The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
The UniProt entry D3ZDM7 is annotated as D-aspartate oxidase (DDO; also called DASPO), encoded by Ddo in Rattus norvegicus. The literature retrieved here uses the same biochemical identity: a mammalian FAD-dependent oxidase specific for acidic D-amino acids, especially D-aspartate (D-Asp), and often called DDO/DASPO with EC 1.4.3.1. Rat DDO was cloned/purified and compared to human/mouse enzymes, strongly supporting that rat Ddo corresponds to the UniProt target rather than an unrelated “Ddo” symbol in another context (Katane et al., 2015; publication date Feb 2015; https://doi.org/10.1248/bpb.b14-00690) (katane2015characterizationofthe pages 1-2, katane2015characterizationofthe pages 2-3).
Ddo/DDO (D-aspartate oxidase; EC 1.4.3.1) is an FAD-containing flavoprotein that catalyzes oxidative deamination of acidic D-amino acids to yield the corresponding 2-oxo acid, hydrogen peroxide (H2O2), and ammonia (NH3) (Katane et al., 2015; https://doi.org/10.1248/bpb.b14-00690) (katane2015characterizationofthe pages 1-2). In the case of D-Asp, the 2-oxo acid product is oxaloacetate (Santillo et al., 2023; publication date Mar 2023; https://doi.org/10.3390/biom13040621) (santillo2023daspartatedepletionperturbs pages 1-2). This reaction provides the core functional annotation for rat Ddo: it is a catabolic enzyme that directly controls tissue D-Asp abundance.
DDO is highly selective for acidic D-amino acids, classically D-Asp and D-glutamate (D-Glu) (Katane et al., 2015; https://doi.org/10.1248/bpb.b14-00690) (katane2015characterizationofthe pages 1-2). Detailed assays of recombinant mammalian DDO show D-Asp is the reference substrate and that the NMDA analog N-methyl-D-aspartate (NMDA) can be an efficient substrate; other D-amino acids are weak substrates (Katane et al., 2015; https://doi.org/10.1248/bpb.b14-00690) (katane2015characterizationofthe pages 4-5). Quantitative substrate activity fractions reported for human DDO include D-Asn 3.4%, D-Pro 0.14%, and D-His 0.17% relative to D-Asp under the assay conditions (Katane et al., 2015; https://doi.org/10.1248/bpb.b14-00690) (katane2015characterizationofthe pages 3-4).
This substrate constraint is important for functional annotation: Ddo is not a broad-spectrum D-amino acid oxidase (DAO-like), but rather a specialized enzyme controlling the pool of acidic D-amino acids.
DDO is an FAD-dependent flavoenzyme, and experimental recombinant preparations and assays include FAD, consistent with tight cofactor dependence (Katane et al., 2015; https://doi.org/10.1248/bpb.b14-00690) (katane2015characterizationofthe pages 2-3, katane2015characterizationofthe pages 3-4). A comparative kinetic compilation reports species differences in catalytic efficiency, including explicit values for rat DASPO/DDO (Pollegioni et al., 2021; publication date Jun 2021; https://doi.org/10.3389/fmolb.2021.689719) (pollegioni2021humandaspartateoxidase pages 4-5). These enzyme-level properties align with UniProt’s assignment to a D-amino acid oxidase-like flavoprotein family.
Multiple sources describe DDO as a peroxisomal enzyme. A mammalian metabolomics/genotype study describes DDO as a peroxisomal flavoprotein catalyzing stereospecific oxidative deamination of acidic D-amino acids (Han et al., 2015; publication date Dec 2015; https://doi.org/10.1016/j.jpba.2015.05.013) (han2015changesindaspartic pages 1-2). Rat-specific peroxisomal localization is supported by the repeated citation of a study describing D-aspartate oxidase as peroxisomal in rat liver (Van Veldhoven et al., 1991, as cited in later works) (sarower2004distributionandsubstrate pages 5-6, molla2020structureandkinetic pages 21-24). A dedicated review likewise describes DASPO/DDO as a peroxisomal FAD-containing enzyme (Pollegioni et al., 2021; https://doi.org/10.3389/fmolb.2021.689719) (pollegioni2021humandaspartateoxidase pages 1-2).
Functional implication: peroxisomal localization positions DDO as a source of peroxisomal H2O2, linking Ddo activity not only to D-Asp turnover but also potentially to redox signaling/oxidative stress microdomains, depending on tissue context.
A cross-species kinetic table reports the following parameters for oxidation of D-Asp:
- Human DASPO/DDO: Km 1.05 mM, kcat 81.3 s−1, kcat/Km 77.4 s−1·mM−1, specific activity 124 U/mg.
- Rat DASPO/DDO: Km 2.3 mM, kcat 31.1 s−1, kcat/Km 14.1 s−1·mM−1, specific activity 71.7 U/mg.
- Mouse DASPO/DDO (example entry): Km 7.4 mM, kcat 9.8 s−1, kcat/Km 1.35 s−1·mM−1.
These values indicate rat Ddo enzyme efficiency is intermediate between human and mouse, and substantiate the frequent assertion that rat DDO is a closer functional model for human DDO than mouse in some assay contexts (Pollegioni et al., 2021; https://doi.org/10.3389/fmolb.2021.689719) (pollegioni2021humandaspartateoxidase pages 4-5).
A compact table of the main quantitative values extracted in this review is provided below.
| Finding/metric | Species/tissue | Quantitative value | Interpretation | Source (author year, DOI URL) |
|---|---|---|---|---|
| Catalytic reaction/products | Mammalian DDO/DASPO; relevant to rat Ddo | Oxidative deamination of D-Asp → oxaloacetate + NH3 + H2O2; DDO also acts on acidic D-amino acids including D-Glu | Defines the primary enzymatic function of rat Ddo orthologs in mammals: a stereospecific FAD-dependent oxidase controlling D-Asp abundance | Katane et al. 2015, https://doi.org/10.1248/bpb.b14-00690; Molla et al. 2020, no URL in extracted context (katane2015characterizationofthe pages 1-2, molla2020structureandkinetic pages 1-5) |
| Subcellular localization evidence | Rat and human liver; mammalian cells | Peroxisomal localization reported; human/rat DDO described as peroxisomal enzyme | Supports that rat Ddo protein functions in peroxisomes rather than cytosol/mitochondria | Van Veldhoven et al. 1991 as cited in later reviews; Pollegioni et al. 2021, https://doi.org/10.3389/fmolb.2021.689719 (sarower2004distributionandsubstrate pages 5-6, pollegioni2021humandaspartateoxidase pages 1-2, molla2020structureandkinetic pages 21-24) |
| Substrate specificity: D-Asp | Human recombinant DDO | Reference activity = 100%; specific activity 87.5 ± 12.3 µmol/min/mg | Preferred physiological substrate | Katane et al. 2015, https://doi.org/10.1248/bpb.b14-00690 (katane2015characterizationofthe pages 4-5) |
| Substrate specificity: NMDA | Human recombinant DDO | Similar to D-Asp; specific activity 91.2 ± 14.8 µmol/min/mg | NMDA is an efficient substrate, explaining DDO relevance to NMDA-related signaling chemistry | Katane et al. 2015, https://doi.org/10.1248/bpb.b14-00690 (katane2015characterizationofthe pages 4-5, katane2015characterizationofthe pages 3-4) |
| Substrate specificity: D-Glu | Human recombinant DDO | 7.82 ± 1.39 µmol/min/mg; ~12.8% of D-Asp activity in another study | Confirms preference for acidic D-amino acids beyond D-Asp, but much lower than D-Asp/NMDA | Katane et al. 2015, https://doi.org/10.1248/bpb.b14-00690; Molla et al. 2020, no URL in extracted context (katane2015characterizationofthe pages 4-5, molla2020structureandkinetic pages 8-11) |
| Substrate specificity: D-Asn | Human recombinant DDO | 2.93 ± 0.47 µmol/min/mg; 3.4% of D-Asp activity in Katane 2015; 9.5% in Molla 2020 assay conditions | Weak substrate; activity depends somewhat on assay format but remains far below D-Asp | Katane et al. 2015, https://doi.org/10.1248/bpb.b14-00690; Molla et al. 2020, no URL in extracted context (katane2015characterizationofthe pages 4-5, katane2015characterizationofthe pages 3-4, molla2020structureandkinetic pages 8-11) |
| Substrate specificity: D-Pro | Human recombinant DDO | 0.12 ± 0.04 µmol/min/mg; 0.14–~1% of D-Asp activity | Very poor substrate | Katane et al. 2015, https://doi.org/10.1248/bpb.b14-00690; Molla et al. 2020, no URL in extracted context (katane2015characterizationofthe pages 4-5, katane2015characterizationofthe pages 3-4, molla2020structureandkinetic pages 8-11) |
| Substrate specificity: D-His | Human recombinant DDO | 0.14 ± 0.06 µmol/min/mg; 0.17–~1% of D-Asp activity | Very poor substrate | Katane et al. 2015, https://doi.org/10.1248/bpb.b14-00690; Molla et al. 2020, no URL in extracted context (katane2015characterizationofthe pages 4-5, katane2015characterizationofthe pages 3-4, molla2020structureandkinetic pages 8-11) |
| Kinetic parameters on D-Asp: human DASPO | Human enzyme | Km = 1.05 mM; kcat = 81.3 s^-1; kcat/Km = 77.4 s^-1·mM^-1; specific activity = 124 U/mg | Highest catalytic efficiency among compared mammalian enzymes in this summary; benchmark for mammalian DASPO | Pollegioni et al. 2021, https://doi.org/10.3389/fmolb.2021.689719 (pollegioni2021humandaspartateoxidase pages 4-5) |
| Kinetic parameters on D-Asp: rat DASPO | Rat enzyme | Km = 2.3 mM; kcat = 31.1 s^-1; kcat/Km = 14.1 s^-1·mM^-1; specific activity = 71.7 U/mg | Rat Ddo product is less efficient than human but substantially more active than mouse; rat is biochemically closer to human than mouse | Pollegioni et al. 2021, https://doi.org/10.3389/fmolb.2021.689719 (pollegioni2021humandaspartateoxidase pages 4-5) |
| Kinetic parameters on D-Asp: mouse DASPO | Mouse enzyme | Km = 7.4 mM; kcat = 9.8 s^-1; kcat/Km = 1.35 s^-1·mM^-1 | Much weaker affinity and catalytic efficiency than rat/human, underscoring species differences in D-Asp turnover | Pollegioni et al. 2021, https://doi.org/10.3389/fmolb.2021.689719 (pollegioni2021humandaspartateoxidase pages 4-5) |
| FAD binding affinity | Human vs mouse DASPO | hDASPO Kd ≈ 33 nM; mouse enzyme shows ~100-fold higher Kd for FAD | Human enzyme binds FAD much more tightly, helping explain higher activity; species differences matter when inferring rat function | Pollegioni et al. 2021, https://doi.org/10.3389/fmolb.2021.689719 (pollegioni2021humandaspartateoxidase pages 4-5) |
| Schizophrenia post-mortem DDO activity: DLPFC | Human dorsolateral prefrontal cortex | Ctrl 35.8 ± 4.3 vs SCZ 52.5 ± 4.4 μU/mg protein; p < 0.01 | ~25–47% higher DDO activity in SCZ DLPFC, linked to lower D-Asp | Nuzzo et al. 2017, https://doi.org/10.1038/s41537-017-0015-7 (nuzzo2017decreasedfreedaspartate pages 4-6, nuzzo2017decreasedfreedaspartate pages 1-2) |
| Schizophrenia post-mortem DDO activity: hippocampus | Human hippocampus | Ctrl 27.7 ± 3.6 vs SCZ 30.0 ± 3.7 μU/mg; p > 0.05 | No significant disease-associated change in hippocampus; effect is region-selective | Nuzzo et al. 2017, https://doi.org/10.1038/s41537-017-0015-7 (nuzzo2017decreasedfreedaspartate pages 4-6) |
| DDO mRNA in schizophrenia cohort | Human DLPFC and hippocampus | DLPFC: Ctrl 0.39 ± 0.05 vs SCZ 0.47 ± 0.14; hippocampus: Ctrl 0.87 ± 0.23 vs SCZ 1.00 ± 0.18; p > 0.05 | Increased DDO activity in SCZ DLPFC was not mirrored by significant mRNA elevation in that cohort | Nuzzo et al. 2017, https://doi.org/10.1038/s41537-017-0015-7 (nuzzo2017decreasedfreedaspartate pages 4-6) |
| DDO promoter methylation | Human DLPFC and hippocampus | DLPFC 24.5 ± 1.4% vs hippocampus 18.8 ± 1.2% in controls; hippocampus SCZ 22.6 ± 1.3% vs control 18.8 ± 1.2%, p < 0.05 | Brain-region methylation differs; SCZ-associated methylation change was seen in hippocampus, not clearly explaining elevated DLPFC DDO activity | Nuzzo et al. 2017, https://doi.org/10.1038/s41537-017-0015-7 (nuzzo2017decreasedfreedaspartate pages 4-6) |
| D-Asp level change in Ddo−/− mice | Mouse brain regions | ~10- to 20-fold increase in D-Asp | Genetic loss of DDO massively elevates D-Asp, establishing DDO as the dominant catabolic control point in vivo | Errico et al. 2018, https://doi.org/10.3389/fpsyt.2018.00559 (errico2018theemergingrole pages 5-6) |
Table: This table compiles key quantitative findings on D-aspartate oxidase relevant to rat Ddo and mammalian biology, including enzymatic function, localization, substrate specificity, kinetics, and disease-associated measurements. It is useful as a compact reference for functional annotation and cross-species interpretation.
A central concept in Ddo biology is that D-Asp is a bioactive neuromodulatory molecule, and DDO expression/activity is a principal mechanism that restricts its levels. D-Asp can stimulate NMDA receptors by binding the L-glutamate site, and DDO therefore indirectly modulates glutamatergic neurotransmission through D-Asp availability (Katane & Homma, 2024; publication date Mar 2024; https://doi.org/10.1248/bpb.b23-00485) (katane2024biosynthesisanddegradation pages 3-4).
Genetic evidence supports DDO as a dominant control point: Ddo knockout is associated with ~10–20× higher brain D-Asp in multiple regions, demonstrating that DDO-mediated catabolism strongly limits steady-state D-Asp (Errico et al., 2018; publication date Nov 2018; https://doi.org/10.3389/fpsyt.2018.00559) (errico2018theemergingrole pages 5-6). Physiologically, DDO loss (and D-Asp elevation) is associated with changes in synaptic plasticity such as enhanced NMDA receptor–dependent neurotransmission and altered LTP/LTD-related phenomena (Katane & Homma, 2024; https://doi.org/10.1248/bpb.b23-00485) (katane2024biosynthesisanddegradation pages 3-4).
Interpretation for rat functional annotation: in rat neurons, peroxisomal DDO is expected to regulate developmental and regional D-Asp availability, thereby influencing NMDA receptor tone and downstream plasticity programs.
Recent rodent work strengthens the view that Ddo also shapes endocrine biology by controlling D-Asp in reproductive tissues.
A 2023 study used a Ddo knock-in mouse constitutively overexpressing DDO to deplete endogenous D-Asp and found that D-Asp depletion was associated with a decrease in serum testosterone and changes consistent with impaired spermatogenesis (reduced PCNA and SYCP3; increased apoptosis markers including cytosolic cytochrome c and TUNEL-positive cells) (Santillo et al., 2023; publication date Mar 2023; https://doi.org/10.3390/biom13040621) (santillo2023daspartatedepletionperturbs pages 1-2). A 2024 review synthesizes evidence that D-Asp supports Leydig cell steroidogenesis and broader spermatogenic processes, and highlights that Ddo knock-in mice (elevated DDO) show reduced testicular D-Asp with reduced testosterone, reinforcing the causal chain: DDO↑ → D-Asp↓ → steroidogenesis/spermatogenesis disruption (Falvo et al., 2024; publication date Aug 2024; https://doi.org/10.3390/cells13161400) (falvo2024newinsightsinto pages 1-2, falvo2024newinsightsinto pages 6-7).
Interpretation for rat functional annotation: because rat Ddo is enzymatically active and peroxisomal (sarower2004distributionandsubstrate pages 5-6, molla2020structureandkinetic pages 21-24), and D-Asp signaling in pituitary/testis is reported as physiologically relevant in rodents, rat Ddo likely contributes to endocrine regulation by limiting D-Asp in these tissues.
A 2023 PNAS study places DDO into a broader physiological role: mammals maintain systemic predominance of L-amino acids in the presence of microbial production of D-amino acids, in part through stereoselective catabolism by DAO and DDO; mammalian DDO is described as degrading only D-aspartate in that framework (Gonda et al., 2023; publication date Apr 2023; https://doi.org/10.1073/pnas.2300817120) (pqac-000000?? not assigned in evidence list; within retrieved papers but not extracted as evidence snippet beyond abstract; therefore not cited as context ID). Because the evidence snippets available here do not include a citable context ID for this point, it should be treated as background unless the full text is added to evidence; the conceptual connection remains plausible but is not directly cited from the current evidence set.
A 2024 review summarizes emerging physiological roles of D-amino acids (including D-Asp) in peripheral and endocrine glands and discusses their biosynthesis/degradation frameworks in mammals, including the key catabolic role of DDO (Katane & Homma, 2024; publication date Mar 2024; https://doi.org/10.1248/bpb.b23-00485) (katane2024biosynthesisanddegradation pages 3-4).
DDO is framed as a druggable target because inhibiting DDO should increase brain D-Asp levels and thereby enhance NMDA receptor function. A medicinal-chemistry study identified DDO inhibitors through large-scale in silico screening (~4 million compounds) followed by biochemical testing, and describes DDO as peroxisomal and FAD-dependent (Katane et al., 2015; publication date Sep 2015; https://doi.org/10.1021/acs.jmedchem.5b00871) (katane2015identificationofnovel pages 3-3, katane2015identificationofnovel pages 8-10). The reported Ki for 5-aminonicotinic acid is ~3.8 µM (Molla et al., 2020; Katane et al., 2015 J Med Chem) (molla2020structureandkinetic pages 1-5, katane2015identificationofnovel pages 1-3).
Recombinant DDO is used as a specific biochemical reagent in analytical workflows. For example, in the Ddo overexpression mouse study, recombinant human DDO was used to selectively degrade the D-Asp HPLC peak to confirm analyte identity in tissue extracts (Santillo et al., 2023; https://doi.org/10.3390/biom13040621) (santillo2023daspartatedepletionperturbs pages 2-4).
Human post-mortem work reports a region-specific relationship between reduced D-Asp and elevated DDO enzymatic activity in schizophrenia dorsolateral prefrontal cortex, suggesting that DDO activity could contribute to a disease-associated neurochemical signature (Nuzzo et al., 2017; publication date Apr 2017; https://doi.org/10.1038/s41537-017-0015-7) (nuzzo2017decreasedfreedaspartate pages 4-6, nuzzo2017decreasedfreedaspartate pages 1-2). Visual evidence from the same paper (Figure panels) is available in the extracted images (nuzzo2017decreasedfreedaspartate media 5587f97f, nuzzo2017decreasedfreedaspartate media 98507419, nuzzo2017decreasedfreedaspartate media d0cedfda).
Authoritative reviews converge on a model in which DDO is the dominant degradative gatekeeper of D-Asp levels, influencing NMDA receptor–dependent neurotransmission and hormone-related functions. For example, Pollegioni et al. emphasize DDO as a peroxisomal FAD enzyme whose structure/function knowledge is enabling targeted strategies such as DDO inhibitors aimed at increasing D-Asp (Pollegioni et al., 2021; https://doi.org/10.3389/fmolb.2021.689719) (pollegioni2021humandaspartateoxidase pages 1-2, pollegioni2021humandaspartateoxidase pages 4-5). Katane & Homma summarize peripheral/endocrine roles and integrate genetic models showing DDO KO phenotypes consistent with altered NMDA-dependent synaptic processes and depression-relevant behavioral readouts (Katane & Homma, 2024; https://doi.org/10.1248/bpb.b23-00485) (katane2024biosynthesisanddegradation pages 3-4).
Key quantitative points relevant to functional annotation include:
- Rat enzyme kinetics: Km 2.3 mM, kcat 31.1 s−1 on D-Asp (Pollegioni et al., 2021; https://doi.org/10.3389/fmolb.2021.689719) (pollegioni2021humandaspartateoxidase pages 4-5).
- In vivo control strength: Ddo−/− mice show ~10–20× higher brain D-Asp (Errico et al., 2018; https://doi.org/10.3389/fpsyt.2018.00559) (errico2018theemergingrole pages 5-6).
- Human disease-linked biochemistry: schizophrenia DLPFC DDO activity 35.8 ± 4.3 → 52.5 ± 4.4 μU/mg (Ctrl→SCZ), while hippocampus shows no significant change (Nuzzo et al., 2017; https://doi.org/10.1038/s41537-017-0015-7) (nuzzo2017decreasedfreedaspartate pages 4-6). These findings are also supported by extracted figure panels (nuzzo2017decreasedfreedaspartate media 5587f97f, nuzzo2017decreasedfreedaspartate media 98507419, nuzzo2017decreasedfreedaspartate media d0cedfda).
Molecular function: peroxisomal FAD-dependent oxidase catalyzing oxidative deamination of D-aspartate (major) and other acidic D-amino acids (minor) to produce the corresponding 2-oxo acid (for D-Asp, oxaloacetate), H2O2, and NH3 (katane2015characterizationofthe pages 1-2, molla2020structureandkinetic pages 1-5, santillo2023daspartatedepletionperturbs pages 1-2).
Cellular component: peroxisome (peroxisomal enzyme in rat liver cited; broader mammalian consensus) (sarower2004distributionandsubstrate pages 5-6, pollegioni2021humandaspartateoxidase pages 1-2, han2015changesindaspartic pages 1-2).
Biological processes / pathways (mechanistic): regulation of D-Asp homeostasis impacting (i) NMDA receptor signaling and synaptic plasticity, and (ii) endocrine functions including testosterone biosynthesis and spermatogenesis via D-Asp availability (katane2024biosynthesisanddegradation pages 3-4, santillo2023daspartatedepletionperturbs pages 1-2, falvo2024newinsightsinto pages 1-2).
While rat DDO has direct biochemical characterization and rat liver peroxisomal localization is supported through citations (sarower2004distributionandsubstrate pages 5-6, molla2020structureandkinetic pages 21-24), the current retrieved evidence set does not include a modern rat-focused immunolocalization/expression atlas paper with direct experimental images for rat tissues. The mechanistic conclusions are therefore best supported for mammals/rodents broadly and for rat enzymology specifically, with some tissue-level functional inferences relying on mouse models.
References
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(nuzzo2017decreasedfreedaspartate pages 4-6): Tommaso Nuzzo, Silvia Sacchi, Francesco Errico, Simona Keller, Orazio Palumbo, Ermanno Florio, Daniela Punzo, Francesco Napolitano, Massimiliano Copetti, Massimo Carella, Lorenzo Chiariotti, Alessandro Bertolino, Loredano Pollegioni, and Alessandro Usiello. Decreased free d-aspartate levels are linked to enhanced d-aspartate oxidase activity in the dorsolateral prefrontal cortex of schizophrenia patients. NPJ Schizophrenia, Apr 2017. URL: https://doi.org/10.1038/s41537-017-0015-7, doi:10.1038/s41537-017-0015-7. This article has 77 citations.
(nuzzo2017decreasedfreedaspartate pages 1-2): Tommaso Nuzzo, Silvia Sacchi, Francesco Errico, Simona Keller, Orazio Palumbo, Ermanno Florio, Daniela Punzo, Francesco Napolitano, Massimiliano Copetti, Massimo Carella, Lorenzo Chiariotti, Alessandro Bertolino, Loredano Pollegioni, and Alessandro Usiello. Decreased free d-aspartate levels are linked to enhanced d-aspartate oxidase activity in the dorsolateral prefrontal cortex of schizophrenia patients. NPJ Schizophrenia, Apr 2017. URL: https://doi.org/10.1038/s41537-017-0015-7, doi:10.1038/s41537-017-0015-7. This article has 77 citations.
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(li2023improvementoflearning pages 1-2): Yu-Jiao Li, Kun Zhang, Ting Sun, Yan-Yan Guo, Qi Yang, Shui-Bing Liu, Yu-Mei Wu, and Ming-Gao Zhao. Improvement of learning and memory by elevating brain d-aspartate in a mouse model of fragile x syndrome. Molecular Neurobiology, 60:6410-6423, Jul 2023. URL: https://doi.org/10.1007/s12035-023-03438-0, doi:10.1007/s12035-023-03438-0. This article has 12 citations and is from a peer-reviewed journal.
(katane2015identificationofnovel pages 3-3): Masumi Katane, Shota Yamada, Go Kawaguchi, Mana Chinen, Maya Matsumura, Takemi Ando, Issei Doi, Kazuki Nakayama, Yuusuke Kaneko, Satsuki Matsuda, Yasuaki Saitoh, Tetsuya Miyamoto, Masae Sekine, Noriyuki Yamaotsu, Shuichi Hirono, and Hiroshi Homma. Identification of novel d-aspartate oxidase inhibitors by in silico screening and their functional and structural characterization in vitro. Journal of medicinal chemistry, 58 18:7328-40, Sep 2015. URL: https://doi.org/10.1021/acs.jmedchem.5b00871, doi:10.1021/acs.jmedchem.5b00871. This article has 28 citations and is from a highest quality peer-reviewed journal.
(katane2015identificationofnovel pages 8-10): Masumi Katane, Shota Yamada, Go Kawaguchi, Mana Chinen, Maya Matsumura, Takemi Ando, Issei Doi, Kazuki Nakayama, Yuusuke Kaneko, Satsuki Matsuda, Yasuaki Saitoh, Tetsuya Miyamoto, Masae Sekine, Noriyuki Yamaotsu, Shuichi Hirono, and Hiroshi Homma. Identification of novel d-aspartate oxidase inhibitors by in silico screening and their functional and structural characterization in vitro. Journal of medicinal chemistry, 58 18:7328-40, Sep 2015. URL: https://doi.org/10.1021/acs.jmedchem.5b00871, doi:10.1021/acs.jmedchem.5b00871. This article has 28 citations and is from a highest quality peer-reviewed journal.
(katane2015identificationofnovel pages 1-3): Masumi Katane, Shota Yamada, Go Kawaguchi, Mana Chinen, Maya Matsumura, Takemi Ando, Issei Doi, Kazuki Nakayama, Yuusuke Kaneko, Satsuki Matsuda, Yasuaki Saitoh, Tetsuya Miyamoto, Masae Sekine, Noriyuki Yamaotsu, Shuichi Hirono, and Hiroshi Homma. Identification of novel d-aspartate oxidase inhibitors by in silico screening and their functional and structural characterization in vitro. Journal of medicinal chemistry, 58 18:7328-40, Sep 2015. URL: https://doi.org/10.1021/acs.jmedchem.5b00871, doi:10.1021/acs.jmedchem.5b00871. This article has 28 citations and is from a highest quality peer-reviewed journal.
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(nuzzo2017decreasedfreedaspartate media 5587f97f): Tommaso Nuzzo, Silvia Sacchi, Francesco Errico, Simona Keller, Orazio Palumbo, Ermanno Florio, Daniela Punzo, Francesco Napolitano, Massimiliano Copetti, Massimo Carella, Lorenzo Chiariotti, Alessandro Bertolino, Loredano Pollegioni, and Alessandro Usiello. Decreased free d-aspartate levels are linked to enhanced d-aspartate oxidase activity in the dorsolateral prefrontal cortex of schizophrenia patients. NPJ Schizophrenia, Apr 2017. URL: https://doi.org/10.1038/s41537-017-0015-7, doi:10.1038/s41537-017-0015-7. This article has 77 citations.
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