The DOI matches its Crossref record; 25 of the 25 references it cites were found in a registry or an index.
Targeted Disruption of the Mouse 3-Phosphoglycerate Dehydrogenase Gene Causes Severe Neurodevelopmental Defects and Results in Embryonic Lethality
Open accessAbstract
D-3-Phosphoglycerate dehydrogenase (Phgdh; EC 1.1.1.95) is the first committed enzyme of L-serine biosynthesis in the phosphorylated pathway. To determine the physiological importance of Phgdh-dependent L-serine biosynthesis in vivo, we generated Phgdh-deficient mice using targeted gene disruption in embryonic stem cells. The absence of Phgdh led to a drastic reduction of L-serine metabolites such as phosphatidyl-L-serine and sphingolipids. Phgdh null embryos have small bodies with abnormalities in selected tissues and died after days post-coitum 13.5. Striking abnormalities were evident in the central nervous system in which the Phgdh null mutation culminated in hypoplasia of the telencephalon, diencephalon, and mesencephalon; in particular, the olfactory bulbs, ganglionic eminence, and cerebellum appeared as indistinct structures. These observations demonstrate that the Phgdh-dependent phosphorylated pathway is essential for normal embryonic development, especially for brain morphogenesis.
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
“However, inhibitors of PHGDH might have a limited therapeutic index, as de novo serine synthesis has an important physiological role in the central nervous system (Furuya, 2008) and PHGDH-deficient mice exhibit severe brain morphogenesis defects (Yoshida et al., 2004).”
From Targeting Metabolism for Cancer Therapy (2017) · cites this paper as Yoshida et al., 2004
Citations
Cites
Efficient in vivo manipulation of mouse genomic sequences at the zygote stage.
Lakso, M., Pichel, J. G., Gorman, J. R., Sauer, B., Okamoto, Y., Lee, E., Alt, F. W., & Westphal, H. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.12.5860 · Cited by 1,125
Menezes, J., & Luskin, M. (1994) · Journal of Neuroscience · doi:10.1523/jneurosci.14-09-05399.1994 · Cited by 475
Shibata, T., Yamada, K., Watanabe, M., Ikenaka, K., Wada, K., Tanaka, K., & Inoue, Y. (1997) · Journal of Neuroscience · doi:10.1523/jneurosci.17-23-09212.1997 · Cited by 407
Self-citationThe bHLH Gene Hes1 as a Repressor of the Neuronal Commitment of CNS Stem Cells
Nakamura, Y., Sakakibara, S.-I., Miyata, T., Ogawa, M., Shimazaki, T., Weiss, S., Kageyama, R., & Okano, H. (2000) · The Journal of Neuroscience · doi:10.1523/jneurosci.20-01-00283.2000 · Cited by 316
l-Serine in disease and development
de Koning, T. J., Snell, K., Durán, M., Berger, R., Poll‐The, B. T., & Surtees, R. A. H. (2003) · Biochemical Journal · doi:10.1042/bj20021785 · Cited by 304
Enzymes of serine metabolism in normal, developing and neoplastic rat tissues
Snell, K. (1984) · Advances in Enzyme Regulation · doi:10.1016/0065-2571(84)90021-9 · Cited by 267
Yamasaki, M., Yamada, K., Furuya, S., Mitoma, J., Hirabayashi, Y., & Watanabe, M. (2001) · Journal of Neuroscience · doi:10.1523/jneurosci.21-19-07691.2001 · Cited by 215
Self-citationFuruya, S., Tabata, T., Mitoma, J., Yamada, K., Yamasaki, M., Makino, A., Yamamoto, T., Watanabe, M., Kano, M., & Hirabayashi, Y. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.200364497 · Cited by 197
Self-citationFURTHER STUDIES ON THE PATHWAY OF SERINE FORMATION FROM CARBOHYDRATE
Ichihara, A., & Greenberg, D. M. (1957) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)65032-x · Cited by 187
Holzenberger, M. (2000) · Nucleic Acids Research · doi:10.1093/nar/28.21.e92 · Cited by 129
Flagged first, then by citations
Research works printed but not linked: 1
- Bligh, 1959, Can. J. Med. Sci., 37, 911
Cited by
Sorted by citations
Items 101–166 of 166
Proteome alteration of U251 human astrocytoma cell after inhibiting retinoic acid synthesis
Zhang, M., Wan, C., Ji, B., Zhang, Z., Zhu, H., Tian, N., La, Y., Huang, K., Jiang, L., He, G., et al. (2008) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-008-9978-z · Cited by 9
“In mouse, homozygous knockout PHGDH gene increases hypoplasia of midbrain, interbrain, telencephalon, olfactory bulb, and cerebellum [30].”
BackgroundOn the quaternary structure of human D‐3‐phosphoglycerate dehydrogenase
Riva, D., Orlando, M., Rabattoni, V., & Pollegioni, L. (2024) · Protein Science · doi:10.1002/pro.5089 · Cited by 8
“L-Ser L-Ser metabolism plays an important role in the development and functioning of the central nervous system (Furuya et al., 2008; Yoshida et al., 2004).”
Yakupova, E. I., Zorov, D. B., & Plotnikov, E. Y. (2021) · Biochemistry (Moscow) · doi:10.1134/s0006297921120099 · Cited by 8
“(i) Deletion of the Phgdh gene in mice causes embryonic lethality owing to multiple developmental defects signifi cantly affecting the central nervous system [51].”
BackgroundL-Serine Decreases Taurine Concentration in the Extracellular Fluid of Brain Slices
Shigemi, K., Tanaka, K., Hayamizu, K., Denbow, D. M., & Furuse, M. (2011) · Neuroscience & Medicine · doi:10.4236/nm.2011.23034 · Cited by 8
“development, especially for brain morphogenesis [5].”
2 Serine, Glycine, and Threonine
de Koning, T. J., Fuchs, S. A., & Klomp, L. W. J. (2007) · Springer eBooks · doi:10.1007/978-0-387-30373-4_2 · Cited by 8
Collagen Biosynthesis in Pulmonary Fibrosis: Unraveling the Metabolic Web
Bernard, K. F. (2018) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2017-0350ed · Cited by 8
Marchesani, F., Michielon, A., Viale, E., Bianchera, A., Cavazzini, D., Pollegioni, L., Murtas, G., Mozzarelli, A., Bettati, S., Peracchi, A., et al. (2023) · Biomolecules · doi:10.3390/biom13081219 · Cited by 7
“To assess the effect of the different PSAT variants on L-Ser synthesis, we performed a continuous assay including the three enzymes—PHGDH, PSAT, and PSP—in the presence of the substrates 3-PG, NAD+ and L-Glu.”
BackgroundInfluentialTAKASAKI, C., Miura, E., & Watanabe, M. (2007) · Biomedical Research · doi:10.2220/biomedres.28.61 · Cited by 7
“Furthermore, targeted disruption of the Phgdh gene in mice results in embryonic lethality at embryonic day 13.5 accompanied by striking defects and retardation of brain development (Yoshida et al., 2004).”
BackgroundInfluentialSelf-citationL-serine metabolic regulation and host respiratory homeostasis
Li, P., Wu, X., Huang, Y., Qin, R., Xiong, P., & Qiu, Y. (2025) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2025.1518659 · Cited by 6
“Owing to the existence of the blood-brain barrier, L-serine absorbed from the diet cannot meet the needs of the brain and thus must be synthesized in situ (Yoshida et al., 2004).”
Metabolic control of cancer progression as novel targets for therapy
Talukdar, S., Emdad, L., Gogna, R., Das, S. K., & Fisher, P. B. (2021) · Advances in cancer research · doi:10.1016/bs.acr.2021.06.002 · Cited by 6
Strain‐specific modifier genes governing craniofacial phenotypes
Mukhopadhyay, P., Brock, G. N., Webb, C. L., Pisano, M., & Greene, R. M. (2012) · Birth Defects Research Part A Clinical and Molecular Teratology · doi:10.1002/bdra.22890 · Cited by 6
“Examples of some “modifier’ candidate genes – known to be involved in neural tube development (Yoshida et al., 2004; Noce et al., 1993; Loebel et al., 2004; Heil et al., 2001; Kuan et al., 1999; Kester et al., 2000) – differentially expressed in the developing NTs of B6 vs 129 mice are: Phgdh, NT…”
BackgroundInfluentialAli, A., Dhahouri, N. A., Almesmari, F. S. A., Fathalla, W. M., & Jasmi, F. A. (2021) · Genes · doi:10.3390/genes12050703 · Cited by 6
“The essential role of PHGDH in L-serine synthesis has been reported, and results indicated that targeted disruption of the PHGDH gene in a mouse model produced severe neurodevelopmental defects [37].”
BackgroundShi, M., Huai, Y., Deng, T., Zhang, C., Song, J., Wang, J., Zhang, Y., Chen, Z., Zhao, H., Wu, K., et al. (2025) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2025.102499 · Cited by 5
Control of epigenomic landscape and development of fetal male germ cells through L-serine metabolism
Hayashi, Y., Kaneko, J., Ito‐Matsuoka, Y., Takehara, A., Funakoshi, M., Maezawa, S., Shirane, K., Furuya, S., & Matsui, Y. (2024) · iScience · doi:10.1016/j.isci.2024.110702 · Cited by 6
Self-citationZhao, J., Tang, K. L., Jiang, G., Yang, X., Cui, M., Wan, C., Ouyang, Z., Zheng, Y., Liu, Z., Wang, M., et al. (2024) · Cell Proliferation · doi:10.1111/cpr.13755 · Cited by 5
“Given that global PHGDH knockout results in embryonic lethality, 77 Cre-loxP system should be used for conditional genetic ablation in germ cells.”
Meinhold, M., Verbrugge, S., Shi, A., Schönfelder, M., Becker, L., Jaspers, R. T., Zammit, P. S., & Wackerhage, H. (2024) · Cell and Tissue Research · doi:10.1007/s00441-023-03851-w · Cited by 5
“However, Phgdh-knockout mice are embryonal lethal (Yoshida et al .”
BackgroundYahyavi, I., Carrillo, F., Nuzzo, T., Vidali, M., Pietracupa, S., Modugno, N., Maio, A. D., Errico, F., Esposito, T., & Usiello, A. (2026) · npj Parkinson s Disease · doi:10.1038/s41531-026-01507-4 · Cited by 5
Xiang, D., Xia, Q., Chen, D., Feng, X., Zhao, Y., Liu, Y., Liao, H., Liu, Y., Li, N., & Yan, H. (2011) · Hepatology Research · doi:10.1111/j.1872-034x.2011.00839.x · Cited by 6
Lin, R., Zhao, C., Jing, L., & Zhao, S. (2015) · Cell Biology International · doi:10.1002/cbin.10458 · Cited by 5
“The expression patterns of target geneswere consistentwith reported (Yoshida et al., 2004; Bei et al., 2007; Blitek et al., 2011).”
BackgroundKustrimovic, N., Rabattoni, V., Riva, D., Motta, Z., Sacchi, S., & Pollegioni, L. (2025) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2025.101438 · Cited by 6
Oral Administration of L-serine Modifies Amino Acid Metabolism in the Brain of Rats
Shigemi, K., Tomonaga, S., Uotsu, N., Denbow, D. M., & Furuse, M. (2016) · Journal of Animal Research and Nutrition · doi:10.21767/2572-5459.100003 · Cited by 4
D-Serine Influences Synaptogenesis in a P19 Cell Model
Fuchs, S. A., Roeleveld, M. W., Klomp, L. W. J., Berger, R., & de Koning, T. J. (2012) · JIMD Reports · doi:10.1007/8904_2011_116 · Cited by 4
Öztürk, Ö., DUARTE, S. D. D. S., BALABAN, H. Y., ŞİMŞEK, H., & Şener, B. (2022) · TURKISH JOURNAL OF MEDICAL SCIENCES · doi:10.55730/1300-0144.5512 · Cited by 3
Syndrome de Neu-Laxova : rapport de trois cas et revue de la littérature
Darouich, S., Boujelbène, N., Kehila, M., Chanoufi, M. B., Reziga, H., Gaigi, S. S., & Masmoudi, A. (2016) · Annales de Pathologie · doi:10.1016/j.annpat.2016.04.004 · Cited by 3
Yamamoto, K., Mohri, S., & Furuya, S. (2020) · Archives of Insect Biochemistry and Physiology · doi:10.1002/arch.21751 · Cited by 3
Self-citationHamano, M., Ichinose, T., Yasuda, T., Ishijima, T., Okada, S., Abe, K., Tashiro, K., & Furuya, S. (2023) · Nutrients · doi:10.3390/nu15122731 · Cited by 3
“Phgdh, which is the first committed enzyme that is necessary for de novo L-serine synthesis in the brain and other tissues [31,32], mediates neuron/cell survival and growth [10,31,33] as well as neuronal transmission by supplying L-serine and D-serine to the central nervous system [32].”
BackgroundSelf-citationDietary and pharmacological induction of serine synthesis genesPreprint
Vázquez, A. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.06.15.151860 · Cited by 3
Myotube hypertrophy is associated with cancer-like metabolic reprogramming and limited by PHGDHPreprint
Stadhouders, L. E. M., Verbrugge, S. A. J., Smith, J. A. B., Gabriel, B. M., Hammersen, T. D., Kolijn, D., Vogel, I. S. P., Mohamed, A. D., de Wit, G. M. J., Offringa, C., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.12.01.403949 · Cited by 3
Post‐translational regulation of human D‐3‐phosphoglycerate dehydrogenase in Alzheimer's disease
Zerbini, E., Riva, D., Maffioli, E., Tedeschi, G., Sacchi, S., & Pollegioni, L. (2026) · Protein Science · doi:10.1002/pro.70505 · Cited by 2
“Therefore, as further confirmed by the early embryonic lethality observed in Phgdh (cid:4) / (cid:4) homozygous knock-out mice (Yoshida et al., 2004), this short cytosolic pathway is crucial to guarantee the correct brain functioning.”
Pagliano, P., Salzano, F., D’Amore, C., Spera, A. M., Conti, V., Folliero, V., Franci, G., & Ascione, T. (2025) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2025.2534056 · 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
“Mice with a PGDH gene deletion and human patients with a mutation in the PPSB gene show reduced serine levels in the brain and blood, respectively, indicating the involvement of PPSB in mammalian serine biosynthesis [17,18].”
BackgroundPannexin 1 regulates ventricular zone neuronal development
Wicki‐Stordeur, L. E. (2015) · UVic’s Research and Learning Repository (University of Victoria) · Cited by 2
Inferring metabolic rewiring in embryonic neural development using single cell dataPreprint
Jatav, S., Malhotra, S., Miller, F. D., Jha, A., & Goyal, S. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.09.03.282442 · Cited by 2
“For instance, deficiency of the two a-KG associated enzymes Psat1 and Phgdh, which are upregulated in RPs, have been reported in microcephaly, psychomotor retardation and epilepsy (Acuna-Hidalgo et al., 2014; Sharma & Prasad, 2017; Yoshida et al., 2003).”
BackgroundD-serine suppresses one-carbon metabolism by competing with mitochondrial L-serine transportPreprint
Suzuki, M., Adachi, K., Wiriyasermukul, P., Fukumura, M., Tamura, R., Hirano, Y., Aizawa, Y., Miyamoto, T., Taniguchi, S., Toda, M., et al. (2026) · bioRxiv · doi:10.1101/2024.09.03.610855 · Cited by 4
“Phgdh deficient mice die in embryo after 13.5 days post-coitum and show systemic growth defects, especially severe hypoplasia of the central nervous system, with marked reductions of L -serine and sphingolipids (Yoshida et al., 2004).”
InfluentialUsiello, A., Arisumi, K., Nuzzo, T., Gilio, L., Taniguchi, S., Russo, R., Motegi, H., di Vito, R., Hata, J., Errico, F., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.05.07.652561 · Cited by 2
Role of Astrocytic Serine in Learning and Memory and its Implications in Alzheimer's Disease.
Maugard, M. (2018) · theses.fr (ABES) · doi:10.70675/2a0528d8zc687z43e6za9b4zfa45cdb5b6d9 · Cited by 1
Hu, X., Gao, H., Zang, X., Li, M., Zhang, C., Yu, L., Tian, F., & Zhai, Q. (2025) · Food Bioscience · doi:10.1016/j.fbio.2025.107472 · Cited by 1
Comparative analysis of the effects of PSPH and PHGDH inhibitors on tumor cell proliferation
Wang, Y., & Sha, L. (2025) · Investigational New Drugs · doi:10.1007/s10637-025-01581-0 · Cited by 1
“For instance, PHGDH knockout mice exhibit severe central nervous system malformations and embryonic lethality [29], while treatment with NCT-503 has been reported to halt embryonic development, likely due to its ability to cross the blood–brain barrier [30].”
Zhao, Y.-H., Ning, J., Zhang, X., Qu, R., Lv, C.-C., & Zhang, Y.-Z. (2026) · Medicine · doi:10.1097/md.0000000000045715 · Cited by 1
Zhang, Z., Tan, J., Lv, M., Duan, Z., Wang, C., Gao, M., Cui, Y., & Feng, Y. (2026) · Frontiers in Pharmacology · doi:10.3389/fphar.2026.1735477 · Cited by 1
“Neurons cannot synthesize L-serine de novo ; PHGDH deficiency in mice leads to brain malformations (Furuya, 2008; Yoshida et al., 2004) owing to defective neurogenesis indicating that endogenously synthesized L-serine is essential for embryonic development (Kawakami et al., 2009).”
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
Lewis, N. A., Keil, M., Ranchordas, M. K., Burke, L. M., Stear, S. J., & Castell, L. M. (2012) · British Journal of Sports Medicine · doi:10.1136/bjsports-2012-091396 · Cited by 1
Yoshimura, R., Takai, M., NAMAKI, H., Minami, K., Imamura, W., Kato, H., Kamei, Y., & Kanamoto, R. (2015) · Journal of Nutritional Science and Vitaminology · doi:10.3177/jnsv.61.441 · Cited by 1
Jennemann, R., Gröne, H., Wiegandt, H., & Sandhoff, R. (2009) · Springer eBooks · doi:10.1007/978-0-387-30378-9_28 · Cited by 1
D-serine in health and disease
Fuchs, S. A. (2010) · Utrecht University Repository (Utrecht University) · Cited by 1
D-serine suppresses one-carbon metabolism by competing with mitochondrial L-serine transportPreprint
Suzuki, M., Adachi, K., Wiriyasermkul, P., Fukumura, M., Tamura, R., Hirano, Y., Aizawa, Y., Miyamoto, T., Taniguchi, S., Toda, M., et al. (2025) · eLife · doi:10.7554/elife.108562.1 · Cited by 1
EXAMINING THE ROLE OF METABOLISM IN MYC-DRIVEN TUMORIGENESIS
Forshell, L. P., & Zi, T. (2011)
Villarreal, B., & Nadilly, Y. (2021) · Figshare
Якупова, Э. И., Zorov, D. B., & Плотников, Е. Ю. (2021) · Biochemistry (Moscow) · doi:10.31857/s0320972521120101
Identification of a Novel Compound Heterozygous Mutation of PHGDH in Neu–Laxova SyndromePreprint
Li, H., Yu, W., Wei, J., Liu, C., & Lyu, Y. (2022) · Research Square · doi:10.21203/rs.3.rs-1685034/v1
Additional file 6 of PHGDH supports liver ceramide synthesis and sustains lipid homeostasis
Kang, Y. P., Falzone, A., Liu, M., González‐Sánchez, P., Choi, B.-H., Coloff, J. L., Saller, J. J., Karreth, F. A., & DeNicola, G. M. (2020) · Figshare · doi:10.6084/m9.figshare.12480131
Additional file 7 of PHGDH supports liver ceramide synthesis and sustains lipid homeostasis
Kang, Y. P., Falzone, A., Liu, M., González‐Sánchez, P., Choi, B.-H., Coloff, J. L., Saller, J. J., Karreth, F. A., & DeNicola, G. M. (2020) · Figshare · doi:10.6084/m9.figshare.12480134
Additional file 5 of PHGDH supports liver ceramide synthesis and sustains lipid homeostasis
Kang, Y. P., Falzone, A., Liu, M., González‐Sánchez, P., Choi, B.-H., Coloff, J. L., Saller, J. J., Karreth, F. A., & DeNicola, G. M. (2020) · Figshare · doi:10.6084/m9.figshare.12480128
Additional file 8 of PHGDH supports liver ceramide synthesis and sustains lipid homeostasis
Kang, Y. P., Falzone, A., Liu, M., González‐Sánchez, P., Choi, B.-H., Coloff, J. L., Saller, J. J., Karreth, F. A., & DeNicola, G. M. (2020) · Figshare · doi:10.6084/m9.figshare.12480137
D-serine suppresses one-carbon metabolism by competing with mitochondrial L-serine transportPreprint
Suzuki, M., Adachi, K., Wiriyasermukul, P., Fukumura, M., Tamura, R., Hirano, Y., Aizawa, Y., Miyamoto, T., Taniguchi, S., Toda, M., et al. (2025) · eLife · doi:10.7554/elife.108562
Additional file 4 of PHGDH supports liver ceramide synthesis and sustains lipid homeostasis
Kang, Y. P., Falzone, A., Liu, M., González‐Sánchez, P., Choi, B.-H., Coloff, J. L., Saller, J. J., Karreth, F. A., & DeNicola, G. M. (2020) · Figshare · doi:10.6084/m9.figshare.12480125
Additional file 1 of PHGDH supports liver ceramide synthesis and sustains lipid homeostasis
Kang, Y. P., Falzone, A., Liu, M., González‐Sánchez, P., Choi, B.-H., Coloff, J. L., Saller, J. J., Karreth, F. A., & DeNicola, G. M. (2020) · Figshare · doi:10.6084/m9.figshare.12480116
Additional file 2 of PHGDH supports liver ceramide synthesis and sustains lipid homeostasis
Kang, Y. P., Falzone, A., Liu, M., González‐Sánchez, P., Choi, B.-H., Coloff, J. L., Saller, J. J., Karreth, F. A., & DeNicola, G. M. (2020) · Figshare · doi:10.6084/m9.figshare.12480119
Additional file 3 of PHGDH supports liver ceramide synthesis and sustains lipid homeostasis
Kang, Y. P., Falzone, A., Liu, M., González‐Sánchez, P., Choi, B.-H., Coloff, J. L., Saller, J. J., Karreth, F. A., & DeNicola, G. M. (2020) · Figshare · doi:10.6084/m9.figshare.12480122
Translatome-based classification of pancreatic cancer
Shin, S. (2020) · theses.fr (ABES) · doi:10.70675/09efa5edz6f6ez4463z90eaz76d4c6c23a9d
Alsolami, S. M., Zhang, Y., Singh, U., Jin, Y., Steiner, N., Szczepski, K., Klein, S. G., Yuan, B., Bi, C., Wang, M., et al. (2026) · Communications Biology · doi:10.1038/s42003-026-10013-5
“Gene Ontology (GO) analysis on the differentially expressed genes (DEGs) in the RNA-seq data revealed that DEGs upregulated at pH 6.8 were enriched in pathways related to stress and immune responses, such as CR2 29,30 , TCF7 31 – 33 ,and IL32 34 ;whereasDEGsupregulatedatpH7.”
Influentialᴅ-serine suppresses one-carbon metabolism by competing with mitochondrial ʟ-serine transportPreprint
Suzuki, M., Adachi, K., Wiriyasermukul, P., Fukumura, M., Tamura, R., Hirano, Y., Aizawa, Y., Miyamoto, T., Taniguchi, S., Toda, M., et al. (2026) · eLife · doi:10.7554/elife.108562.2
Zaino, J., Anderson, A., Alaoui, O. R., & Ponomarova, O. (2026) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2026.113667
Marchant, M. (2026) · Zenodo (CERN European Organization for Nuclear Research) · doi:10.5281/zenodo.19389875
D-serine suppresses one-carbon metabolism by competing with mitochondrial L-serine transportPreprint
Suzuki, M., Adachi, K., Wiriyasermukul, P., Fukumura, M., Tamura, R., Hirano, Y., Aizawa, Y., Miyamoto, T., Taniguchi, S., Toda, M., et al. (2026) · eLife · doi:10.7554/elife.108562.3
Metadata
- Authors
- Yoshida, K., Furuya, S., Osuka, S., Mitoma, J., Shinoda, Y., Watanabe, M., Azuma, N., Tanaka, H., Hashikawa, T., Itohara, S., & Hirabayashi, Y.
- Affiliations
- RIKEN (JP)
- Sanford Burnham Prebys Medical Discovery Institute (US)
- Hokkaido University (JP)
- Utsunomiya University (JP)
- Corresponding author
- Furuya, Shigeki
- Hirabayashi, Yoshio
- ORCID
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2004-01
- Volume
- 279
- Issue
- 5
- Pages
- 3573-3577
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2097895708
- Cited by
- 161
- References
- 25
- Citations by year
- 2026: 9 · 2025: 11 · 2024: 10 · 2023: 9 · 2022: 7 · 2021: 13 · 2020: 15 · 2019: 4 · 2018: 11 · 2017: 4 · 2016: 8 · 2015: 6 · 2014: 4 · 2013: 3 · 2012: 8
- FWCI
- 2.18
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Amino Acid Enzymes and Metabolism
- Life Sciences › Neuroscience › Developmental Neuroscience › Neurogenesis and neuroplasticity mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Metabolism and Genetic Disorders
- Keywords
- 3-phosphoglycerate dehydrogenase, PHGDH, L-serine biosynthesis, embryonic lethality, neurodevelopmental defects, brain morphogenesis, sphingolipids, olfactory bulb hypoplasia, ganglionic eminence, cerebellum, telencephalon, diencephalon, midbrain
- MeSH terms
- Alleles, Animals, Brain, Carbohydrate Dehydrogenases, Cytosol, Exons, Heterozygote, Immunohistochemistry, Introns, Liver, Mice, Inbred C57BL, Mice, Transgenic, Microscopy, Fluorescence, Mutation, Nervous System, Phenotype, Phosphorylation, Serine, Stem Cells, Time Factors, Blotting, Southern, Blotting, Western, Polymerase Chain Reaction, Phosphoglycerate Dehydrogenase, Mice
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