamine
Bossuyt, X., & Blanckaert, N. J. C. (1995) · Biochemical Journal · doi:10.1042/bj3050321 · Cited by 42 · see citing works
Moreau, R. F., & Dabrowski, K. R. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.17.10279 · Cited by 42 · see citing works
Formation of glucuronic acid from uridinediphosphate glucuronic acid
Ginsburg, V., Weissbach, A., & Maxwell, E. S. (1958) · Biochimica et Biophysica Acta · doi:10.1016/0006-3002(58)90538-9 · Cited by 42 · see citing works
Role of endogenous regucalcin in bone metabolism: Bone loss is induced in regucalcin transgenic rats
Yamaguchi, M., Misawa, H., Uchiyama, S., Morooka, Y., & Tsurusaki, Y. (2002) · International Journal of Molecular Medicine · doi:10.3892/ijmm.10.4.377 · Cited by 41 · see citing works
Villalba, J. M., Canalejo, A., Rodríguez‐Aguilera, J. C., Bur�n, M. I., Morr�, D. J., & Navas, P. (1993) · Journal of Bioenergetics and Biomembranes · doi:10.1007/bf00762467 · Cited by 39 · see citing works
Inhibition kinetics of human kidney aldose and aldehyde reductases by aldose reductase inhibitors
Bhatnagar, A., Liu, S., Das, B., Ansari, N. H., & Sk, S. (1990) · Biochemical Pharmacology · doi:10.1016/0006-2952(90)90292-s · Cited by 38 · see citing works
Puskás, F., Braun, L., Csala, M., Kardon, T., Marcolongo, P., Benedetti, A., Mandl, J., & Bánhegyi, G. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)00678-4 · Cited by 38 · see citing works
Braun, L., Csala, M., Poussu, A. M., Garzó, T., Mandl, J., & Bánhegyi, G. (1996) · FEBS Letters · doi:10.1016/0014-5793(96)00548-0 · Cited by 37 · see citing works
On the microsomal and soluble lactonases
Yamada, K., Ishikawa, S., & Shimazono, N. (1959) · Biochimica et Biophysica Acta · doi:10.1016/0006-3002(59)90576-1 · Cited by 36 · see citing works
Heterologous expression and site-directed mutagenesis of an ascorbate-reducible cytochrome b561
Bérczi, A., Su, D., Lakshminarasimhan, M., Vargas, A., & Asard, H. (2005) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2005.09.006 · Cited by 36 · see citing works
The Enzymatic Defect in Essential Pentosuria
Wang, Y.-M., & van Eys, J. (1970) · New England Journal of Medicine · doi:10.1056/nejm197004162821604 · Cited by 35 · see citing works
Campos, E., Baldomà, L., Aguilar, J., & Badı́a, J. (2004) · Journal of Bacteriology · doi:10.1128/jb.186.6.1720-1728.2004 · Cited by 34 · see citing works
Navas, P., Estévez, A., Burón, M. I., Villalba, J. M., & Crane, F. L. (1988) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(88)90243-4 · Cited by 33 · see citing works
Purification and properties of human liver aldehyde reductases
Petrash, J. M., & Srivastava, S. K. (1982) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(82)90402-2 · Cited by 33 · see citing works
Sorbitol Dehydrogenase from Bovine Lens: Purification and Properties
Marini, I., Bucchioni, L., Borella, P., CORSO, A. D., & Mura, U. (1997) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1997.9882 · Cited by 33 · see citing works
The role of aldonolactonase in the conversion of L-gulonate to L-ascorbate
Bublitz, C., & Lehninger, A. L. (1961) · Biochimica et Biophysica Acta · doi:10.1016/0006-3002(61)90289-x · Cited by 31 · see citing works
Bicarbonate promotes a cleavage of lactone ring of dehydroascorbate
Koshiishi, I., Mamura, Y., & Imanari, T. (1998) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/s0304-4165(97)00106-2 · Cited by 31 · see citing works
Takigami, T., Takeuchi, F., Nakagawa, M., Hase, T., & Tsubaki, M. (2003) · Biochemistry · doi:10.1021/bi0267588 · Cited by 30 · see citing works
Shirabe, K., Yubisui, T., & Takeshita, M. (1989) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/0167-4781(80)90007-x · Cited by 29 · see citing works
Enzymic delactonization of dehydro-l-ascorbate in animal tissues
Kagawa, Y., Takiguchi, H., & Shimazono, N. (1961) · Biochimica et Biophysica Acta · doi:10.1016/0006-3002(61)90196-2 · Cited by 28 · see citing works
Glucuronate, the precursor of vitamin C, is directly formed from UDP‐glucuronate in liver
Linster, C. L., & SCHAFTINGEN, E. V. (2006) · FEBS Journal · doi:10.1111/j.1742-4658.2006.05172.x · Cited by 25 · see citing works
Self-citationLinster, C. L., & SCHAFTINGEN, E. V. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m306593200 · Cited by 25 · see citing works
Self-citationHorio, F., KIMURA, M., & Yoshida, A. (1983) · Journal of Nutritional Science and Vitaminology · doi:10.3177/jnsv.29.233 · Cited by 25 · see citing works
On the nature of l-xylulose reductase deficiency in essential pentosuria
Lane, A. B. (1985) · Biochemical Genetics · doi:10.1007/bf00499113 · Cited by 25 · see citing works
CHRONIC PENTOSURIA AND MIGRAINE
MARGOLIS, J. I. (1929) · The American Journal of the Medical Sciences · doi:10.1097/00000441-192903000-00005 · Cited by 24 · see citing works
Intragenic deletion in the gene encoding L-gulonolactone oxidase causes vitamin C deficiency in pigs
Hasan, L., V�geli, P., Stoll, P., KramerStranzinger, P. P. G., & Neuenschwander, S. (2004) · Mammalian Genome · doi:10.1007/s00335-003-2324-6 · Cited by 24 · see citing works
Enzymic formation of l-xylulose from β-keto-l-gulonic acid
Winkelman, J. W., & Ashwell, G. (1961) · Biochimica et Biophysica Acta · doi:10.1016/0006-3002(61)90914-3 · Cited by 24 · see citing works
Structural and Functional Characterization of Rabbit and Human l-Gulonate 3-Dehydrogenase
Ishikura, S. (2005) · The Journal of Biochemistry · doi:10.1093/jb/mvi033 · Cited by 24 · see citing works
Extracellular ascorbate stabilization: Enzymatic or chemical process?
Rodríguez‐Aguilera, J. C., & Navas, P. (1994) · Journal of Bioenergetics and Biomembranes · doi:10.1007/bf00762778 · Cited by 24 · see citing works
Sakai, K., Morishita, Y., Ishikawa, S., Miura, T., Nemoto, T., Mori, M., & Shimizu, Y. (1999) · The FASEB Journal · Cited by 24 · see citing works
Horio, F., Shibata, T., Makino, S., Machino, S., Hayashi, Y., Hattori, T., & Yoshida, A. (1993) · Journal of Nutrition · doi:10.1093/jn/123.12.2075 · Cited by 23 · see citing works
Thioltranferase Mediated Ascorbate Recycling in Human Lens Epithelial Cells
Fernando, M. R., Satake, M., Monnier, V. M., & Lou, M. F. (2003) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.03-0545 · Cited by 20 · see citing works
Enzymatic Studies on Ascorbic Add Catabolism in Animals
Kagawa, Y., & Takiguchi, H. (1962) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a127521 · Cited by 19 · see citing works
Titani, K., Ishikura, H., & Minakami, S. (1957) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a126779 · Cited by 19 · see citing works
Assay, Purification, and Properties of Bovine Liver D-Xylulokinase
Dills, W. L., Parsons, P. D., Westgate, C. L., & Komplin, N. J. A. (1994) · Protein Expression and Purification · doi:10.1006/prep.1994.1039 · Cited by 18 · see citing works
Gluconeogenesis from ascorbic acid: ascorbate recycling in isolated murine hepatocytes
Braun, L., Puskás, F., Csala, M., Gyórffy, E., Garzó, T., Mandl, J., & Bánhegyi, G. (1996) · FEBS Letters · doi:10.1016/0014-5793(96)00654-0 · Cited by 18 · see citing works
Stirpe, F., & Comporti, M. (1965) · Biochemical Journal · doi:10.1042/bj0950354 · Cited by 17 · see citing works
Eliceiri, G. L., Lai, E. K., & McCay, P. B. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)83447-0 · Cited by 17 · see citing works
Tamari, M., Daigo, Y., Ishikawa, S., & Nakamura, Y. (1998) · Cytogenetic and Genome Research · doi:10.1159/000015076 · Cited by 17 · see citing works
Braun, L., Mile, V., Schaff, Z., Csala, M., Kardon, T., Mandl, J., & Bánhegyi, G. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)01184-9 · Cited by 17 · see citing works
Hochman, Y., & Zakim, D. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)91043-4 · Cited by 16 · see citing works
No enzymatic activities are necessary for the stabilization of ascorbic acid by K‐562 cells
Schweinzer, E., Waeg, G., Esterbauer, H., & Goldenberg, H. (1993) · FEBS Letters · doi:10.1016/0014-5793(93)81691-r · Cited by 16 · see citing works
Campos, E., Aguilar, J., Baldomà, L., & Badı́a, J. (2002) · Journal of Bacteriology · doi:10.1128/jb.184.21.6065-6068.2002 · Cited by 16 · see citing works
Puhakainen, E. V., & Hänninen, O. (1976) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1976.tb10007.x · Cited by 15 · see citing works
Forouhar, F., Lee, I., Benach, J., Kulkarni, K., Xiao, R., Acton, T., Montelione, G. T., & Tong, L. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313580200 · Cited by 12 · see citing works
Uchiyama, S., & Yamaguchi, M. (2004) · International Journal of Molecular Medicine · doi:10.3892/ijmm.14.3.451 · Cited by 12 · see citing works
Glycogenolysis is directed towards ascorbate synthesis by glutathione conjugation
Chan, T. S., Wilson, J. X., & O’Brien, P. J. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.03.022 · Cited by 11 · see citing works
Stabilization of Extracellular Ascorbate Mediated by Coenzyme Q Transmembrane Electron Transport
Arroyo, A., Rodríguez‐Aguilera, J. C., Santos‐Ocaña, C., Villalba, J. M., & Navas, P. (2004) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(04)78017-9 · Cited by 10 · see citing works
Preliminary X-ray data of NADH-cytochrome b5 reductase from human erythrocytes
Takano, T., Ogawa, K., Sato, M., Bando, S., & Yubisui, T. (1987) · Journal of Molecular Biology · doi:10.1016/0022-2836(87)90195-1 · Cited by 10 · see citing works
Griffin, B. W. (1992) · Enzyme and Microbial Technology · doi:10.1016/0141-0229(92)90107-y · Cited by 10 · see citing works
Moreau, R. F., & Dabrowski, K. R. (1998) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(98)00114-2 · Cited by 10 · see citing works
Isolation of ascorbate free radical reductase from rabbit lens soluble fraction
Bando, M., Inoue, T., Oka, M. T., Nakamura, K., Kawai, K., Obazawa, H., Kobayashi, S., & Takehana, M. (2004) · Experimental Eye Research · doi:10.1016/j.exer.2004.08.011 · Cited by 7 · see citing works
VanDuijn, M. M., Buijs, J. T., Jolanda Van der, Z. E. E., & den Broek, P. J. A. V. (2001) · PROTOPLASMA · doi:10.1007/bf01289418 · Cited by 6 · see citing works
Flagged first, then by citations
1 of the 159 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Ascorbic acid: Chemistry, biology and the treatment of cancer
Du, J., Cullen, J. J., & Buettner, G. R. (2012) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2012.06.003 · Cited by 1,071 · see citing works
Cadmium stress: an oxidative challenge
Cuypers, A., Plusquin, M., Remans, T., Jozefczak, M., Keunen, E., Gielen, H., Opdenakker, K., Nair, A. R., Munters, E., Artois, T., et al. (2010) · BioMetals · doi:10.1007/s10534-010-9329-x · Cited by 1,058 · see citing works
Yun, J., Mullarky, E., Lu, C., Bosch, K. N., Kavalier, A., Rivera, K., Roper, J., Chio, I. I. C., Giannopoulou, E. G., Rago, C., et al. (2015) · Science · doi:10.1126/science.aaa5004 · Cited by 913 · see citing works
Vitamin C: The known and the unknown and Goldilocks
Padayatty, S., & Levine, M. (2016) · Oral Diseases · doi:10.1111/odi.12446 · Cited by 753 · see citing works
Ascorbic acid metabolism and functions: A comparison of plants and mammals
Smirnoff, N. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.03.033 · Cited by 683 · see citing works
Protein Disulfide Isomerase: A Critical Evaluation of Its Function in Disulfide Bond Formation
Hatahet, F., & Ruddock, L. W. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2466 · Cited by 673 · see citing works
Antioxidant Compounds and Their Antioxidant Mechanism
Santos-Sánchez, N. F., Salas-Coronado, R., Villanueva‐Cañongo, C., & Hernández, B. (2019) · IntechOpen eBooks · doi:10.5772/intechopen.85270 · Cited by 616 · see citing works
Role of Reactive Oxygen Species (ROS) in Therapeutics and Drug Resistance in Cancer and Bacteria
Allimuthu, D. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b01243 · Cited by 583 · see citing works
Santos, C. X. C., Tanaka, L. Y., Wosniak, J., & Laurindo, F. R. M. (2009) · Antioxidants & Redox Signaling · doi:10.1089/ars.2009.2625 · Cited by 572 · see citing works
Ascorbic acid: The chemistry underlying its antioxidant properties
Njus, D., Kelley, P. M., Tu, Y., & Schlegel, H. B. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.07.013 · Cited by 565 · see citing works
Vitamin C-Sources, Physiological Role, Kinetics, Deficiency, Use, Toxicity, and Determination
Doseděl, M., Jirkovský, E., Macáková, K., Krčmová, L., Javorská, L., Pourová, J., Mercolini, L., Remião, F., Nováková, L., Mladěnka, P., et al. (2021) · Nutrients · doi:10.3390/nu13020615 · Cited by 553 · see citing works
The Aldo-Keto Reductase Superfamily and its Role in Drug Metabolism and Detoxification
Barski, O. A., Tipparaju, S. M., & Bhatnagar, A. (2008) · Drug Metabolism Reviews · doi:10.1080/03602530802431439 · Cited by 543 · see citing works
Direct and indirect antioxidant properties of inducers of cytoprotective proteins
Dinkova‐Kostova, A. T., & Talalay, P. (2008) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.200700195 · Cited by 535 · see citing works
Interplay between Metabolism and Epigenetics: A Nuclear Adaptation to Environmental Changes
Etchegaray, J., & Mostoslavsky, R. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.05.029 · Cited by 521 · see citing works
Dietary selenium's protective effects against methylmercury toxicity
Ralston, N. V. C., & Raymond, L. J. (2010) · Toxicology · doi:10.1016/j.tox.2010.06.004 · Cited by 500 · see citing works
Vitamin C: Update on physiology and pharmacology
Mandl, J., Szarka, A., & Bánhegyi, G. (2009) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2009.00282.x · Cited by 451 · see citing works
Individual variability in human blood metabolites identifies age-related differences
Chaleckis, R., Murakami, I., Takada, J., Kondoh, H., & Yanagida, M. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1603023113 · Cited by 373 · see citing works
The Genetics of Vitamin C Loss in Vertebrates
Drouin, G., Godin, J. R. P., & Pagé, B. (2011) · Current Genomics · doi:10.2174/138920211796429736 · Cited by 359 · see citing works
Keshari, K. R., & Wilson, D. M. (2013) · Chemical Society Reviews · doi:10.1039/c3cs60124b · Cited by 357 · see citing works
The role of antioxidants in sperm freezing: a review
Amidi, F., Pazhohan, A., Nashtaei, M. S., Khodarahmian, M., & Nekoonam, S. (2016) · Cell and Tissue Banking · doi:10.1007/s10561-016-9566-5 · Cited by 342 · see citing works
Male infertility testing: reactive oxygen species and antioxidant capacity
Ko, E., Sabanegh, E. S., & Agarwal, A. K. (2014) · Fertility and Sterility · doi:10.1016/j.fertnstert.2014.10.020 · Cited by 336 · see citing works
Vitamin C in Plants: From Functions to Biofortification
Paciolla, C., Fortunato, S., Dipierro, N., Paradiso, A., Leonardis, S. D., Mastropasqua, L., & de Pinto, M. C. (2019) · Antioxidants · doi:10.3390/antiox8110519 · Cited by 330 · see citing works
Regulation of the epigenome by vitamin C
Young, J. I., Züchner, S., & Wang, G. (2015) · Annual Review of Nutrition · doi:10.1146/annurev-nutr-071714-034228 · Cited by 319 · see citing works
Ascorbate as seen through plant evolution: the rise of a successful molecule?
Gest, N., Gautier, H., & Stevens, R. G. (2012) · Journal of Experimental Botany · doi:10.1093/jxb/ers297 · Cited by 292 · see citing works
Nguyen, V. D., Saaranen, M. J., Karala, A., Lappi, A., Wang, L., Raykhel, I. B., Alanen, H. I., Salo, K. E. H., Wang, C.-C., & Ruddock, L. W. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.12.039 · Cited by 266 · see citing works
Vitamin C in Health and Disease: Its Role in the Metabolism of Cells and Redox State in the Brain
Figueroa-Méndez, R., & Rivas-Arancibia, S. (2015) · Frontiers in Physiology · doi:10.3389/fphys.2015.00397 · Cited by 265 · see citing works
Lane, D. J. R., & Richardson, D. R. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.07.007 · Cited by 264 · see citing works
Plant-Derived Natural Antioxidants in Meat and Meat Products
Manessis, G., Kalogianni, A. I., Lazou, T. P., Moschovas, M., Bossis, I., & Gelasakis, A. Ι. (2020) · Antioxidants · doi:10.3390/antiox9121215 · Cited by 260 · see citing works
The Roles and Mechanisms of Actions of Vitamin C in Bone: New Developments
Aghajanian, P., Hall, S. L., Wongworawat, M. D., & Mohan, S. (2015) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.2709 · Cited by 232 · see citing works
Antioxidants in Translational Medicine
Schmidt, H. H. H. W., Stocker, R., Vollbracht, C., Paulsen, G., Riley, D. P., Daiber, A., & Cuadrado, A. (2015) · Antioxidants and Redox Signaling · doi:10.1089/ars.2015.6393 · Cited by 231 · see citing works
Vitamin C increases viral mimicry induced by 5-aza-2′-deoxycytidine
Liu, M., Ohtani, H., Zhou, W., Ørskov, A. D., Charlet, J., Zhang, Y. W., Shen, H., Baylin, S. B., Liang, G., Grønbæk, K., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1612262113 · Cited by 225 · see citing works
Antioxidant supplements and semen parameters: An evidence based review
Ahmadi, S., Bashiri, R., Ghadiri‐Anari, A., & Nadjarzadeh, A. (2016) · International Journal of Reproductive BioMedicine (IJRM) · doi:10.29252/ijrm.14.12.729 · Cited by 224 · see citing works
Boo, Y. C. (2022) · Antioxidants · doi:10.3390/antiox11091663 · Cited by 218 · see citing works
Dietary vitamin C in human health
Granger, M., & Eck, P. (2018) · Advances in food and nutrition research · doi:10.1016/bs.afnr.2017.11.006 · Cited by 217 · see citing works
Metabolic biomarkers related to oxidative stress and antioxidant status in Saudi autistic children
Al-Gadani, Y., El-Ansary, A. K., Al-Attas, O., & AL-Ayadhi, L. Y. (2009) · Clinical Biochemistry · doi:10.1016/j.clinbiochem.2009.03.011 · Cited by 216 · see citing works
Nzou, G., Wicks, R. T., Wicks, E. E., Seale, S. A., Sane, C. H., Chen, A.-D., Murphy, S. V., Jackson, J. D., & Atala, A. (2018) · Scientific Reports · doi:10.1038/s41598-018-25603-5 · Cited by 214 · see citing works
Desai, K. M., Chang, T., Wang, H., Banigesh, A., Dhar, A., Liu, J., Untereiner, A. A., & Wu, L. (2010) · Canadian Journal of Physiology and Pharmacology · doi:10.1139/y10-001 · Cited by 211 · see citing works
l-Ascorbate biosynthesis in higher plants: the role of VTC2
Linster, C. L., & Clarke, S. G. (2008) · Trends in Plant Science · doi:10.1016/j.tplants.2008.08.005 · Cited by 202 · see citing works
Self-citationMicronutritional approaches to periodontal therapy
Van der Velden, U., Kuzmanova, D., & Chapple, I. L. C. (2011) · Journal of Clinical Periodontology · doi:10.1111/j.1600-051x.2010.01663.x · Cited by 199 · see citing works
Vitamin C in stem cell reprogramming and cancer
Cimmino, L., Neel, B. G., & Aifantis, I. (2018) · Trends in Cell Biology · doi:10.1016/j.tcb.2018.04.001 · Cited by 197 · see citing works
Alves, F. M., Lane, D. J. R., Nguyen, T. P. M., Bush, A. I., & Ayton, S. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-02088-5 · Cited by 197 · see citing works
Cellular pathways for transport and efflux of ascorbate and dehydroascorbate
Corti, A., Casini, A. F., & Pompella, A. (2010) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2010.05.014 · Cited by 193 · see citing works
Bohndiek, S. E., Kettunen, M. I., Hu, D., Kennedy, B. W. C., Boren, J., Gallagher, F. A., & Brindle, K. M. (2011) · Journal of the American Chemical Society · doi:10.1021/ja2045925 · Cited by 190 · see citing works
Potential Mechanisms of Action for Vitamin C in Cancer: Reviewing the Evidence
Vissers, M. C. M., & Das, A. B. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.00809 · Cited by 188 · see citing works
The Gel State of the Vitreous and Ascorbate-Dependent Oxygen Consumption
Shui, Y. B. (2009) · Archives of Ophthalmology · doi:10.1001/archophthalmol.2008.621 · Cited by 188 · see citing works
Wheeler, G. L., Ishikawa, T., Pornsaksit, V., & Smirnoff, N. (2015) · eLife · doi:10.7554/elife.06369 · Cited by 187 · see citing works
Kim, Y., Kim, H., Bae, S., Choi, J., Lim, S., Lee, N., Kong, J. M., Hwang, Y.-I., Kang, J. S., & Lee, W. J. (2013) · Immune Network · doi:10.4110/in.2013.13.2.70 · Cited by 186 · see citing works
Linster, C. L., Gomez, T. A., Christensen, K. C., Adler, L. N., Young, B. D., Brenner, C., & Clarke, S. G. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702094200 · Cited by 186 · see citing works
Self-citationAntioxidant Defenses in the ocular surface
Chen, Y., Mehta, G., & Vasiliou, V. (2009) · The Ocular Surface · doi:10.1016/s1542-0124(12)70185-4 · Cited by 182 · see citing works
Vitamin C: a wound healing perspective
Moores, J. (2013) · British Journal of Community Nursing · doi:10.12968/bjcn.2013.18.sup12.s6 · Cited by 175 · see citing works
Scientific Opinion on Dietary Reference Values for vitamin C
EFSA Panel on Dietetic Products, N. A. A. (. (2013) · EFSA Journal · doi:10.2903/j.efsa.2013.3418 · Cited by 173 · see citing works
Cerullo, G., Negro, M., Parimbelli, M., Pecoraro, M., Perna, S., Liguori, G., Rondanelli, M., Cena, H., & D’Antona, G. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.574029 · Cited by 171 · see citing works
Gazdik, Z., Zitka, O., Petrlova, J., Adam, V., Zehnalek, J., Horna, A., Reznicek, V., Beklova, M., & Kizek, R. (2008) · Sensors · doi:10.3390/s8117097 · Cited by 170 · see citing works
Ripoli, M. C., D’Aprile, A., Quarato, G., Sinnreich, M. F., Gouttenoire, J., Scrima, R., Cela, O., Boffoli, D., Heim, M. H., Moradpour, D., et al. (2009) · Journal of Virology · doi:10.1128/jvi.00769-09 · Cited by 169 · see citing works
Vitamin C and Cardiovascular Disease: An Update
Morelli, M. B., Gambardella, J., Castellanos, V., Trimarco, V., & Santulli, G. (2020) · Antioxidants · doi:10.3390/antiox9121227 · Cited by 169 · see citing works
Vitamin C and the Role of Citrus Juices as Functional Food
Martí, N., Mena, P. R., Cánovas, J. A., Micol, V., & Saura, D. (2009) · Natural Product Communications · doi:10.1177/1934578x0900400506 · Cited by 168 · see citing works
Kuiper, C., & Vissers, M. C. M. (2014) · Frontiers in Oncology · doi:10.3389/fonc.2014.00359 · Cited by 163 · see citing works
Plants need their vitamins too
Smith, A. G., Croft, M. T., Moulin, M., & Webb, M. E. (2007) · Current Opinion in Plant Biology · doi:10.1016/j.pbi.2007.04.009 · Cited by 162 · see citing works
Hyperpolarized 13 C dehydroascorbate as an endogenous redox sensor for in vivo metabolic imaging
Keshari, K. R., Kurhanewicz, J. V., Bok, R., Larson, P. E. Z., Vigneron, D. B., & Wilson, D. M. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1106920108 · Cited by 160 · see citing works
Halal Cosmetics: A Review on Ingredients, Production, and Testing Methods
Sugibayashi, K., Yusuf, E., Todo, H., Dahlizar, S., Sakdiset, P., Arce, F. J., & See, G. L. (2019) · Cosmetics · doi:10.3390/cosmetics6030037 · Cited by 157 · see citing works
Rajoka, M. S. R., Thirumdas, R., Mehwish, H. M., Umair, M., Khurshid, M., Hayat, H. F., Phimolsiripol, Y., Pallarés, N., Martí-Quijal, F. J., & Barba, F. J. (2021) · Antioxidants · doi:10.3390/antiox10101563 · Cited by 157 · see citing works
Dietary antioxidants and oxidative stress from a human and plant perspective: a review.
Andre, C., Larondelle, Y., & Evers, D. (2010) · Current Nutrition & Food Science · doi:10.2174/157340110790909563 · Cited by 157 · see citing works
Sands, D. C., Morris, C. E., Dratz, E. A., & Pilgeram, A. L. (2009) · Plant Science · doi:10.1016/j.plantsci.2009.07.011 · Cited by 155 · see citing works
Duodenal Cytochrome b (DCYTB) in Iron Metabolism: An Update on Function and Regulation
Lane, D. J. R., Bae, D.-H., Merlot, A. M., Sahni, S., & Richardson, D. R. (2015) · Nutrients · doi:10.3390/nu7042274 · Cited by 153 · see citing works
Regulation of vitamin C homeostasis during deficiency
Lindblad, M., Tveden-Nyborg, P., & Lykkesfeldt, J. (2013) · Nutrients · doi:10.3390/nu5082860 · Cited by 151 · see citing works
VTC4 Is a Bifunctional Enzyme That Affects Myoinositol and Ascorbate Biosynthesis in Plants
Torabinejad, J., Donahue, J. L., Gunesekera, B., Allen-Daniels, M. J., & Gillaspy, G. E. (2009) · PLANT PHYSIOLOGY · doi:10.1104/pp.108.135129 · Cited by 151 · see citing works
Maione-Silva, L., de Castro, E. G., Nascimento, T. L., Cintra, E. R., Moreira, L. C., Cintra, B. A. S., Valadares, M. C., & Lima, E. M. (2019) · Scientific Reports · doi:10.1038/s41598-018-36682-9 · Cited by 148 · see citing works
Balter, V., Lamboux, A., Zazzo, A., Télouk, P., Leverrier, Y., Marvel, J., MOLONEY, A. P., Monahan, F. J., Schmidt, O., & Albarède, F. (2013) · Metallomics · doi:10.1039/c3mt00151b · Cited by 144 · see citing works
Hiller, M., Schaar, B. T., Indjeian, V. B., Kingsley, D. M., Hagey, L. R., & Bejerano, G. (2012) · Cell Reports · doi:10.1016/j.celrep.2012.08.032 · Cited by 144 · see citing works
Hemavathi, Upadhyaya, C. P., Young, K. E., Nookaraju, A., Kim, H. S., Heung, J. J., Oh, O. M., Aswath, C. R., Chun, S. C., Kim, D. H., et al. (2009) · Plant Science · doi:10.1016/j.plantsci.2009.08.004 · Cited by 143 · see citing works
Old Things New View: Ascorbic Acid Protects the Brain in Neurodegenerative Disorders
Covarrubias‐Pinto, A., Acuña, A. I., Beltrán, F. A., Torres-Díaz, L., & Castro, M. A. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms161226095 · Cited by 140 · see citing works
Bioactive Compounds in Mango (Mangifera indica L.)
Ribeiro, S. M. R., & Schieber, A. (2009) · Elsevier eBooks · doi:10.1016/b978-0-12-374628-3.00034-7 · Cited by 136 · see citing works
Industrial Production of l-Ascorbic Acid (Vitamin C) and d-Isoascorbic Acid
Pappenberger, G., & Hohmann, H. (2013) · Advances in biochemical engineering, biotechnology · doi:10.1007/10_2013_243 · Cited by 133 · see citing works
Vitamin C in Stem Cell Biology: Impact on Extracellular Matrix Homeostasis and Epigenetics
D’Aniello, C., Cermola, F., Patriarca, E. J., & Minchiotti, G. (2017) · Stem Cells International · doi:10.1155/2017/8936156 · Cited by 132 · see citing works
Yang, B., & Shi, J. (2020) · Journal of the American Chemical Society · doi:10.1021/jacs.0c09984 · Cited by 127 · see citing works
Rivas, C. I., Zuñiga, F. A., Salas-Burgos, A., Mardones, L., Ormazábal, V., & Vera, J. C. (2008) · Journal of Physiology and Biochemistry · doi:10.1007/bf03174092 · Cited by 127 · see citing works
Nonenzymatic Exogenous and Endogenous Antioxidants
Moussa, Z., Judeh, Z. M. A., & Ahmed, S. A. (2019) · IntechOpen eBooks · doi:10.5772/intechopen.87778 · Cited by 123 · see citing works
Vitamin C in the Treatment of COVID-19
Milani, G. P., Macchi, M., & Guz‐Mark, A. (2021) · Nutrients · doi:10.3390/nu13041172 · Cited by 121 · see citing works
Ascorbic acid intake and oxalate synthesis
Knight, J. L., Madduma-Liyanage, K., Mobley, J. A., Assimos, D. G., & Holmes, R. P. (2016) · Urolithiasis · doi:10.1007/s00240-016-0868-7 · Cited by 119 · see citing works
Zito, E., Hansen, H. G., Yeo, G. S. H., Fujii, J., & Ron, D. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.08.010 · Cited by 116 · see citing works
The Biochemistry and Effectiveness of Antioxidants in Food, Fruits, and Marine Algae
Pruteanu, L.-L., Bailey, D. S., Grădinaru, A. C., & Jäntschi, L. (2023) · Antioxidants · doi:10.3390/antiox12040860 · Cited by 114 · see citing works
Vitamin C restores healthy aging in a mouse model for Werner syndrome
Massip, L., Garand, C., Paquet, É. R., Cogger, V. C., O'Reilly, J. N., Tworek, L., Hatherell, A., Taylor, C. G., Thorin, É., Zahradka, P. C., et al. (2009) · The FASEB Journal · doi:10.1096/fj.09-137133 · Cited by 114 · see citing works
Myths, Artifacts, and Fatal Flaws: Identifying Limitations and Opportunities in Vitamin C Research
Michels, A., & Frei, B. (2013) · Nutrients · doi:10.3390/nu5125161 · Cited by 111 · see citing works
Boddupalli, S. S., Mein, J. R., Lakkanna, S., & James, D. R. (2012) · Frontiers in Genetics · doi:10.3389/fgene.2012.00007 · Cited by 110 · see citing works
Strategies to increase vitamin C in plants: from plant defense perspective to food biofortification
Locato, V., Cimini, S., & Gara, L. D. (2013) · Frontiers in Plant Science · doi:10.3389/fpls.2013.00152 · Cited by 108 · see citing works
Oxalate in renal stone disease: the terminal metabolite that just won't go away
Marengo, S. R., & Romani, A. M. (2008) · Nature Clinical Practice Nephrology · doi:10.1038/ncpneph0845 · Cited by 106 · see citing works
Gabbay, K. H., Bohren, K. M., Morello, R., Bertin, T., Liu, J., & Vogel, P. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.110247 · Cited by 105 · see citing works
Epigenetic Regulation of Genomic Stability by Vitamin C
Brabson, J. P., Leesang, T. E., Mohammad, S., & Cimmino, L. (2021) · Frontiers in Genetics · doi:10.3389/fgene.2021.675780 · Cited by 105 · see citing works
Urzica, E. I., Adler, L. N., Page, M. D., Linster, C. L., Arbing, M. A., Casero, D., Pellegrini, M. A., Merchant, S., & Clarke, S. G. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.341982 · Cited by 103 · see citing works
Self-citationGlyoxalase 1 Modulation in Obesity and Diabetes
Rabbani, N., & Thornalley, P. J. (2019) · Antioxidants & Redox Signaling · doi:10.1089/ars.2017.7424 · Cited by 102 · see citing works
Protection and controlled release of vitamin C by different micro/nanocarriers
Comunian, T. A., Babazadeh, A., Rehman, A., Shaddel, R., Akbari‐Alavijeh, S., Boostani, S., & Jafari, S. M. (2020) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2020.1865258 · Cited by 100 · see citing works
Leferink, N. G. H., van den Berg, W., & van Berkel, W. J. H. (2008) · FEBS Journal · doi:10.1111/j.1742-4658.2007.06233.x · Cited by 99 · see citing works
Inactivation dates of the human and guinea pig vitamin C genes
Lachapelle, M. Y., & Drouin, G. (2010) · Genetica · doi:10.1007/s10709-010-9537-x · Cited by 98 · see citing works
Psychopharmacology of COVID-19
Bilbul, M., Paparone, P., Kim, A. M., Mutalik, S. P., & Ernst, C. L. (2020) · Psychosomatics · doi:10.1016/j.psym.2020.05.006 · Cited by 95 · see citing works
The effect of Vitamin C on melanin pigmentation – A systematic review
Sanadi, R. M., & Deshmukh, R. S. (2020) · Journal of Oral and Maxillofacial Pathology · doi:10.4103/jomfp.jomfp_207_20 · Cited by 95 · see citing works
Alós, E., Rodrigo, M. J., & Zacarı́as, L. (2014) · Planta · doi:10.1007/s00425-014-2044-z · Cited by 95 · see citing works
Montecinos, V. P., Guzman, P. C. C., Barra, V., Villagrán, M., Muñoz-Montesino, C., Sotomayor, K., Escobar, E., Godoy, A., Mardones, L., Sotomayor, P. C., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m608361200 · Cited by 95 · see citing works
The participation of oxidative stress in the pathogenesis of bronchial asthma
Kleniewska, P., & Pawliczak, R. (2017) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2017.07.066 · Cited by 92 · see citing works
Thompson, C. M., Proctor, D. M., Suh, M., Haws, L. C., Kirman, C. R., & Harris, M. A. (2013) · Critical Reviews in Toxicology · doi:10.3109/10408444.2013.768596 · Cited by 90 · see citing works
Tocopherol metabolism, oxidation and recycling under high light stress in Arabidopsis
Kobayashi, N., & DellaPenna, D. (2008) · The Plant Journal · doi:10.1111/j.1365-313x.2008.03539.x · Cited by 90 · see citing works
- Authors
- Linster, C. L., & Van Schaftingen, E.
- Affiliations
- de Duve Institute (BE)
- ORCID
- Linster, Carole L.
- Venue
- The FEBS Journal
- Publisher
- Wiley
- Published
- 2006-12-06
- Volume
- 274
- Issue
- 1
- Pages
- 1-22
- ISSN
- 1742-464X (ISSN-L)
- 1742-4658
- OpenAlex
- W2065016714
- Cited by
- 757
- References
- 159
- Citations by year
- 2026: 20 · 2025: 42 · 2024: 66 · 2023: 46 · 2022: 49 · 2021: 61 · 2020: 65 · 2019: 36 · 2018: 26 · 2017: 31 · 2016: 34 · 2015: 31 · 2014: 38 · 2013: 44 · 2012: 37
- FWCI
- 2.57
- Type
- journal article
- Language
- en
- Open access
- green
- orbilu.uni.lu
- Licence
- Locations
- FEBS Journal (publishedVersion)
- PubMed (publishedVersion)
- Digital Access to Libraries (submittedVersion)
- Open Repository and Bibliography (University of Luxembourg) (submittedVersion, cc-by-nc-sa)
- Topics
- Health Sciences › Nursing › Nutrition and Dietetics › Vitamin C and Antioxidants Research
- Health Sciences › Medicine › Biochemistry › Antioxidant Activity and Oxidative Stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Keywords
- vitamin C, ascorbic acid biosynthesis, UDP-glucuronate, UDP-glucuronosyltransferase, aldehyde reductase, aldo-keto reductase superfamily, L-gulonolactone oxidase, SMP30, regucalcin, dehydroascorbic acid, glutathione, vitamin C degradation, scurvy
- MeSH terms
- Animals, Ascorbic Acid, Carbohydrate Dehydrogenases, Escherichia coli, Glucuronates, Humans, Hydrolysis, Mammals, Models, Biological, Pentose Phosphate Pathway, Uridine Diphosphate Glucuronic Acid, L-Gulonolactone Oxidase
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review