Reversion of a Chinese Hamster Cell Auxotrophic Mutant
Open accessAbstract
A mutant cell strain derived from a Chinese hamster line by mutagenesis with ethylmethane sulfonate requires glycine for growth. In the wild type, glycine synthesis is catalyzed by serine hydroxymethyltransferase (EC 2.1.2.1). Cell fractionation by differential centrifugation and isopycnic sucrose gradient analysis reveals that the enzyme activity is found in both the mitochondrial and cytosol fractions. The specific activity in the mitochondrial fraction is about 20 times higher than in the cytosol, and is much more stable to thermal inactivation. The glycine-requiring mutant has lost all of the mitochondrial enzyme activity, while retaining the cytosol activity. The mutant is very stable but can be induced to revert by several chemical mutagens. One glycine-independent revertant induced by ethyl methane sulfonate was studied in detail. Serine hydroxymethyltransferase activity is again present in the mitochondrial fraction, at about [unk] of the wild-type level. However, the revertant mitochondrial enzyme exhibits an altered thermal sensitivity, with a half-life at 45° of 55 min as compared to 180 min in the wild type. The half-life for the cytosol enzyme in all three strains is 7 min. Mixing experiments demonstrate that the heat lability of the revertant enzyme is not due to a dissociable factor in the extract. The data are consistent with the idea that the original mutation occurred in the structural gene for one isozyme of the enzyme and that the revertant has undergone a second mutation in this gene, partially restoring enzyme activity.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The text we found for this paper looks like another document, so the self-check wasn’t run.
Cites
PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENT
Lowry, O. H., Rosebrough, N., Farr, A. L., & Randall, R. (1951) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)52451-6 · Cited by 315,771 · see citing works
Clonal growth of mammalian cells in a chemically defined, synthetic medium
Ham, R. G. (1965) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.53.2.288 · Cited by 559 · see citing works
Kao, F., & Puck, T. T. (1968) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.60.4.1275 · Cited by 461 · see citing works
Chu, E. H. Y., & Malling, H. V. (1968) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.61.4.1306 · Cited by 374 · see citing works
Genetics of somatic mammalian cells. IX. Quantitation of mutagenesis by physical and chemical agents
Kao, F., & Puck, T. T. (1969) · Journal of Cellular Physiology · doi:10.1002/jcp.1040740305 · Cited by 243 · see citing works
Mutation rates in cells at different ploidy levels
Harris, M. (1971) · Journal of Cellular Physiology · doi:10.1002/jcp.1040780204 · Cited by 172 · see citing works
Mitochondrial DNA: Physicochemical Properties, Replication, and Genetic Function
Borst, P., & Kroon, A. M. (1969) · International review of cytology · doi:10.1016/s0074-7696(08)61635-6 · Cited by 171 · see citing works
Amino Acid Replacements and the Genetic CodePreprint
Yanofsky, C., Ito, J., & Horn, V. (1966) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.1966.031.01.023 · Cited by 163 · see citing works
Tissue fractionation. Past and present.
Duve, C. D. (1971) · PubMed · Cited by 162 · see citing works
Chemical Mutagenesis at the Phosphoribosyltransferase Locus in Cultured Human Lymphoblasts
Sato, K., Slesinski, R. S., & Littlefield, J. W. (1972) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.69.5.1244 · Cited by 141 · see citing works
The effect of ploidy on chemical mutagenesis in cultured chinese hamster cells
Chasin, L. A. (1973) · Journal of Cellular Physiology · doi:10.1002/jcp.1040820218 · Cited by 140 · see citing works
Self-citationBeaudet, A. L., Roufa, D. J., & Caskey, C. T. (1973) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.70.2.320 · Cited by 140 · see citing works
GENETICS OF SOMATIC MAMMALIAN CELLS, X. COMPLEMENTATION ANALYSIS OF GLYCINE-REQUIRING MUTANTS
Kao, F., Chasin, L. A., & Puck, T. T. (1969) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.64.4.1284 · Cited by 131 · see citing works
Self-citationThe structural gene for yeast cytochrome C.
Sherman, F., Stewart, J. W., Margoliash, E., Parker, J., & Campbell, W. (1966) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.55.6.1498 · Cited by 119 · see citing works
Mammalian Cells with Altered Forms of RNA Polymerase II
Chan, V., Whitmore, G. F., & Siminovitch, L. (1972) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.69.11.3119 · Cited by 116 · see citing works
Albrecht, A., Biedler, J. L., & Hutchison, D. J. (1972) · PubMed · Cited by 102 · see citing works
Effect of Ploidy and Mutagens on Bromodeoxyuridine Resistance in Haploid and Diploid Frog Cells
Mezger‐Freed, L. (1972) · Nature New Biology · doi:10.1038/newbio235245a0 · Cited by 95 · see citing works
Studies on serine hydroxymethylase isoenzymes from rat liver
Nakano, Y., Fujioka, M., & Wada, H. (1968) · Biochimica et Biophysica Acta (BBA) - Enzymology · doi:10.1016/0005-2744(68)90240-4 · Cited by 67 · see citing works
Fujioka, M. (1969) · Biochimica et Biophysica Acta (BBA) - Enzymology · doi:10.1016/0005-2744(69)90427-6 · Cited by 60 · see citing works
Mitochondrial protein synthesis in HeLa cells
Galper, J., & Darnell, J. E., Jr. (1971) · Journal of Molecular Biology · doi:10.1016/0022-2836(71)90354-8 · Cited by 56 · see citing works
Chemical Reactivity of Chromosomal DNA as Related to Mutagenicity: Studies with Human Cell LinesPreprint
Szybalski, W. (1964) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.1964.029.01.019 · Cited by 37 · see citing works
Wang, F. K., Koch, J., & Stokstad, E. L. R. (1967) · PubMed · Cited by 32 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
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 multifaceted contributions of mitochondria to cellular metabolism
Spinelli, J. B., & Haigis, M. C. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0124-1 · Cited by 1,935 · 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
Isolation of Chinese hamster cell mutants deficient in dihydrofolate reductase activity
Urlaub, G., & Chasin, L. A. (1980) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.77.7.4216 · Cited by 876 · see citing works
Self-citationChapter 1 Folate‐Mediated One‐Carbon Metabolism
Fox, J. T., & Stover, P. J. (2008) · Vitamins & Hormones · doi:10.1016/s0083-6729(08)00401-9 · Cited by 402 · 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
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
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
Ritacco, F. V., Wu, Y., & Khetan, A. (2018) · Biotechnology Progress · doi:10.1002/btpr.2706 · Cited by 263 · see citing works
Toward a better understanding of folate metabolism in health and disease
Zheng, Y., & Cantley, L. C. (2018) · The Journal of Experimental Medicine · doi:10.1084/jem.20181965 · Cited by 235 · see citing works
Genetic Approaches to Steroid Hormone Action
Yamamoto, K. R., Stampfer, M. R., Gehring, U., & Sibley, C. H. (1976) · Elsevier eBooks · doi:10.1016/b978-0-12-571132-6.50008-7 · Cited by 198 · see citing works
Hsie, A. W., Brimer, P. A., Mitchell, T. J., & Gosslee, D. G. (1975) · Somatic Cell and Molecular Genetics · doi:10.1007/bf01538449 · Cited by 193 · see citing works
Maaheimo, H., Fiaux, J., Çakar, Z. P., Bailey, J. E., Sauer, U., & Szyperski, T. (2001) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2001.02126.x · Cited by 181 · see citing works
Nguyen, H. T., Medford, R. M., & Nadal‐Ginard, B. (1983) · Cell · doi:10.1016/0092-8674(83)90159-9 · Cited by 151 · see citing works
Griffin, J. E. (1979) · Journal of Clinical Investigation · doi:10.1172/jci109624 · Cited by 134 · 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
SHMT inhibition is effective and synergizes with methotrexate in T-cell acute lymphoblastic leukemia
García‐Cañaveras, J. C., Lancho, O., Ducker, G. S., Ghergurovich, J. M., Xu, X., da Silva-Diz, V., Minuzzo, S. A., Indraccolo, S., Kim, H., Herranz, D., et al. (2020) · Leukemia · doi:10.1038/s41375-020-0845-6 · Cited by 129 · see citing works
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
Molecular analysis of spontaneous somatic mutants
Adetugbo, K., Milstein, C., & Secher, D. S. (1977) · Nature · doi:10.1038/265299a0 · Cited by 118 · see citing works
Somatic mutation as the basis for malignant transformation of BHK cells by chemical carcinogens
Bouck, N., & di Mayorca, G. (1976) · Nature · doi:10.1038/264722a0 · Cited by 114 · see citing works
Mitochondrial One-Carbon Pathway Supports Cytosolic Folate Integrity in Cancer Cells
Zheng, Y., Lin, T.-Y., Lee, G., Paddock, M. N., Momb, J., Cheng, Z., Li, Q., Fei, D. L., Stein, B. D., Ramsamooj, S., et al. (2018) · Cell · doi:10.1016/j.cell.2018.09.041 · Cited by 106 · see citing works
Cossins, E. A. (1980) · Elsevier eBooks · doi:10.1016/b978-0-12-675402-5.50015-5 · Cited by 100 · see citing works
Physiology of cultured animal cells
Doverskog, M., Ljunggren, J., Öhman, L., & Häggström, L. (1997) · Journal of Biotechnology · doi:10.1016/s0168-1656(97)00172-7 · Cited by 98 · see citing works
McNeil, J. B., McIntosh, E. M., Taylor, B. V., Zhang, F., Tang, S., & Bognar, A. L. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)37089-8 · Cited by 96 · see citing works
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
Rosenstraus, M., & Chasin, L. A. (1975) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.72.2.493 · Cited by 91 · see citing works
Self-citationSerine hydroxymethyltransferase and threonine aldolase: are they identical?
Ogawa, H., Gomi, T., & Fujioka, M. (2000) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(99)00113-2 · Cited by 84 · see citing works
Shannon, K. W., & Rabinowitz, J. C. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)68558-8 · Cited by 82 · see citing works
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
Lowe, K. E., Osborne, C., Lin, B., Kim, J. S., Hsu, J. C., & Shane, B. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)80593-6 · Cited by 78 · see citing works
Monschau, N., Stahmann, K. ‐., Sahm, H., McNeil, J. B., & Bognar, A. L. (2006) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.1997.tb10349.x · Cited by 75 · see citing works
Patterson, D., & Carnright, D. V. (1977) · Somatic Cell and Molecular Genetics · doi:10.1007/bf01539120 · Cited by 75 · see citing works
Christensen, K. E., & MacKenzie, R. E. (2008) · Vitamins and hormones · doi:10.1016/s0083-6729(08)00414-7 · Cited by 73 · see citing works
Sources and Sinks of Serine in Nutrition, Health, and Disease
Handzlik, M. K., & Metallo, C. M. (2023) · Annual Review of Nutrition · doi:10.1146/annurev-nutr-061021-022648 · Cited by 73 · see citing works
McCarthy, E. A., Titus, S. A., Taylor, S. M., Jackson‐Cook, C. K., & Moran, R. G. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m403677200 · Cited by 68 · see citing works
Patel, H., Pietro, E. D., & MacKenzie, R. E. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301718200 · Cited by 62 · see citing works
Chromosome-Wide Event Accompanies the Expression of Recessive Mutations in Tetraploid Cells
Chasin, L. A., & Urlaub, G. (1975) · Science · doi:10.1126/science.1167702 · Cited by 61 · see citing works
Self-citationNegative control of the helix-loop-helix family of myogenic regulators in the NFB mutant
Peterson, C. A., Gordon, H., Hall, Z. W., Paterson, B. M., & Blau, H. M. (1990) · Cell · doi:10.1016/0092-8674(90)90014-6 · Cited by 61 · see citing works
Mimosine Targets Serine Hydroxymethyltransferase
Lin, H.-B., Falchetto, R. A., Mosca, P. J., Shabanowitz, J., Hunt, D. F., & Hamlin, J. L. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.5.2548 · Cited by 59 · see citing works
Intramitochondrial localization and proposed metabolic significance of serine transhydroxymethylase
Cybulski, R. L., & Fisher, R. R. (1976) · Biochemistry · doi:10.1021/bi00660a004 · Cited by 51 · see citing works
Selective Systems in Somatic Cell Genetics
Chu, E. H. Y., & Powell, S. S. (1976) · Springer eBooks · doi:10.1007/978-1-4757-0659-8_5 · Cited by 51 · see citing works
Lin, B., & Shane, B. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)36940-5 · Cited by 46 · see citing works
Pind, S., Slominski, E., Mauthe, J., Pearlman, K., Swoboda, K. J., Wilkins, J. A., Sauder, P. J., & Natowicz, M. R. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m111419200 · Cited by 43 · see citing works
Genetic Aspects of Folate Metabolism
Erbe, R. W. (1979) · Springer eBooks · doi:10.1007/978-1-4615-8276-2_5 · Cited by 41 · see citing works
Wurm, M. J., & Wurm, F. M. (2021) · Biotechnology Journal · doi:10.1002/biot.202100165 · Cited by 40 · see citing works
Pietro, E. D., Wang, X.-L., & MacKenzie, R. E. (2004) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2004.06.014 · Cited by 39 · see citing works
SOMATIC CELL GENETICS AND ITS APPLICATION TO MEDICINE
Puck, T. T., & Kao, F. (1982) · Annual Review of Genetics · doi:10.1146/annurev.ge.16.120182.001301 · Cited by 39 · see citing works
Zelikson, R., & Luzzati, M. (1977) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1977.tb11808.x · Cited by 37 · see citing works
Folate Biochemical Pathways and Their Regulation
Stover, P. J. (2009) · CRC Press eBooks · doi:10.1201/9781420071252-c3 · Cited by 35 · see citing works
Suicide substrates for mitochondrial enzymes
Alston, T. A. (1981) · Pharmacology & Therapeutics · doi:10.1016/0163-7258(81)90074-7 · Cited by 31 · see citing works
Cadigan, K. M., Chang, C. C. Y., & Chang, T. (1989) · The Journal of Cell Biology · doi:10.1083/jcb.108.6.2201 · Cited by 30 · see citing works
Folate Biochemistry and the Metabolism of One-Carbon Units
Cossins, E. A. (1987) · Elsevier eBooks · doi:10.1016/b978-0-12-675411-7.50015-x · Cited by 28 · see citing works
Matthews, R. G., Drummond, J. T., & Webb, H. K. (1998) · Advances in Enzyme Regulation · doi:10.1016/s0065-2571(97)00006-x · Cited by 26 · see citing works
A mammalian cell mutant with temperature-sensitive thymidine kinase
NAKANO, M. M., Sekiguchi, T., & Yamada, M. (1978) · Somatic Cell and Molecular Genetics · doi:10.1007/bf01538982 · Cited by 25 · see citing works
Fenwick, R. G., Wasmuth, J. J., & Caskey, C. T. (1977) · Somatic Cell and Molecular Genetics · doi:10.1007/bf01551815 · Cited by 24 · see citing works
Kohl, R. L., Perez-Polo, J. R., & Quay, W. B. (1980) · Journal of Neuroscience Research · doi:10.1002/jnr.490050403 · Cited by 21 · see citing works
A web site for the computational analysis of yeast regulatory sequences
van Helden, J., Andr�, B., & Collado‐Vides, J. (2000) · Yeast · doi:10.1002/(sici)1097-0061(20000130)16:2 · Cited by 179 · see citing works
Role of DNA Repair in Mutation and Cancer Production
Trosko, J. E., & Chang, C. (1976) · Springer eBooks · doi:10.1007/978-1-4757-1662-7_20 · Cited by 18 · see citing works
Biochemical and Molecular Studies of Human Methenyltetrahydrofolate Synthetase
Jolivet, J., Dayan, A., Beauchemin, M., Chahla, D., Mamo, A., & Bertrand, R. (1996) · Stem Cells · doi:10.1002/stem.140033 · Cited by 17 · see citing works
Defining the steps of the folate one-carbon shuffle and homocysteine metabolism
Cook, R. (2000) · American Journal of Clinical Nutrition · doi:10.1093/ajcn/72.6.1419 · Cited by 17 · see citing works
Tremblay, G. B., Mejia, N. R., & MacKenzie, R. E. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42439-8 · Cited by 13 · see citing works
Häggström, L. (2000) · doi:10.1002/0471250570.spi040 · Cited by 12 · see citing works
Mutants of Chinese hamster ovary cells with altered glucose-6-phosphate dehydrogenase activity
Rosenstraus, M., & Chasin, L. A. (1977) · Somatic Cell and Molecular Genetics · doi:10.1007/bf01538750 · Cited by 12 · see citing works
Self-citationYe, Y., Chan, Y.-T., Liu, H.-C., Lu, H.-T., & Huang, R.-F. S. (2009) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2009.05.005 · Cited by 11 · see citing works
Byrne, P. C., SHIPLEY, J. M., Chave, K. J., Sanders, P. G., & Snell, K. (1996) · Human Genetics · doi:10.1007/bf02185768 · Cited by 11 · see citing works
Revertants of an S49 Cell Mutant That Expresses Altered Cyclic AMP-Dependent Protein Kinase
Wetters, T. V. D., & Coffino, P. (1982) · Molecular and Cellular Biology · doi:10.1128/mcb.2.10.1229 · Cited by 11 · see citing works
Flintoff, W. F., & Weber, M. (1980) · Somatic Cell and Molecular Genetics · doi:10.1007/bf01539153 · Cited by 9 · see citing works
The selection of wild-type revertants from methotrexate permeability mutants
Flintoff, W. F., & Saya, L. (1978) · Somatic Cell and Molecular Genetics · doi:10.1007/bf01538980 · Cited by 9 · see citing works
Citrulline metabolism in normal and citrullinemic human lymphocyte lines
Spector, E., Lockridge, O., & Bloom, A. D. (1975) · Biochemical Genetics · doi:10.1007/bf00485789 · Cited by 8 · see citing works
Biochemical and Molecular Studies of Human Methenyltetrahydrofolate Synthetase
Jolivet, J., Dayan, A., Beauchemin, M., Chahla, D., Mamo, A., & Bertrand, R. (1996) · The Oncologist · doi:10.1634/theoncologist.1-4-248 · Cited by 8 · see citing works
Loss of cytosolic serine hydroxymethyltransferase in a formate mutant ofNeurospora crassa
Cossins, E. A., & Pang, S. H. Y. (1980) · Cellular and Molecular Life Sciences · doi:10.1007/bf01952280 · Cited by 5 · see citing works
A mammalian cell line designed to test the mutagenic activity of anti‐herpes nucleosides
Pizer, L. I., Mitchell, D. H., Bentele, B., & Betz, J. L. (1987) · International Journal of Cancer · doi:10.1002/ijc.2910400121 · Cited by 4 · see citing works
Fenwick, R. G., Konecki, D. S., & Caskey, C. T. (1982) · Springer eBooks · doi:10.1007/978-1-4684-4256-4_2 · Cited by 3 · see citing works
Genetic Determination of Membrane Transport
Slayman, C. W. (1978) · Springer eBooks · doi:10.1007/978-3-642-46370-9_7 · Cited by 3 · see citing works
Perrone, S., Cifuente, J. O., Mastrella, L., Marina, A., Trastoy, B., Becker‐Kettern, J., Conrotte, J., Jiménez, A. A., Corzana, F., Glaab, E., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-74211-9 · Cited by 1 · see citing works
Mammalian Cell Mutagenesis: Relevance For Detection of Environmental Mutagens/Carcinogens
Kuroki, T. (1983) · Springer eBooks · doi:10.1007/978-1-4613-3566-5_12 · Cited by 1 · see citing works
Genetic Variants of Cultured Animal Cells
Ray, P. N., & Siminovitch, L. (1982) · Springer eBooks · doi:10.1007/978-1-4684-4256-4_9 · Cited by 1 · see citing works
Pike, S. (2008) · Texas ScholarWorks (Texas Digital Library)
Prasannan, P. (2006) · Texas ScholarWorks (Texas Digital Library)
Ferritin and Serine Hydroxymethyltransferase
Stover, P. J. (2006) · CRC Press eBooks · doi:10.1201/9780849332296.ch11
Ferritin and Serine Hydroxymethyltransferase
Stover, P. J. (2006) · CRC Press eBooks · doi:10.1201/9781420004847.ch11
- Authors
- Chasin, L. A., Feldman, A., Konstam, M., & Urlaub, G.
- Affiliations
- Columbia University (US)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 1974-03
- Volume
- 71
- Issue
- 3
- Pages
- 718-722
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC388084
- OpenAlex
- W2165776297
- Cited by
- 81
- References
- 22
- Citations by year
- 2026: 1 · 2023: 1 · 2021: 1 · 2020: 1 · 2018: 4 · 2016: 2
- FWCI
- 2.75
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Molecular Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Amino Acid Enzymes and Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Metabolism and Genetic Disorders
- Keywords
- serine hydroxymethyltransferase, revertant mutations, Chinese hamster cells, EMS mutagenesis, mitochondrial enzyme activity, cytosolic enzyme activity, enzyme thermostability, isozymes, enzyme half-life
- MeSH terms
- Acid Phosphatase, Animals, Cell Fractionation, Cell Line, Cell Nucleus, Electron Transport Complex IV, Cytosol, Female, Genes, Glycine, Cricetinae, Hot Temperature, Mitochondria, Mutation, Ovary, Phenotype, Serine, Tetrahydrofolates, Transferases
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