The DOI matches its Crossref record; 197 of the 202 references it cites were found in a registry or an index.
Enzymes of serine metabolism in normal, developing and neoplastic rat tissues
Abstract
1.|The cellular pattern of serine metabolism was conceptualized into four main areas of metabolic sequences: the biosynthesis of serine from intermediates of the glycolytic pathway (the so-called “phosphorylated pathway”); and alternative pathways of serine utilization initiated by serine dehydratase, serine aminotransferase and serine hydroxymethyltransferase. 2.|The known regulatory and adaptive properties of the enzymes involved in these pathways were reviewed in detail and key enzymes associated with each pathway (phosphoserine aminotransferase, serine dehydratase, serine aminotransferase, and serine hydroxymethyltransferase, respectively) were selected for further investigation. 3.|Tissue distribution studies in the rat revealed that whereas serine dehydratase and serine aminotransferase activities were largely confined to the liver, phosphoserine aminotransferase and serine hydroxymethyltransferase activities were more broadly distributed. In particular in tissues with a high rate of cell turnover, phosphoserine aminotransferase and serine hydroxymethyltransferase activities were coordinately increased. An increase in serine hydroxymethyltransferase activity coincided temporally with the incorporation of [3-14C]serine and thymidine into DNA in normal human lymphocytes during proliferation after mitogenic stimulation by phytohemagglutinin. The evidence suggested a primarily gluconeogenic role for serine dehydratase and serine aminotransferase. Serine hydroxymethyl-transferase has a role in providing glycine and one-carbon folate co-factors as precursors for nucleotide biosynthesis and in some situations serves to metabolically couple the pathway of serine biosynthesis to utilization for de novo purine and pyrimidine synthesis. 4.|Multiple enzymic forms were distinguished for serine dehydratase, serine aminotransferase and serine hydroxymethyltransferase. For serine dehydratase the two cytosolic multiple forms had no apparent functional significance; the multiple forms were catalytically unmodified by conditions promoting phosphorylation-dephosphorylation in vitro. The mitochondrial form of serine aminotransferase showed adaptive responses in gluconcogenic situations, and the hypothesis was proposed that the mitochondrial isoenzyme of serine hydroxymethyltransferase is associated together with serine aminotransferase in a pathway for gluconeogenesis from protein-derived amino acids such as glycine and hydroxyproline. 5.|The adaptive behaviour of the enzymes during the neonatal development of rat liver revealed that serine aminotransferase reached a peak in the mid-suckling period at a time when gluconcogenesis is known to be increased. Use of phosphoenolypyruvate carboxykinase inhibitors (mercaptopicolinate or quinolinate) supported a pathway via serine aminotransferase for gluconeogenesis from serine and hydroxyproline at this developmental stage. The concept of the involvement in a carbon salvage pathway to deal with increased body collagen turnover at this time was advanced. The developmental adaptation of serine aminotransferase at birth was shown to involve glucagon, acting via cyclic AMP, and to be dependent on transcriptional gene regulation. 6.|Serine dehydratase showed a biphasic developmental pattern, similar to other enzymes involved in amino acid catabolism. The peaks of activity at the early neonatal and weaning developmental stages were shown to involve the joint action of glucagon, acting via cyclic AMP, and corticosteroid hormones. The inductions were dependent, at least initially, on transcriptional gene regulation but the precise mechanistic role of the two classes of hormone has yet to be defined. At both developmental peaks the distribution of serine dehydratase multiple forms was identical, and differential developmental regulation of the forms was not involved in determining the overall pattern of serine dehydratase development. 7.|Phosphoserine aminotransferase and cytosolic serine hydroxymethyl-transferase showed similar developmental patterns with a peak of activity in the perinatal period. This coincides with an active period of hepatocyte proliferation and of nucleotide biosynthesis. A further rise of serine hydroxymethyltransferase coinciding with a second postnatal surge of proliferative hepatocellular growth was independent of de novo serine biosynthesis and reflected increased provision of serine from dietary sources. 8.|A survey of the key enzymes of serine metabolism in transplantable rat neoplasms revealed that, in general, serine dehydratase and serine aminotransferase were deleted from the cellular repertoire of metabolic capacities. In contrast, phosphoserine aminotransferase and serine hydroxymethyltransferase were selectively retained to varying degrees in neoplastic tissues. 9.|The pattern of serine metabolism displayed in normal, developing and neoplastic tissues revealed an integrated, genetically-programmed, response of enzymes of serine biosynthesis and of alt
Overview
Integrity signals
Registry
Cites
Statistics
Verification
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?
In the citing paper
“Increased activity of de novo serine synthesis enzymes in cancer has been observed for more than 30 years (Snell, 1984; Snell et al., 1988).”
From Targeting Metabolism for Cancer Therapy (2017) · cites this paper as Snell, 1984
Citations
Cites
The role of protein phosphorylation in neural and hormonal control of cellular activity
Cohen, P. (1982) · Nature · doi:10.1038/296613a0 · Cited by 1,126
Weber, G. F. (1977) · New England Journal of Medicine · doi:10.1056/nejm197703032960905 · Cited by 650
Weber, G. F. (1983) · PubMed · Cited by 547
Control of Gluconeogenesis in Liver
Exton, J. H., & Park, C. R. (1967) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)99617-1 · Cited by 496
Weber, G. F. (1977) · New England Journal of Medicine · doi:10.1056/nejm197703102961005 · Cited by 416
The rate of gluconeogenesis from various precursors in the perfused rat liver
Ross, B. D., Hems, R., & Krebs, H. A. (1967) · Biochemical Journal · doi:10.1042/bj1020942 · Cited by 408
The glycine cleavage system: Composition, reaction mechanism, and physiological significance
Kikuchi, G. (1973) · Molecular and Cellular Biochemistry · doi:10.1007/bf01659328 · Cited by 361
A Symposium on Amino Acid Metabolism
Neuberger, A. (1956) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(56)90075-3 · Cited by 314
The Biochemical development of the fetus and neonate
Jones, C. T. (1982) · Medical Entomology and Zoology · Cited by 264
Some aspects of the regulation of fuel supply in omnivorous animals
Krebs, H. A. (1972) · Advances in Enzyme Regulation · doi:10.1016/0065-2571(72)90025-8 · Cited by 249
Research works printed but not linked: 6
- Walker, 1968, Developmental aspects of carbohydrate metabolism, Vol. 1, 465
- Machovich, 1972, Thymidine kinase in rat tissues during growth and differentiation, Biochim. Biophys. Acta, 286, 375, 10.1016/0304-4165(72)90273-5 · DOI
- Nakagawa, 1969, Studies on substrate induction of serine dehydratase of rat liver, J. Biochem., 66, 549, 10.1093/oxfordjournals.jbchem.a129180 · DOI
- Ichihara, 1957, Studies on the purification and properties of d-glyceric acid kinase of liver, J. Biol. Chem., 225, 949, 10.1016/S0021-9258(18)64892-6 · DOI
- Remesy, 1983, Control of hepatic utilization of serine, glycine and threonine in fed and starved rat, J. Nutr., 113, 28, 10.1093/jn/113.1.28 · DOI
- Metz, 1972, Comparative studies on the influence of quinolinic acid on the metabolism of l-serine and l-alanine in the isolated perfused rat liver, Hoppe-Seyler's Z. Physiol. Chem., 353, 1496
Cited by
Sorted by citations
Items 201–269 of 269
Resistant to Targeted Therapy - Aim for Metabolic Liabilities
Queiroz, A. L., Vakifahmetoglu-Norberg, H., & Norberg, E. (2018) · Theranostics · doi:10.7150/thno.24454 · Cited by 8
“Although, PHGDH has been associated to human cancers for more than 30 years [8], more recently, the Vander Heiden lab [9] and the Sabatini lab [10] identified PHGDH as often amplified or overexpressed in breast and melanoma tumors.”
ResultWünschiers, R., Jahn, M., Jahn, D., Schomburg, I., Peifer, S., Heinzle, E., BURTSCHER, H. J., Garbe, J., Steen, A., Schobert, M., et al. (2012) · Wiley eBooks · doi:10.1002/9781118657072.ch3 · Cited by 8
Zhang, Y., Li, R., Zheng, D., Zhao, J., Qing, K., He, R., Ma, Z., Chen, J., Xue, N., Tian, X., et al. (2025) · The Plant Cell · doi:10.1093/plcell/koaf126 · Cited by 8
“(Ser or serine is short for L-serine below) In bacteria and mammals, serine is primarily synthesized via the phosphorylated pathway of serine biosynthesis (PPSB), which begins with the glycolytic intermediate 3-phosphoglycerate (3-PGA) (Pizer 1963; Snell 1984; Dey et al. 2005).”
Fatal cerebral edema associated with serine deficiency in CSF
Keularts, I. M. L. W., Leroy, P. L. J. M., Rubio‐Gozalbo, M. E., Spaapen, L. J. M., Weber, B., Dorland, B., de Koning, T. J., & Verhoeven‐Duif, N. M. (2010) · Journal of Inherited Metabolic Disease · doi:10.1007/s10545-010-9067-9 · Cited by 7
“L-Serine, a nonessential amino acid, plays an important role in cellular proliferation (Snell 1984).”
TAKASAKI, C., Miura, E., & Watanabe, M. (2007) · Biomedical Research · doi:10.2220/biomedres.28.61 · Cited by 7
“Introduction L-Serine is classified as a non-essential amino acid, since it can be synthesized sufficiently in human and animal bodies and the nitrogen balance is maintained without dietary intake (Snell, 1984).”
BackgroundInfluentialKanamoto, R., Fujita, K., KUMASAKI, M., Imai, S., Kotaru, M., SAEKI, T., & Iwami, K. (2004) · Bioscience Biotechnology and Biochemistry · doi:10.1271/bbb.68.888 · Cited by 7
Masuda, T., Ogawa, H., Matsushima, T., Kawamata, S., Sasahara, M., Kuroda, K., Suzuki, Y., Takata, Y., Yamazaki, M., Takusagawa, F., et al. (2003) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(02)00302-3 · Cited by 6
Zhang, D., Pan, J., Zhou, H., & Cao, Y. (2020) · Zoological Letters · doi:10.1186/s40851-020-00159-3 · Cited by 6
Crystallization and preliminary crystallographic analysis of human serine dehydratase
Sun, L., Li, X., Dong, Y.-J., Yang, M., Liu, Y., Han, X., Zhang, X., Pang, H., & Rao, Z. (2003) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444903020110 · Cited by 6
“Extensive studies have been carried out on SDH from rat and the enzyme has been found to play an important role in gluconeogenesis; its activity is induced by the consumption of high-protein diets, starvation and other treatments (Snell, 1984; Ebara et al., 2001).”
BackgroundRegulatory elements for the tissue-specific expression of the rat serine dehydratase-encoding gene
Su, Y., Kanamoto, R., Ogawa, H., & Pilot, H. C. (1992) · Gene · doi:10.1016/0378-1119(92)90110-b · Cited by 6
The gene encoding rat 3-phosphoglycerate dehydrogenase
Robbi, M., Achouri, Y., Szpirer, C., & SCHAFTINGEN, E. V. (2000) · Mammalian Genome · doi:10.1007/s003350010189 · Cited by 6
“PHGDH appears also to be quite active in proliferating cells (Snell 1984), most likely owing to transcriptional regulation (Cho et al.”
BackgroundMatsuda, K., Noda, C., Fukushima, C., & Ichihara, A. (1991) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(91)90936-2 · Cited by 6
HPLC Monitoring of Spontaneous Non-Linear Peptidization Dynamics of Selected Amino Acids in Solution
Godziek, A., Maciejowska, A., Sajewicz, M., & Kowalska, T. (2014) · Journal of Chromatographic Science · doi:10.1093/chromsci/bmu122 · Cited by 5
Wang, T., Sun, Y., Zhao, Y., Huang, J., & Huang, Y. (2024) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2023.1332287 · Cited by 5
“SDSL is an enzyme with serine dehydratase-like activity that is primarily found in the liver (27).”
BackgroundUrine Metabolome during Parturition
Gevi, F., Meloni, A., Mereu, R., Lelli, V., Chiodo, A., Ragusa, A., & Timperio, A. M. (2020) · Metabolites · doi:10.3390/metabo10070290 · Cited by 6
“The importance of serine metabolism during fetal development is underscored by its role as a precursor of nucleotide biosynthesis during the rapid growth phase in neonatal rats [31,32] and as a source of the one-carbon pool for nucleotide synthesis and during cell proliferation [33].”
BackgroundPeragón, J., Barroso, J. B., de la Higuera, M., & Lupiáñez, J. A. (2007) · Journal of Experimental Zoology Part A Ecological Genetics and Physiology · doi:10.1002/jez.429 · Cited by 5
Castagné, V., Finot, P. A., & Maire, J.-C. E. (1994) · Life Sciences · doi:10.1016/0024-3205(94)00576-1 · Cited by 5
Haque, M. R., Hirowatari, A., Koyanagi, A., Ichinose, T., Abiru, M., Mohri, S., Furuya, S., & Yamamoto, K. (2019) · Archives of Insect Biochemistry and Physiology · doi:10.1002/arch.21553 · Cited by 4
Wang, Z., Jiang, Y.-R., Sun, Y., Li, Q., Li, Y.-P., Du, Z.-J., Liu, Y., & Qin, L. (2013) · Biochemical Systematics and Ecology · doi:10.1016/j.bse.2013.01.006 · Cited by 4
Metabolic Reprogramming and Molecular Rewiring in Cancer: Therapeutic Opportunities
Meiliana, A., Dewi, N. M., & Wijaya, A. (2021) · The Indonesian Biomedical Journal · doi:10.18585/inabj.v13i2.1598 · Cited by 3
MicroRNA-mediated reprogramming of glucose, fatty acid and amino acid metabolism in cancer
Ding, J., Wen, Y., Yuan, X., & He, X. (2022) · Genome Instability & Disease · doi:10.1007/s42764-022-00078-x · Cited by 4
“3-phosphoserine is dephosphorylated by the final enzyme in the pathway, phosphoserine phosphatase (PSPH), to produce serine (Snell, 1984).”
BackgroundSubedi, A., Muroi, M., Futamura, Y., Kawamura, T., Aono, H., Nishi, M., Ryo, A., Watanabe, N., & Osada, H. (2019) · FEBS Letters · doi:10.1002/1873-3468.13361 · Cited by 4
Haque, M. R., Hirowatari, A., Saruta, F., Furuya, S., & Yamamoto, K. (2019) · Insect Molecular Biology · doi:10.1111/imb.12609 · Cited by 4
“This non-essential amino acid is also necessary for the production of sphingolipids, porphyrins and neuromodulators in living organisms (Snell, 1984; Snyder and Kim, 2000).”
BackgroundOcular Manifestations of Inborn Errors of Metabolism
Ganesh, A., Al-Murshedi, F., Al-Zuhaibi, S. S., & Al‐Thihli, K. (2017) · Springer eBooks · doi:10.1007/978-3-319-18389-3_13 · Cited by 5
l-serine and GABA uptake by synaptosomes during postnatal development of rat
Cheluja, M. G., Scolari, M. J., Coelho, T. M., Blake, M. G., Boccia, M. M., Baratti, C. M., & Acosta, G. B. (2006) · Comparative Biochemistry and Physiology Part A Molecular & Integrative Physiology · doi:10.1016/j.cbpa.2005.12.012 · Cited by 4
Loss of NOL10 leads to impaired disease progression of NUP98::DDX10 leukemia
Shima, Y., Yamagata, K., Kuroki, Y., Sasaki, K., Aikawa, Y., & Kitabayashi, I. (2025) · Leukemia · doi:10.1038/s41375-025-02607-5 · Cited by 3
“Increased production of serine by cells is one of the metabolic changes associated with carcinogenesis [25, 26].”
Yamamoto, K., Mohri, S., & Furuya, S. (2020) · Archives of Insect Biochemistry and Physiology · doi:10.1002/arch.21751 · Cited by 3
(2013) · CRC Press eBooks · doi:10.1201/b14661-4 · Cited by 3
Foster, G. D., Zhang, J., & Moon, T. W. (1994) · Fish Physiology and Biochemistry · doi:10.1007/bf00004120 · Cited by 3
Non-canonical function of PHGDH promotes HCC metastasis by interacting with METTL3
Cheng, B., Ma, J., Tang, N., Liu, R. R., Peng, P., & Wang, K. (2024) · Cellular Oncology · doi:10.1007/s13402-024-01029-2 · Cited by 2
“PHGDH, a pivotal metabolic enzyme in the serine syn - thesis pathway, is frequently overexpressed in various tumors and contributes to malignant progression through multiple mechanisms [ 11, 34–36].”
PLK1-mediated phosphorylation of PHGDH reprograms serine metabolism in advanced prostate cancer
Rao, X., Allison, D. B., Flight, R. M., Lin, P., He, D., Li, Z., Zhang, Y., Wang, R., Li, C., Wang, J., et al. (2026) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2618349123 · Cited by 2
Kumar, S. M., Pampa, K. J., Manjula, M., Kumar, G. H., KUNISHIMA, N., & Lokanath, N. K. (2014) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2014.07.075 · Cited by 2
Thangaraj, S. V., Bellingham, M., Lea, R. G., Evans, N. P., Sinclair, K. D., & Padmanabhan, V. (2025) · Environmental Pollution · doi:10.1016/j.envpol.2025.125630 · Cited by 2
Peragón, J., de la Higuera, M., & Lupiáñez, J. A. (2010) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/j.cbpb.2010.06.005 · Cited by 2
“In rat, this enzyme has a gluconeogenic character and helps to regulate hepatic glucose biosynthesis from serine in different dietary and hormonal states (Snell, 1984).”
BackgroundLuo, H., Hong, R., Xu, Y., Zheng, Q., Xia, W., Lu, Q., Jiang, K., Xu, F., Chen, M., Shi, D., et al. (2023) · Gland Surgery · doi:10.21037/gs-23-6 · Cited by 2
Molecular Structure of Phosphoserine Aminotransferase from Saccharomyces cerevisiae
Jang, J., & Chang, J. H. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24065139 · Cited by 2
Ogawa, H., & Ansai, Y. (1995) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/0305-0491(95)00053-b · Cited by 2
Interaction of adrenal and pancreatic hormones in the control of hepatic enzymes during development
Böhme, H.-J., Belay, D., Dettmer, D., Goltzsch, W., Hofmann, E., Lange, R., Schubert, C., Schulze, E., Sparmann, G. H., & Weiss, E. (1987) · Advances in Enzyme Regulation · doi:10.1016/0065-2571(87)90005-7 · Cited by 2
Khan, A., Siddiqui, S. I., Husain, S. A., Mazurek, S., & Iqbal, M. A. (2020) · doi:10.22541/au.160684227.70170021/v1 · Cited by 2
Perán, S., Muñoz, M., & Saiz, M. T. (1991) · Springer eBooks · doi:10.1007/978-1-4757-9601-8_9 · Cited by 2
Zhuyuan, Y., Meng, X., Zong, Z., Song, Q., Huo, Y., & Chen, H. (2025) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2025.120570 · Cited by 4
Korwitz-Reichelt, A., Schulke, D., Walter, M., & Sass, J. O. (2025) · Journal of Inherited Metabolic Disease · doi:10.1002/jimd.70119 · Cited by 1
Pinton, F., Rimskaya-Korsakova, N. N., Felbel, K., Grimmer, E., & Hejnol, A. (2026) · BMC Biology · doi:10.1186/s12915-026-02506-w · Cited by 3
“The upregulated host transcripts we could characterise are serine dehydratase and transient receptor potential cation channel M. Serine dehydratase is an enzyme converting serine into pyruvate [234], the starting substrate for Krebs cycle [235].”
Metabolic Enzymes: The Novel Targets for Cancer Stem Cells
Li, J. L. P. (2014) · Journal of Stem Cell Research & Therapy · doi:10.4172/2157-7633.1000197 · Cited by 1
“Phosphoglycerate dehydrogenase (PHDGH) catalyzes the first step of the serine biosynthetic pathway downstream of glycolysis, which is a metabolic gatekeeper both for macromolecular biosynthesis and serine-dependent DNA synthesis [29].”
BackgroundWahl, D. R., & Venneti, S. (2017) · Springer eBooks · doi:10.1007/978-3-319-61401-4_6 · Cited by 1
Glycine, Serine and the One‐Carbon Pool
Bender, D. A. (2012) · doi:10.1002/9781118357514.ch4 · Cited by 1
The Fate of Glutamine in Human Metabolism. The interplay with glucose in proliferating cellsPreprint
Mazat, J., & Ransac, S. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/477224 · Cited by 1
“In his pioneer work, Snell 314 demonstrated the importance of serine biosynthesis in rat carcinoma [35].”
BackgroundHulea, L., Gravel, S., Morita, M., Cargnello, M., Uchenunu, O., Im, Y. K., McLaughlan, S., Larsson, O. S., Ohh, M., Ferreira, T., et al. (2018) · SSRN Electronic Journal · doi:10.2139/ssrn.3155732 · Cited by 1
Weber, G. (1987) · Springer eBooks · doi:10.1007/978-1-4757-9564-6_1
Postnatal development of the glycine cleavage system in rat liver
Kalbag, S. S., & Palekar, A. G. (1990) · Biochemical Medicine and Metabolic Biology · doi:10.1016/0885-4505(90)90017-u
Konno, A., Oota, Y., Hashimoto, Y., Kon, Y., & Iwanaga, T. (2004) · Biomedical Research · doi:10.2220/biomedres.25.195
EXAMINING THE ROLE OF METABOLISM IN MYC-DRIVEN TUMORIGENESIS
Forshell, L. P., & Zi, T. (2011)
Role of SIRT6 in Metabolic Reprogramming During Colorectal Carcinoma
Sebastián, C. (2014) · Defense Technical Information Center (DTIC) · doi:10.21236/ada614181
Hattingen, E., & Pilatus, U. (2014) · Medical radiology · doi:10.1007/174_2014_1031
Dissecting the molecular mechanisms of breast cancer bone metastasis for therapeutic targeting
Pollari, S. (2012) · UTUPub (University of Turku)
Smith, C., & Wood, E. (1992) · Springer eBooks · doi:10.1007/978-94-011-2356-3_7
Peleias, F. S. (2017) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/t.85.2017.tde-10082017-120230
Profiling L-serine Transport Throughout Growth and Meiotic Maturation in Mouse Oocytes
Zhang, H. (2019) · uO Research (University of Ottawa) · doi:10.20381/ruor-23495
Investigation of phosphoserine aminotransferase 1(PSAT1) in breast cancer progression.
Metcalf, S. A. (2019) · ThinkIR: The University of Louisville's Institutional Repository (University of Louisville) · doi:10.18297/etd/3345
van carbolines, H. V., Schouten, O., & Amsterdam, G. T. (2012)
(2012) · Wiley eBooks · doi:10.1002/9781118357514.biblio
One-carbon metabolism in lung cancer
Yao, S. (2020) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-8273
Approaches to Study Tumor Metabolism in MicePreprint
Gültekin, Y., Heiden, M. G. V., & Lien, E. C. (2023) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a041420
Rare forms of hypomyelination and delayed myelination
Mura, E., Parazzini, C., & Tonduti, D. (2024) · Handbook of clinical neurology · doi:10.1016/b978-0-323-99209-1.00002-8
Marchant, M. (2026) · Zenodo (CERN European Organization for Nuclear Research) · doi:10.5281/zenodo.19389875
BindingDB (2024) · UC San Diego · doi:10.7270/q2pg1wxw
Metadata
- Authors
- Snell, K.
- Venue
- Advances in Enzyme Regulation
- Publisher
- Elsevier BV
- Published
- 1984-01
- Volume
- 22
- Pages
- 325-400
- ISSN
- 0065-2571 (ISSN-L)
- OpenAlex
- W1979511656
- Cited by
- 267
- References
- 202
- Citations by year
- 2026: 2 · 2025: 6 · 2024: 5 · 2023: 9 · 2022: 7 · 2021: 11 · 2020: 9 · 2019: 10 · 2018: 14 · 2017: 8 · 2016: 7 · 2015: 9 · 2014: 12 · 2013: 6 · 2012: 9
- FWCI
- 2.37
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Advances in Enzyme Regulation (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Amino Acid Enzymes and Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Molecular Research
- Health Sciences › Nursing › Nutrition and Dietetics › Folate and B Vitamins Research
- Keywords
- serine metabolism, serine dehydratase, serine hydroxymethyltransferase, phosphoserine aminotransferase, gluconeogenesis, nucleotide synthesis, isozymes, tissue distribution, cell proliferation, lymphocytes, phytohemagglutinin
- MeSH terms
- Transaminases, Animals, Carbohydrate Dehydrogenases, Cell Division, Cell Line, DNA, Female, Fetus, Growth, Isoenzymes, Liver, Male, Neoplasms, Phosphoric Monoester Hydrolases, Rats, Inbred Strains, Serine, L-Serine Dehydratase, Glycine Hydroxymethyltransferase, Subcellular Fractions, Tissue Distribution, Phosphoglycerate Dehydrogenase, Rats
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
