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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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 target protein is zebrafish ldhd (UniProt F1QXM5), annotated as mitochondrial D-lactate dehydrogenase (LDHD). This identity is supported by direct zebrafish loss-of-function data showing stereospecific accumulation of D-lactate (but not L-lactate) when ldhd is disrupted, consistent with the expected role of mitochondrial LDHD in D-lactate clearance. (monroe2019identificationofhuman pages 3-4)
Lactate exists as two stereoisomers, L-lactate and D-lactate. In vertebrates, L-lactate is abundant and is primarily handled by NAD-dependent cytosolic LDH isoforms (LDHA/LDHB), whereas D-lactate is usually present at low concentrations and is mainly produced by (i) intestinal bacterial metabolism and (ii) endogenous methylglyoxal/glyoxalase metabolism, which yields D-lactate as a downstream product. Clinical literature emphasizes that D-lactate is typically low in healthy humans (reported range 5–20 μmol/L), but can rise markedly when clearance is impaired. (kwong2021humand‐lactatedehydrogenase pages 1-2)
In vertebrates, LDHD refers to a mitochondrial flavoprotein that oxidizes D-lactate to pyruvate. Importantly, mammalian LDHD is not the classical NAD-dependent “LDH” family (LDHA/LDHB), but a distinct enzyme class with different cofactor and mechanism. (jin2023lactatedehydrogenased pages 1-2)
The conserved vertebrate function of LDHD is oxidation of D-lactate to pyruvate. In zebrafish, the essential in vivo readout is that ldhd loss-of-function increases D-lactate levels while L-lactate remains unchanged, demonstrating stereospecificity for D-lactate metabolism. (monroe2019identificationofhuman pages 3-4, monroe2019identificationofhuman pages 5-6)
Beyond D-lactate, vertebrate LDHD acts more broadly on D-2-hydroxyacids. In human cases associated with LDHD variants, additional metabolites such as D-2-hydroxyisovaleric acid and D-2-hydroxyisocaproic acid can be elevated, and zebrafish data in the same study are consistent with LDHD participating in the metabolism of D-lactate and related D-2-hydroxyacids. (monroe2019identificationofhuman pages 5-6, monroe2019identificationofhuman pages 2-3)
The most detailed mechanistic/structural characterization comes from mammalian LDHD (mouse), which is strongly informative for zebrafish functional annotation because zebrafish genetics show the same directionality (D-lactate accumulation on loss). Mouse LDHD is:
Kinetic parameters reported for oxidation of D-lactate → pyruvate by mouse LDHD include KM = 122.0 ± 4.5 μM and kcat = 61.0 ± 0.6 min−1 (with Vmax 1.22 ± 0.01 μmol·min−1·mg−1). (jin2023lactatedehydrogenased pages 2-3)
Structural evidence supports a mechanism in which substrate binding and catalysis are coordinated by a positively charged pocket and a hydrophobic pocket; key residues coordinate Mn2+, and hydride transfer occurs to the flavin. (jin2023lactatedehydrogenased pages 6-7)
Vertebrate LDHD is consistently described as mitochondrial and associated with the mitochondrial inner membrane. Clinical/biochemical discussions cite mitochondrial uptake and metabolism of D-lactate and place the enzyme within mitochondrial metabolism rather than cytosolic glycolysis. (kwong2021humand‐lactatedehydrogenase pages 6-7)
A 2024 mitochondrial physiology study explicitly notes that LDHD is known to be associated with the mitochondrial inner membrane, and uses permeabilized-cell assays designed to preserve mitochondrial bioenergetics. (to2024pmfseqahighly pages 3-4)
A key open question historically was the physiological electron acceptor for mammalian LDHD. A 2024 study provided direct evidence that human LDHD transfers electrons from D-lactate to cytochrome c, thereby supporting mitochondrial membrane polarization. (to2024pmfseqahighly pages 1-2, to2024pmfseqahighly pages 4-5)
Experimentally, LDHD knockout (A375 and HepG2) cells showed a blunted mitochondrial membrane potential (ΔΨm) response to D-lactate, while retaining responses to ascorbate/TMPD (which donates electrons directly to cytochrome c), consistent with LDHD acting upstream of cytochrome c reduction. (to2024pmfseqahighly pages 3-4)
In vitro biochemical characterization in the same work quantified LDHD kinetics for cytochrome c reduction with kcat ~103 min−1 and KM ~112 μM (reported with uncertainty in the paper). (to2024pmfseqahighly pages 4-5)
The central zebrafish functional evidence comes from a zebrafish ldhd knockout allele (sa15623) that disrupts an essential splice site and yields an ldhd−/− line that is adult viable and fertile. (monroe2019identificationofhuman pages 6-7)
At larval stages, maternal-zygotic ldhd−/− embryos were reported to have elevated D-lactate while L-lactate remained unchanged, and no obvious morphological abnormalities were observed at early developmental time points examined. (monroe2019identificationofhuman pages 3-4, monroe2019identificationofhuman pages 5-6)
Causality and conservation were tested by mRNA rescue: microinjection of wild-type human LDHD mRNA restored D-lactate toward baseline, whereas mRNAs encoding patient-associated LDHD variants failed to rescue, supporting that the zebrafish phenotype reflects LDHD enzymatic loss-of-function rather than background effects. (monroe2019identificationofhuman pages 3-4)
A key pathway framing is that D-lactate is not only microbe-derived, but can also arise endogenously from central carbon metabolism via the methylglyoxal (MG) / glyoxalase pathway. LDHD is discussed as part of the broader concept of metabolite repair, in which enzymes prevent accumulation of side-products and damaged metabolites; in this view, mitochondrial LDHD clears D-lactate and potentially other D-2-hydroxyacids. (monroe2019identificationofhuman pages 4-5, kwong2021humand‐lactatedehydrogenase pages 6-7)
A 2023 Nature Communications study established LDHD as an Mn2+-dependent FAD enzyme with broad activity toward hydrophobic D-2-hydroxyacids, and provided multiple structures of the enzyme with FAD/Mn2+ and ligands, substantially strengthening the mechanistic basis for substrate specificity and interpretation of pathogenic variants. (Publication date: Oct 2023; URL: https://doi.org/10.1038/s41467-023-42456-3) (jin2023lactatedehydrogenased pages 1-2, jin2023lactatedehydrogenased pages 2-3)
A 2023 Rheumatology paper linked rare recessive LDHD variants to early-onset (juvenile) gout, with homozygotes having significantly altered urate handling and higher D-lactate (blood and urine) compared with non-homozygotes in at least one family analysis. (Publication date: Apr 2023; URL: https://doi.org/10.1093/rheumatology/kead118) (jin2023lactatedehydrogenased pages 9-10)
A 2024 Nature Metabolism study provided direct biochemical and functional evidence that human LDHD transfers electrons from D-lactate to cytochrome c, establishing a concrete respiratory-chain connection and explaining LDHD-dependent mitochondrial membrane polarization in permeabilized cells. (Publication date: Feb 2024; URL: https://doi.org/10.1038/s42255-024-00994-0) (to2024pmfseqahighly pages 1-2, to2024pmfseqahighly pages 4-5)
Human genetics and biochemical phenotyping indicate that LDHD loss-of-function is a cause of chronically elevated D-lactate in plasma/urine, expanding differential diagnoses beyond classic short-bowel D-lactic acidosis. In the 2019 Nature Communications report, one patient’s mean urinary D-lactate excretion was reported as 1686 mmol/mol creatinine, with plasma D-lactate 0.7 mM, and the report notes that overt D-lactic acidosis is typically considered at plasma D-lactate >3 mmol/L. (Publication date: Apr 2019; URL: https://doi.org/10.1038/s41467-019-09458-6) (monroe2019identificationofhuman pages 1-2)
These findings support real-world use of D-lactate measurements (blood/urine) and potentially additional D-2-hydroxyacid profiles as part of the diagnostic workup for unexplained D-lactate elevations. (monroe2019identificationofhuman pages 2-3, jin2023lactatedehydrogenased pages 9-10)
Zebrafish ldhd knockout provides an in vivo system for mechanistic validation of human variants (via mRNA rescue) and for studying D-lactate homeostasis. The reported absence of gross early developmental abnormalities while showing a strong biochemical phenotype suggests feasibility for metabolic/pathway experiments without confounding early lethality. (monroe2019identificationofhuman pages 3-4, monroe2019identificationofhuman pages 6-7)
The following table consolidates claims, evidence type, quantitative values, organism context, and citations.
| Claim/annotation item | Evidence type (genetic, biochemical, structural, review) | Key details (reaction, cofactors, localization, phenotype) | Organism/model | Key quantitative data | Primary source (authors, journal, year) with URL | PaperQA citation id |
|---|---|---|---|---|---|---|
| Identity verification for target gene | Database-supported functional annotation + comparative evidence | UniProt F1QXM5 corresponds to Danio rerio ldhd, annotated as mitochondrial D-lactate dehydrogenase in the FAD-binding oxidoreductase/transferase family; zebrafish functional studies align with this identity because ldhd loss selectively elevates D-lactate, not L-lactate | Zebrafish; vertebrate comparison | Maternal-zygotic ldhd−/− embryos show increased D-lactate with unchanged L-lactate; no overt early morphology defect reported | Monroe et al., Nature Communications (2019). https://doi.org/10.1038/s41467-019-09458-6 | (monroe2019identificationofhuman pages 3-4, monroe2019identificationofhuman pages 4-5) |
| Primary enzymatic function | Human/vertebrate genetics + biochemistry | LDHD catalyzes oxidation of D-lactate to pyruvate; zebrafish knockout/rescue supports the same pathway assignment for ldhd | Human, mouse, zebrafish | Human baseline circulating D-lactate reported as 5–20 μmol/L; patient serum D-lactate 0.61 mmol/L in one case report | Kwong et al., JIMD Reports (2021). https://doi.org/10.1002/jmd2.12220; Jin et al., Nature Communications (2023). https://doi.org/10.1038/s41467-023-42456-3 | (kwong2021humand‐lactatedehydrogenase pages 1-2, jin2023lactatedehydrogenased pages 1-2) |
| Zebrafish loss-of-function phenotype | Genetic | ENU allele sa15623 disrupts a donor splice site after exon 3, generating a knockout; homozygous fish are viable/fertile, but embryos accumulate D-lactate; wild-type human LDHD mRNA rescues, patient-variant mRNAs do not | Danio rerio | Assays at 3 dpf; 3 biological replicates of pooled 10 embryos; injected mRNA 5 ng/μl | Monroe et al., Nature Communications (2019). https://doi.org/10.1038/s41467-019-09458-6 | (monroe2019identificationofhuman pages 3-4, monroe2019identificationofhuman pages 5-6, monroe2019identificationofhuman pages 6-7) |
| Stereospecificity | Genetic + biochemical | LDHD is specific for D- not L- hydroxyacids; zebrafish ldhd loss increases D-lactate while leaving L-lactate unchanged; purified mammalian LDHD shows no activity/binding for L-lactate | Zebrafish; mouse | Mouse LDHD: no measurable activity with L-lactate; zebrafish knockout selectively elevates D-lactate | Monroe et al., Nature Communications (2019). https://doi.org/10.1038/s41467-019-09458-6; Jin et al., Nature Communications (2023). https://doi.org/10.1038/s41467-023-42456-3 | (monroe2019identificationofhuman pages 3-4, jin2023lactatedehydrogenased pages 2-3) |
| Broader substrate specificity | Biochemical + structural | LDHD is a general dehydrogenase for D-2-hydroxyacids with hydrophobic C2 substituents, including D-2-hydroxyisovalerate, D-2-hydroxyisocaproate, and D-2-hydroxy-3-methylvalerate; likely explains elevated branched-chain D-2-hydroxyacids in patients | Mouse enzyme; human disease inference | D-lactate: Vmax 1.22 μmol·min−1·mg−1, KM 122.0 ± 4.5 μM, kcat 61.0 ± 0.6 min−1, kcat/KM 0.50 min−1·μM−1; some alternative D-2-hydroxyacids show 2.5–8-fold higher catalytic efficiencies than D-lactate | Jin et al., Nature Communications (2023). https://doi.org/10.1038/s41467-023-42456-3 | (jin2023lactatedehydrogenased pages 3-4, jin2023lactatedehydrogenased pages 2-3) |
| Cofactor requirement | Biochemical + structural | LDHD is an FAD-containing flavoprotein; purified protein is yellow and shows 450-nm absorbance; FAD-binding defects explain pathogenic variants | Mouse enzyme; human disease inference | FAD:protein molar ratio 0.73 ± 0.04 | Jin et al., Nature Communications (2023). https://doi.org/10.1038/s41467-023-42456-3 | (jin2023lactatedehydrogenased pages 1-2, jin2023lactatedehydrogenased pages 8-9) |
| Metal dependence | Biochemical + structural | LDHD is Mn2+-dependent; active site includes Mn2+ coordinated by catalytic residues; no activity without divalent metal ions | Mouse enzyme | Optimal Mn2+ concentration 30–200 μM; reduced activity with Co2+, Ni2+, Ca2+; none with Mg2+, Zn2+, Cd2+, Cu2+ | Jin et al., Nature Communications (2023). https://doi.org/10.1038/s41467-023-42456-3 | (jin2023lactatedehydrogenased pages 2-3, jin2023lactatedehydrogenased pages 6-7) |
| Catalytic mechanism | Structural + biochemical | Positively charged subsite binds the glycolate/carboxylate moiety and Mn2+; hydrophobic subsite accommodates variable hydrophobic groups; His443 acts as catalytic base and hydride is transferred to FAD N5 | Mouse enzyme, structural model for vertebrate LDHD | Pathogenic or active-site mutations cause near-complete activity loss; alanine substitutions abolish activity | Jin et al., Nature Communications (2023). https://doi.org/10.1038/s41467-023-42456-3 | (jin2023lactatedehydrogenased pages 6-7, jin2023lactatedehydrogenased pages 8-9) |
| Subcellular localization | Comparative/clinical evidence + structural/annotation synthesis | LDHD is described as mitochondrial, with localization to the mitochondrial inner membrane; rat liver mitochondrial uptake/metabolism data and human clinical literature support mitochondrial localization; this matches UniProt annotation for zebrafish F1QXM5 | Mammals; inferred conserved vertebrate localization including zebrafish | No zebrafish-specific localization quantitation reported in extracted evidence | Kwong et al., JIMD Reports (2021). https://doi.org/10.1002/jmd2.12220; Jin et al., Nature Communications (2023). https://doi.org/10.1038/s41467-023-42456-3 | (kwong2021humand‐lactatedehydrogenase pages 6-7, jin2023lactatedehydrogenased pages 1-2) |
| Electron transfer / respiratory-chain coupling | Recent primary mechanistic study | Human LDHD specifically conveys electrons from D-lactate into cytochrome c to support mitochondrial membrane polarization; response is LDHD-dependent and distinct from direct cytochrome c donation by ascorbate/TMPD | Human cell lines; purified human LDHD | Human LDHD biochemical parameters reported as kcat 103.36 ± 2.14 min−1, KM 112.46 ± 10.68 μM | To et al., Nature Metabolism (2024). https://doi.org/10.1038/s42255-024-00994-0 | (to2024pmfseqahighly pages 3-4) |
| Physiological redox partner remains partly unresolved in earlier work | Review/analysis of mechanistic literature | Earlier vertebrate work inferred respiratory-chain coupling and possible cytochrome-c linkage from lower organisms/plants, but mammalian electron acceptor assignment was uncertain before direct 2024 evidence | Mammals/lower organisms | Not quantified in excerpt | Kwong et al., JIMD Reports (2021). https://doi.org/10.1002/jmd2.12220 | (kwong2021humand‐lactatedehydrogenase pages 6-7, kwong2021humand‐lactatedehydrogenase pages 7-8) |
| Disease association: D-lactic acidosis | Human genetics + zebrafish functional validation | Damaging LDHD variants cause loss of function with elevated plasma/urine D-lactate; zebrafish rescue experiments establish causality for LDHD in vivo | Human; zebrafish | Urinary D-lactate excretion reported at 1686 mmol/mol creatinine; plasma D-lactate 0.7 mM in one 2019 case; D-lactic acidosis threshold noted as >3 mmol/L plasma | Monroe et al., Nature Communications (2019). https://doi.org/10.1038/s41467-019-09458-6 | (monroe2019identificationofhuman pages 1-2) |
| Disease association: neurological/mitochondrial phenotype | Human case report | LDHD deficiency can co-occur with neurological manifestations and mitochondrial complex IV deficiency, expanding possible clinical relevance beyond isolated biochemical abnormality | Human patient | Serum D-lactate 0.61 mmol/L (reference 0–0.25 mmol/L) | Kwong et al., JIMD Reports (2021). https://doi.org/10.1002/jmd2.12220 | (kwong2021humand‐lactatedehydrogenase pages 1-2) |
| Disease association: gout/hyperuricemia | Human genetics (recent) | Rare recessive LDHD variants linked to early-onset gout, likely via D-lactate accumulation and impaired urate handling; suggests broader metabolic significance of LDHD deficiency | Human families | In one family: higher hyperuricemia (p = 0.02), lower FCU (p = 0.002), higher blood D-lactate (p = 0.04), higher urine D-lactate (p = 0.06) in homozygotes | Bardin et al., Rheumatology (2023). https://doi.org/10.1093/rheumatology/kead118 | (jin2023lactatedehydrogenased pages 9-10) |
| Pathway context | Review + primary evidence | LDHD functions downstream of the methylglyoxal/glyoxalase pathway, removing D-lactate generated endogenously; may also clear other D-2-hydroxyacid “metabolite damage” products | Vertebrates | Not primarily quantitative in excerpt | Bommer et al., Trends in Biochemical Sciences (2020). https://doi.org/10.1016/j.tibs.2019.07.004; Monroe et al., Nature Communications (2019). https://doi.org/10.1038/s41467-019-09458-6 | (monroe2019identificationofhuman pages 4-5, monroe2019identificationofhuman pages 5-6) |
Table: This table summarizes the strongest evidence for functional annotation of zebrafish ldhd (UniProt F1QXM5) together with vertebrate LDHD literature. It emphasizes verified identity, catalytic function, localization, pathway context, and the best available quantitative data from primary studies.
Collectively, the strongest evidence supports annotating zebrafish ldhd (F1QXM5) as a mitochondrial FAD-dependent D-2-hydroxyacid dehydrogenase whose primary physiological role is oxidation of D-lactate to pyruvate, with high stereoselectivity for D- over L-lactate. In zebrafish, genetic loss of ldhd causes in vivo accumulation of D-lactate without major early morphological defects in reported assays, and the biochemical phenotype is rescuable by wild-type LDHD. (monroe2019identificationofhuman pages 3-4, monroe2019identificationofhuman pages 5-6)
Modern vertebrate mechanistic work (2023–2024) further indicates that LDHD is Mn2+-dependent, can act on multiple hydrophobic D-2-hydroxyacids, and in humans can transfer electrons from D-lactate to cytochrome c to support mitochondrial membrane polarization—positioning LDHD at the interface of D-lactate clearance and mitochondrial redox physiology. (jin2023lactatedehydrogenased pages 2-3, to2024pmfseqahighly pages 1-2, to2024pmfseqahighly pages 4-5)
References
(monroe2019identificationofhuman pages 3-4): Glen R. Monroe, Albertien M. van Eerde, Federico Tessadori, Karen J. Duran, Sanne M. C. Savelberg, Johanna C. van Alfen, Paulien A. Terhal, Saskia N. van der Crabben, Klaske D. Lichtenbelt, Sabine A. Fuchs, Johan Gerrits, Markus J. van Roosmalen, Koen L. van Gassen, Mirjam van Aalderen, Bart G. Koot, Marlies Oostendorp, Marinus Duran, Gepke Visser, Tom J. de Koning, Francesco Calì, Paolo Bosco, Karin Geleijns, Monique G. M. de Sain-van der Velden, Nine V. Knoers, Jeroen Bakkers, Nanda M. Verhoeven-Duif, Gijs van Haaften, and Judith J. Jans. Identification of human d lactate dehydrogenase deficiency. Nature Communications, Apr 2019. URL: https://doi.org/10.1038/s41467-019-09458-6, doi:10.1038/s41467-019-09458-6. This article has 109 citations and is from a highest quality peer-reviewed journal.
(kwong2021humand‐lactatedehydrogenase pages 1-2): Anna Ka‐Yee Kwong, Sheila Suet‐Na Wong, Richard J. T. Rodenburg, Jan Smeitink, Godfrey Chi Fung Chan, and Cheuk‐Wing Fung. Human d‐lactate dehydrogenase deficiency by ldhd mutation in a patient with neurological manifestations and mitochondrial complex iv deficiency. JIMD Reports, 60:15-22, May 2021. URL: https://doi.org/10.1002/jmd2.12220, doi:10.1002/jmd2.12220. This article has 16 citations and is from a peer-reviewed journal.
(jin2023lactatedehydrogenased pages 1-2): Shan Jin, Xingchen Chen, Jun Yang, and Jianping Ding. Lactate dehydrogenase d is a general dehydrogenase for d-2-hydroxyacids and is associated with d-lactic acidosis. Nature Communications, Oct 2023. URL: https://doi.org/10.1038/s41467-023-42456-3, doi:10.1038/s41467-023-42456-3. This article has 61 citations and is from a highest quality peer-reviewed journal.
(monroe2019identificationofhuman pages 5-6): Glen R. Monroe, Albertien M. van Eerde, Federico Tessadori, Karen J. Duran, Sanne M. C. Savelberg, Johanna C. van Alfen, Paulien A. Terhal, Saskia N. van der Crabben, Klaske D. Lichtenbelt, Sabine A. Fuchs, Johan Gerrits, Markus J. van Roosmalen, Koen L. van Gassen, Mirjam van Aalderen, Bart G. Koot, Marlies Oostendorp, Marinus Duran, Gepke Visser, Tom J. de Koning, Francesco Calì, Paolo Bosco, Karin Geleijns, Monique G. M. de Sain-van der Velden, Nine V. Knoers, Jeroen Bakkers, Nanda M. Verhoeven-Duif, Gijs van Haaften, and Judith J. Jans. Identification of human d lactate dehydrogenase deficiency. Nature Communications, Apr 2019. URL: https://doi.org/10.1038/s41467-019-09458-6, doi:10.1038/s41467-019-09458-6. This article has 109 citations and is from a highest quality peer-reviewed journal.
(monroe2019identificationofhuman pages 2-3): Glen R. Monroe, Albertien M. van Eerde, Federico Tessadori, Karen J. Duran, Sanne M. C. Savelberg, Johanna C. van Alfen, Paulien A. Terhal, Saskia N. van der Crabben, Klaske D. Lichtenbelt, Sabine A. Fuchs, Johan Gerrits, Markus J. van Roosmalen, Koen L. van Gassen, Mirjam van Aalderen, Bart G. Koot, Marlies Oostendorp, Marinus Duran, Gepke Visser, Tom J. de Koning, Francesco Calì, Paolo Bosco, Karin Geleijns, Monique G. M. de Sain-van der Velden, Nine V. Knoers, Jeroen Bakkers, Nanda M. Verhoeven-Duif, Gijs van Haaften, and Judith J. Jans. Identification of human d lactate dehydrogenase deficiency. Nature Communications, Apr 2019. URL: https://doi.org/10.1038/s41467-019-09458-6, doi:10.1038/s41467-019-09458-6. This article has 109 citations and is from a highest quality peer-reviewed journal.
(jin2023lactatedehydrogenased pages 2-3): Shan Jin, Xingchen Chen, Jun Yang, and Jianping Ding. Lactate dehydrogenase d is a general dehydrogenase for d-2-hydroxyacids and is associated with d-lactic acidosis. Nature Communications, Oct 2023. URL: https://doi.org/10.1038/s41467-023-42456-3, doi:10.1038/s41467-023-42456-3. This article has 61 citations and is from a highest quality peer-reviewed journal.
(jin2023lactatedehydrogenased pages 6-7): Shan Jin, Xingchen Chen, Jun Yang, and Jianping Ding. Lactate dehydrogenase d is a general dehydrogenase for d-2-hydroxyacids and is associated with d-lactic acidosis. Nature Communications, Oct 2023. URL: https://doi.org/10.1038/s41467-023-42456-3, doi:10.1038/s41467-023-42456-3. This article has 61 citations and is from a highest quality peer-reviewed journal.
(kwong2021humand‐lactatedehydrogenase pages 6-7): Anna Ka‐Yee Kwong, Sheila Suet‐Na Wong, Richard J. T. Rodenburg, Jan Smeitink, Godfrey Chi Fung Chan, and Cheuk‐Wing Fung. Human d‐lactate dehydrogenase deficiency by ldhd mutation in a patient with neurological manifestations and mitochondrial complex iv deficiency. JIMD Reports, 60:15-22, May 2021. URL: https://doi.org/10.1002/jmd2.12220, doi:10.1002/jmd2.12220. This article has 16 citations and is from a peer-reviewed journal.
(to2024pmfseqahighly pages 3-4): Tsz-Leung To, Jason G. McCoy, Naomi K. Ostriker, Lev S. Sandler, Carmen A. Mannella, and Vamsi K. Mootha. Pmf-seq: a highly scalable screening strategy for linking genetics to mitochondrial bioenergetics. Nature Metabolism, 6:687-696, Feb 2024. URL: https://doi.org/10.1038/s42255-024-00994-0, doi:10.1038/s42255-024-00994-0. This article has 8 citations and is from a domain leading peer-reviewed journal.
(to2024pmfseqahighly pages 1-2): Tsz-Leung To, Jason G. McCoy, Naomi K. Ostriker, Lev S. Sandler, Carmen A. Mannella, and Vamsi K. Mootha. Pmf-seq: a highly scalable screening strategy for linking genetics to mitochondrial bioenergetics. Nature Metabolism, 6:687-696, Feb 2024. URL: https://doi.org/10.1038/s42255-024-00994-0, doi:10.1038/s42255-024-00994-0. This article has 8 citations and is from a domain leading peer-reviewed journal.
(to2024pmfseqahighly pages 4-5): Tsz-Leung To, Jason G. McCoy, Naomi K. Ostriker, Lev S. Sandler, Carmen A. Mannella, and Vamsi K. Mootha. Pmf-seq: a highly scalable screening strategy for linking genetics to mitochondrial bioenergetics. Nature Metabolism, 6:687-696, Feb 2024. URL: https://doi.org/10.1038/s42255-024-00994-0, doi:10.1038/s42255-024-00994-0. This article has 8 citations and is from a domain leading peer-reviewed journal.
(monroe2019identificationofhuman pages 6-7): Glen R. Monroe, Albertien M. van Eerde, Federico Tessadori, Karen J. Duran, Sanne M. C. Savelberg, Johanna C. van Alfen, Paulien A. Terhal, Saskia N. van der Crabben, Klaske D. Lichtenbelt, Sabine A. Fuchs, Johan Gerrits, Markus J. van Roosmalen, Koen L. van Gassen, Mirjam van Aalderen, Bart G. Koot, Marlies Oostendorp, Marinus Duran, Gepke Visser, Tom J. de Koning, Francesco Calì, Paolo Bosco, Karin Geleijns, Monique G. M. de Sain-van der Velden, Nine V. Knoers, Jeroen Bakkers, Nanda M. Verhoeven-Duif, Gijs van Haaften, and Judith J. Jans. Identification of human d lactate dehydrogenase deficiency. Nature Communications, Apr 2019. URL: https://doi.org/10.1038/s41467-019-09458-6, doi:10.1038/s41467-019-09458-6. This article has 109 citations and is from a highest quality peer-reviewed journal.
(monroe2019identificationofhuman pages 4-5): Glen R. Monroe, Albertien M. van Eerde, Federico Tessadori, Karen J. Duran, Sanne M. C. Savelberg, Johanna C. van Alfen, Paulien A. Terhal, Saskia N. van der Crabben, Klaske D. Lichtenbelt, Sabine A. Fuchs, Johan Gerrits, Markus J. van Roosmalen, Koen L. van Gassen, Mirjam van Aalderen, Bart G. Koot, Marlies Oostendorp, Marinus Duran, Gepke Visser, Tom J. de Koning, Francesco Calì, Paolo Bosco, Karin Geleijns, Monique G. M. de Sain-van der Velden, Nine V. Knoers, Jeroen Bakkers, Nanda M. Verhoeven-Duif, Gijs van Haaften, and Judith J. Jans. Identification of human d lactate dehydrogenase deficiency. Nature Communications, Apr 2019. URL: https://doi.org/10.1038/s41467-019-09458-6, doi:10.1038/s41467-019-09458-6. This article has 109 citations and is from a highest quality peer-reviewed journal.
(jin2023lactatedehydrogenased pages 9-10): Shan Jin, Xingchen Chen, Jun Yang, and Jianping Ding. Lactate dehydrogenase d is a general dehydrogenase for d-2-hydroxyacids and is associated with d-lactic acidosis. Nature Communications, Oct 2023. URL: https://doi.org/10.1038/s41467-023-42456-3, doi:10.1038/s41467-023-42456-3. This article has 61 citations and is from a highest quality peer-reviewed journal.
(monroe2019identificationofhuman pages 1-2): Glen R. Monroe, Albertien M. van Eerde, Federico Tessadori, Karen J. Duran, Sanne M. C. Savelberg, Johanna C. van Alfen, Paulien A. Terhal, Saskia N. van der Crabben, Klaske D. Lichtenbelt, Sabine A. Fuchs, Johan Gerrits, Markus J. van Roosmalen, Koen L. van Gassen, Mirjam van Aalderen, Bart G. Koot, Marlies Oostendorp, Marinus Duran, Gepke Visser, Tom J. de Koning, Francesco Calì, Paolo Bosco, Karin Geleijns, Monique G. M. de Sain-van der Velden, Nine V. Knoers, Jeroen Bakkers, Nanda M. Verhoeven-Duif, Gijs van Haaften, and Judith J. Jans. Identification of human d lactate dehydrogenase deficiency. Nature Communications, Apr 2019. URL: https://doi.org/10.1038/s41467-019-09458-6, doi:10.1038/s41467-019-09458-6. This article has 109 citations and is from a highest quality peer-reviewed journal.
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(jin2023lactatedehydrogenased pages 3-4): Shan Jin, Xingchen Chen, Jun Yang, and Jianping Ding. Lactate dehydrogenase d is a general dehydrogenase for d-2-hydroxyacids and is associated with d-lactic acidosis. Nature Communications, Oct 2023. URL: https://doi.org/10.1038/s41467-023-42456-3, doi:10.1038/s41467-023-42456-3. This article has 61 citations and is from a highest quality peer-reviewed journal.
(jin2023lactatedehydrogenased pages 8-9): Shan Jin, Xingchen Chen, Jun Yang, and Jianping Ding. Lactate dehydrogenase d is a general dehydrogenase for d-2-hydroxyacids and is associated with d-lactic acidosis. Nature Communications, Oct 2023. URL: https://doi.org/10.1038/s41467-023-42456-3, doi:10.1038/s41467-023-42456-3. This article has 61 citations and is from a highest quality peer-reviewed journal.