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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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 accession P11348 corresponds to Qdpr (syn. Dhpr) from Rattus norvegicus, encoding dihydropteridine reductase (DHPR; QDPR), an NAD(H)-dependent oxidoreductase that catalyzes regeneration of tetrahydrobiopterin (BH4) from quinonoid dihydrobiopterin (qBH2). Its primary biological role is to maintain BH4 in the reduced, active form to support BH4-dependent enzymes—including phenylalanine hydroxylase (PAH), tyrosine hydroxylase (TH), tryptophan hydroxylase (TPH), and nitric oxide synthase (NOS)—thereby linking QDPR activity to amino-acid metabolism, monoamine neurotransmitter synthesis, and nitric oxide biology. The rat enzyme has a well-defined dimeric structure with an NADH-binding Rossmann fold and a four-helix bundle dimer interface. (varughese1992crystalstructureof pages 1-2, varughese1992crystalstructureof pages 2-4, tai2024dopaminesynthesisand pages 4-5, thony2000tetrahydrobiopterinbiosynthesisregeneration pages 12-13)
Dihydropteridine reductase (DHPR/QDPR) is the terminal enzyme of the canonical BH4 recycling (regeneration) pathway. In the BH4 network, BH4 is consumed/oxidized during aromatic amino-acid hydroxylase reactions and NOS catalysis; recycling prevents functional BH4 depletion and limits accumulation of oxidized biopterins. (breuer2018characterizingthefunction pages 15-19)
The core reaction catalyzed by rat DHPR is the reduction of quinonoid dihydrobiopterin (qBH2) to tetrahydrobiopterin (BH4). A 2024 expert review in the context of dopamine disorders explicitly states DHPR (gene QDPR) catalyzes the reduction of qBH2 back to BH4 and that it uses NADH as cofactor. (tai2024dopaminesynthesisand pages 4-5)
Mechanistically, the rat crystal structure demonstrates DHPR transfers the pro-S hydrogen of NADH to N5 of qBH2, classifying DHPR as a B-stereospecific dehydrogenase. (varughese1992crystalstructureof pages 2-4)
A widely used conceptual model of BH4 homeostasis divides BH4 metabolism into (i) de novo synthesis (GTPCH → PTPS → SPR) and (ii) a two-step recycling pathway in which pterin-4α-carbinolamine dehydratase (PCD) converts a carbinolamine intermediate to qBH2, which is then reduced back to BH4 by DHPR/QDPR. (breuer2018characterizingthefunction pages 15-19)
Direct structural evidence shows NADH bound in the rat DHPR crystal structure and supports NADH as the physiologic electron donor. (varughese1992crystalstructureof pages 1-2, varughese1992crystalstructureof pages 2-4)
Older rat biochemical work indicates NADH is more effective than NADPH in vitro, while allowing that NADPH may contribute in vivo depending on cellular redox pools. (cutler1986dihydropteridinereductase pages 58-64)
The canonical rat DHPR structure was solved from rat liver as a binary complex with NADH (publication date: July 1992, PNAS). The enzyme shows an α/β architecture with a Rossmann-type dinucleotide-binding fold, consistent with an NAD(H)-binding dehydrogenase/reductase enzyme. (varughese1992crystalstructureof pages 1-2)
The protein exists as a dimer in solution; dimerization is mediated by a four-helix bundle formed by helices contributed from each protomer. (varughese1992crystalstructureof pages 2-4)
The active site lies in a U-shaped cleft adjacent to the bound NADH; structural figures in the PNAS report depict both the dimer interface and an inferred substrate binding mode. (varughese1992crystalstructureof media 27840a6e, varughese1992crystalstructureof media a6c6b231)
Rat DHPR is classically described as a dimeric enzyme (~50–52 kDa) with subunits ~25–26 kDa, aligning with biochemical descriptions used in the DHPR deficiency literature. (cutler1986dihydropteridinereductase pages 58-64, smooker1995molecularbasisof pages 1-3)
QDPR supports PAH function by sustaining BH4 availability; impairment of QDPR function can therefore contribute to hyperphenylalaninemia via BH4 deficiency mechanisms. (breuer2018characterizingthefunction pages 19-24, ghanei2023acomprehensivestudy pages 1-2)
BH4 is an obligate cofactor for TH and TPH, and the BH4 recycling reaction mediated by DHPR is therefore an upstream determinant of monoamine neurotransmitter biosynthetic capacity. (breuer2018characterizingthefunction pages 15-19, tai2024dopaminesynthesisand pages 1-2)
A 2024 authoritative review on dopamine synthesis and therapeutics explicitly includes DHPR/QDPR among the “main proteins involved in DA synthesis and transport,” highlighting that DHPR regenerates BH4 from qBH2 and uses NADH. (tai2024dopaminesynthesisand pages 4-5)
BH4 is required for NOS activity. The BH4 network description explicitly notes BH4 is necessary for NOS-mediated NO production (arginine → citrulline + NO), and DHPR participates by maintaining BH4 in the reduced form through recycling. (breuer2018characterizingthefunction pages 15-19)
A highly cited BH4 pathway review states DHPR is widely distributed in animal tissues and is present in brain and adrenal medulla, where it supports the tyrosine and tryptophan hydroxylation systems (consistent with a role in monoamine biosynthesis). (thony2000tetrahydrobiopterinbiosynthesisregeneration pages 12-13)
The biochemical role of DHPR in BH4 recycling is most consistent with a soluble cytosolic enzyme that interacts with cytosolic BH4-dependent hydroxylation systems; a cell-based study reported wild-type QDPR is mainly cytoplasmic (with a mutant showing altered localization). (si2017a278cmutationof pages 5-6, breuer2018characterizingthefunction pages 15-19)
Note on annotation scope: Some comparative vertebrate expression evidence suggests glial enrichment for QDPR orthologs, but this is not yet definitive specifically for rat Qdpr/P11348 and should be treated as hypothesis-generating rather than primary annotation. (breuer2018characterizingthefunction pages 106-108)
A 2024 review (Biochemical Society Transactions; publication date May 2024) highlights DHPR deficiency as a cause of severe neurological disease and provides quantitative context: DHPR defects account for ~33% of BH4 deficiency cases with ~303 reported patients. This framing underscores QDPR’s clinical importance despite rarity and reflects current expert consensus about its mechanistic role in neurotransmitter disorders. (tai2024dopaminesynthesisand pages 4-5)
URL/DOI: https://doi.org/10.1042/bst20231061 (tai2024dopaminesynthesisand pages 4-5)
A 2024 review (Journal of Inherited Metabolic Disease; publication date Jan 2024) catalogues available murine models of BH4 biosynthesis and recycling disorders and explicitly lists a DHPR-deficient knockout model (Dpr-ko) among core BH4-pathway models used for mechanistic and therapeutic studies. (thony2024mousemodelsfor pages 8-9)
URL/DOI: https://doi.org/10.1002/jimd.12710 (thony2024mousemodelsfor pages 8-9)
A 2023 systematic review of Iranian hyperphenylalaninemia sequencing studies (Human Heredity; publication date Jan 2023) provides actionable clinical-genetics data for QDPR:
- 29 distinct disease-causing QDPR variants, including 17 novel variants. (ghanei2023acomprehensivestudy pages 1-1, ghanei2023acomprehensivestudy pages 2-3)
- The authors propose a preliminary genetic diagnostic panel including 18 QDPR variants, arguing it would capture >75% of documented disease-causing variants in that population. (ghanei2023acomprehensivestudy pages 1-1, ghanei2023acomprehensivestudy pages 1-2)
- QDPR evidence base was limited to 3 studies and 50 individuals, but still yielded high allelic diversity—supporting inclusion of QDPR in multi-gene HPA/BH4-deficiency panels as a cost-effective diagnostic implementation. (ghanei2023acomprehensivestudy pages 2-3)
URL/DOI: https://doi.org/10.1159/000529037 (ghanei2023acomprehensivestudy pages 1-1)
While newborn screening programs typically detect elevated phenylalanine, definitive etiologic classification of hyperphenylalaninemia requires biochemical and/or genetic differentiation of PAH deficiency vs BH4-pathway defects (including QDPR). The 2023 systematic review explicitly notes that routine screening measurements do not identify causative variants and that sequencing enables definitive familial variant identification and prenatal diagnosis. (ghanei2023acomprehensivestudy pages 2-3)
In clinical neurometabolic practice and in therapeutic strategy discussions for dopamine-deficiency disorders, DHPR/QDPR is treated as part of the BH4 cofactor axis that can be targeted with replacement strategies (BH4 and neurotransmitter precursors) and with emerging disease-modifying approaches for dopamine disorders. This is reflected by inclusion of DHPR/QDPR among core proteins in a 2024 therapeutics-focused review. (tai2024dopaminesynthesisand pages 4-5, tai2024dopaminesynthesisand pages 1-2)
The existence of DHPR-deficient animal models (e.g., Dpr-ko) supports real-world experimental implementations for mechanism discovery and therapy testing in monoamine neurotransmitter disorders and BH4 biology. (thony2024mousemodelsfor pages 8-9)
Key quantitative points supported by the retrieved literature include:
- DHPR deficiency proportion and case count: ~33% of BH4 deficiency cases, ~303 reported patients (reviewed 2024). (tai2024dopaminesynthesisand pages 4-5)
- QDPR variant spectrum (Iranian HPA): 29 QDPR disease-causing variants, 17 novel, with 18 proposed for a panel capturing >75% of documented variants (systematic review 2023). (ghanei2023acomprehensivestudy pages 1-1)
- Rat DHPR macromolecular properties: dimeric enzyme, ~50–52 kDa holoenzyme with ~25–26 kDa subunits (rat biochemical work), consistent with other DHPR literature. (cutler1986dihydropteridinereductase pages 58-64, smooker1995molecularbasisof pages 1-3)
- Structural/mechanistic detail: hydride transfer from NADH pro-S hydrogen to qBH2 N5, indicating B-stereospecificity (rat crystal structure 1992). (varughese1992crystalstructureof pages 2-4)
The strongest and most conservative functional annotation for rat Qdpr (P11348) is a cytosolic BH4-recycling enzyme that ensures reduced BH4 availability for BH4-dependent hydroxylases and NOS. This interpretation is anchored by (i) direct rat structural biology demonstrating NADH binding, dimeric architecture, and mechanistic hydride transfer, and (ii) modern expert reviews that explicitly tie the enzyme’s reaction to monoamine neurotransmitter disorders and provide updated disease-burden estimates. (varughese1992crystalstructureof pages 2-4, tai2024dopaminesynthesisand pages 4-5)
From an annotation perspective, it is also important that QDPR sits at a metabolic “chokepoint”: even if BH4 synthesis is intact, loss of BH4 regeneration can effectively create functional BH4 deficiency in tissues with high BH4 turnover (e.g., CNS monoamine systems), consistent with severe neurological phenotypes described in clinical reviews. (tai2024dopaminesynthesisand pages 4-5, thony2000tetrahydrobiopterinbiosynthesisregeneration pages 12-13)
The following table compiles the most relevant functional-annotation facts, including recent 2023–2024 developments and key quantitative values.
| Aspect | Current understanding | Key evidence | Pub year | URL/DOI |
|---|---|---|---|---|
| Target identity / disambiguation | UniProt P11348 corresponds to rat Qdpr/Dhpr, the enzyme dihydropteridine reductase (DHPR) from Rattus norvegicus; structural and biochemical literature on rat liver DHPR aligns with the UniProt description and supports use of mammalian QDPR literature for pathway interpretation. | Rat liver DHPR structure solved directly; rat and human enzymes are highly similar, supporting identity mapping to mammalian QDPR/DHPR (varughese1992crystalstructureof pages 1-2, varughese1992crystalstructureof pages 2-4) | 1992 | https://doi.org/10.1073/pnas.89.13.6080 |
| Reaction catalyzed | DHPR catalyzes reduction of quinonoid dihydrobiopterin (qBH2) back to tetrahydrobiopterin (BH4), regenerating the reduced pterin cofactor required after aromatic amino acid hydroxylase reactions. | Rat structural paper and reviews explicitly describe qBH2 → BH4 reduction; 2024 review reiterates this as the core QDPR reaction (varughese1992crystalstructureof pages 1-2, tai2024dopaminesynthesisand pages 4-5, breuer2018characterizingthefunction pages 15-19) | 1992, 2024 | https://doi.org/10.1073/pnas.89.13.6080; https://doi.org/10.1042/bst20231061 |
| Substrates and products | Physiological substrate is quinonoid dihydrobiopterin; product is BH4. In pathway context, BH4 is oxidized during PAH/TH/TPH reactions, converted via PCD to qBH2, then recycled by DHPR. | BH4 recycling pathway described in detail: BH4 oxidation during hydroxylation, PCD conversion to qBH2, then DHPR-mediated regeneration (breuer2018characterizingthefunction pages 15-19) | 2018 | https://doi.org/10.11588/heidok.00024357 |
| Cofactor preference | NADH is the best-supported cofactor and is directly observed in the rat crystal structure; older biochemical work indicates NADH is more effective than NADPH in vitro, though NADPH activity may occur under some conditions. | NADH bound in rat DHPR crystal; hydride transfer from NADH described. Rat biochemical dissertation reports NADH more effective than NADPH in vitro (varughese1992crystalstructureof pages 2-4, cutler1986dihydropteridinereductase pages 58-64) | 1992, 1986 | https://doi.org/10.1073/pnas.89.13.6080; https://doi.org/10.48780/publications.aston.ac.uk.00014506 |
| Catalytic mechanism / stereochemistry | DHPR is a B-stereospecific dehydrogenase; the enzyme transfers the pro-S hydrogen of NADH to N5 of qBH2. | Explicit mechanistic description from rat NADH-bound structure (varughese1992crystalstructureof pages 2-4) | 1992 | https://doi.org/10.1073/pnas.89.13.6080 |
| Oligomeric state and size | Rat DHPR is a dimeric enzyme with subunits of about 25–26 kDa; the intact enzyme is about 50–52 kDa. | Rat biochemical work and human mutation review converge on dimeric organization and ~26 kDa subunits (cutler1986dihydropteridinereductase pages 58-64, smooker1995molecularbasisof pages 1-3, breuer2018characterizingthefunction pages 19-24) | 1986, 1995, 2018 | https://doi.org/10.48780/publications.aston.ac.uk.00014506; https://doi.org/10.1002/humu.1380050402; https://doi.org/10.11588/heidok.00024357 |
| Structural fold | Rat DHPR adopts an α/β architecture with a Rossmann-type dinucleotide-binding fold for NADH binding, consistent with its assignment to the dehydrogenase/reductase superfamily and compatible with the UniProt SDR-family annotation. | Rat crystal structure directly identifies a Rossmann-type fold for NADH binding (varughese1992crystalstructureof pages 1-2, varughese1992crystalstructureof pages 2-4) | 1992 | https://doi.org/10.1073/pnas.89.13.6080 |
| Dimer interface / active-site architecture | Dimerization is mediated by a four-helix bundle contributed by helices from each protomer; the active site lies in a U-shaped cleft near bound NADH. | Structural figures and text summarize four-helix dimer interface and active-site cleft in rat DHPR (varughese1992crystalstructureof pages 1-2, varughese1992crystalstructureof media 27840a6e, varughese1992crystalstructureof media a6c6b231) | 1992 | https://doi.org/10.1073/pnas.89.13.6080 |
| Core biochemical pathway | Qdpr functions in BH4 recycling, complementing BH4 de novo synthesis and maintaining reduced cofactor supply for PAH, TH, and TPH. This is the primary function most relevant for annotation. | BH4 pathway reviews and mechanistic summaries identify DHPR as the key regeneration enzyme supporting aromatic amino acid hydroxylases (breuer2018characterizingthefunction pages 15-19, breuer2018characterizingthefunction pages 19-24, tai2024dopaminesynthesisand pages 1-2, thony2000tetrahydrobiopterinbiosynthesisregeneration pages 12-13) | 2000, 2018, 2024 | https://doi.org/10.1042/bj3470001; https://doi.org/10.11588/heidok.00024357; https://doi.org/10.1042/bst20231061 |
| Biological role: phenylalanine metabolism | By regenerating BH4, DHPR supports phenylalanine hydroxylase (PAH) activity and thus phenylalanine-to-tyrosine metabolism; deficiency contributes to hyperphenylalaninemia. | Reviews connect QDPR loss to HPA/BH4 deficiency; zebrafish qdpra perturbation caused a PKU-like amino-acid pattern supporting conserved PAH-coupled function (breuer2018characterizingthefunction pages 100-103, breuer2018characterizingthefunction pages 19-24, ghanei2023acomprehensivestudy pages 1-2) | 2018, 2023 | https://doi.org/10.11588/heidok.00024357; https://doi.org/10.1159/000529037 |
| Biological role: monoamine synthesis | DHPR indirectly supports dopamine and serotonin synthesis because TH and TPH require BH4; loss of QDPR reduces monoamine biosynthetic capacity and is linked to neurological disease. | 2024 dopamine review places DHPR among key proteins for DA synthesis; BH4 dependence of TH/TPH described in pathway reviews (tai2024dopaminesynthesisand pages 4-5, breuer2018characterizingthefunction pages 15-19, tai2024dopaminesynthesisand pages 1-2, thony2000tetrahydrobiopterinbiosynthesisregeneration pages 12-13) | 2000, 2024 | https://doi.org/10.1042/bj3470001; https://doi.org/10.1042/bst20231061 |
| Biological role: nitric oxide synthase | BH4 regenerated by DHPR is also required for nitric oxide synthase (NOS) activity; thus Qdpr contributes indirectly to NO production and BH4/BH2 redox balance relevant to NOS coupling. | BH4 dependence of NOS is described in BH4 pathway summaries and DHPR-centered reviews (breuer2018characterizingthefunction pages 15-19, lucock2025folatebiopterincrosstalkin pages 2-3, breuer2018characterizingthefunction pages 19-24) | 2018, 2025 | https://doi.org/10.11588/heidok.00024357; https://doi.org/10.14218/erhm.2025.00020 |
| Tissue distribution | DHPR is widely distributed in animal tissues and is present in brain and adrenal medulla in systems using tyrosine and tryptophan hydroxylation; rat liver has been the classical structural/biochemical source. | Biochemical Journal review notes broad tissue distribution including brain/adrenal medulla; rat liver enzyme provided the crystal structure (varughese1992crystalstructureof pages 1-2, thony2000tetrahydrobiopterinbiosynthesisregeneration pages 12-13) | 1992, 2000 | https://doi.org/10.1073/pnas.89.13.6080; https://doi.org/10.1042/bj3470001 |
| Subcellular localization | Evidence supports a predominantly cytosolic role consistent with soluble BH4 recycling and soluble aromatic amino acid hydroxylase systems; wild-type QDPR has been reported mainly in the cytoplasm in cell experiments. | Cytosolic pathway context in reviews plus direct report of mainly cytoplasmic localization for wild-type QDPR in cell assays (si2017a278cmutationof pages 5-6, breuer2018characterizingthefunction pages 15-19) | 2017, 2018 | https://doi.org/10.1093/abbs/gmx061; https://doi.org/10.11588/heidok.00024357 |
| Localization caveat | Some newer systems-level studies suggest broader or cell-type-specific roles (e.g., glial enrichment in vertebrate nervous systems), but these are not yet definitive for rat Qdpr primary annotation. | Zebrafish/comparative work links DHPR strongly to glial expression; this is suggestive rather than conclusive for rat (breuer2018characterizingthefunction pages 106-108) | 2018 | https://doi.org/10.11588/heidok.00024357 |
| Recent 2024 expert view | A 2024 expert review of dopamine synthesis/therapeutics identifies DHPR/QDPR as a key enzyme in BH4 regeneration for neurotransmitter synthesis and discusses its relevance to inherited monoamine disorders and parkinsonism. | Review states DHPR catalyzes qBH2 reduction to BH4 using NADH and places QDPR among disorders affecting DA synthesis (tai2024dopaminesynthesisand pages 4-5, tai2024dopaminesynthesisand pages 1-2) | 2024 | https://doi.org/10.1042/bst20231061 |
| Recent 2024 disease statistics | The 2024 review reports that DHPR defects account for ~33% of BH4 deficiency cases and cites ~303 reported patients, emphasizing strong clinical relevance despite rarity. | Explicit numerical summary from 2024 review (tai2024dopaminesynthesisand pages 4-5) | 2024 | https://doi.org/10.1042/bst20231061 |
| Recent 2024 model systems | A 2024 review of inherited monoamine-disorder mouse models lists Dpr-ko among available BH4-pathway models, underscoring current use of DHPR-deficient animals for mechanistic and therapeutic studies. | Mouse-model review names Dpr-ko as a DHPR-deficiency model within BH4-pathway disease research (thony2024mousemodelsfor pages 8-9) | 2024 | https://doi.org/10.1002/jimd.12710 |
| Recent 2023 human genetics / implementation | A 2023 systematic review of Iranian HPA patients found 29 distinct QDPR disease-causing variants, including 17 novel variants; 18 QDPR variants were proposed for diagnostic panels capturing >75% of documented disease-causing variants in that population. | Sequencing-based systematic review provides concrete variant counts and panel rationale for real-world genetic testing implementation (ghanei2023acomprehensivestudy pages 1-1, ghanei2023acomprehensivestudy pages 2-3, ghanei2023acomprehensivestudy pages 1-2) | 2023 | https://doi.org/10.1159/000529037 |
| Recent 2023 cohort statistics | In the same review, only 3 studies specifically assessed QDPR, covering 50 individuals with QDPR deficiency; this indicates limited but clinically meaningful evidence for QDPR-specific mutational spectra. | QDPR-specific evidence base summarized quantitatively (ghanei2023acomprehensivestudy pages 4-5, ghanei2023acomprehensivestudy pages 2-3) | 2023 | https://doi.org/10.1159/000529037 |
| Functional-annotation takeaway | For rat Qdpr/P11348, the most defensible primary annotation is a cytosolic, dimeric, NADH-dependent BH4-recycling oxidoreductase that regenerates BH4 for PAH/TH/TPH and thereby supports phenylalanine metabolism, monoamine biosynthesis, and NOS-related BH4 homeostasis. | This synthesis is supported by rat structural data, classic BH4 reviews, and recent 2024 disease-focused reviews (varughese1992crystalstructureof pages 1-2, varughese1992crystalstructureof pages 2-4, tai2024dopaminesynthesisand pages 4-5, thony2000tetrahydrobiopterinbiosynthesisregeneration pages 12-13) | 1992, 2000, 2024 | https://doi.org/10.1073/pnas.89.13.6080; https://doi.org/10.1042/bj3470001; https://doi.org/10.1042/bst20231061 |
Table: This table summarizes the strongest evidence supporting functional annotation of rat Qdpr/DHPR (UniProt P11348), including reaction chemistry, structural biology, pathway roles, localization, and recent clinical/genetic developments from 2023-2024.
Structural images from the rat DHPR crystal structure illustrate the four-helix dimer interface and the NADH-adjacent active-site cleft used to rationalize substrate binding.
(varughese1992crystalstructureof media 27840a6e, varughese1992crystalstructureof media a6c6b231)
References
(varughese1992crystalstructureof pages 1-2): K. Varughese, Matthew M. Skinner, John M. WHITELEYt, David A. MATrHEWS, and N. Xuong. Crystal structure of rat liver dihydropteridine reductase. Proceedings of the National Academy of Sciences of the United States of America, 89 13:6080-4, Jul 1992. URL: https://doi.org/10.1073/pnas.89.13.6080, doi:10.1073/pnas.89.13.6080. This article has 210 citations and is from a highest quality peer-reviewed journal.
(varughese1992crystalstructureof pages 2-4): K. Varughese, Matthew M. Skinner, John M. WHITELEYt, David A. MATrHEWS, and N. Xuong. Crystal structure of rat liver dihydropteridine reductase. Proceedings of the National Academy of Sciences of the United States of America, 89 13:6080-4, Jul 1992. URL: https://doi.org/10.1073/pnas.89.13.6080, doi:10.1073/pnas.89.13.6080. This article has 210 citations and is from a highest quality peer-reviewed journal.
(tai2024dopaminesynthesisand pages 4-5): Mary Dayne Sia Tai, Gloria Gamiz-Arco, and Aurora Martinez. Dopamine synthesis and transport: current and novel therapeutics for parkinsonisms. Biochemical Society Transactions, 52:1275-1291, May 2024. URL: https://doi.org/10.1042/bst20231061, doi:10.1042/bst20231061. This article has 16 citations and is from a peer-reviewed journal.
(thony2000tetrahydrobiopterinbiosynthesisregeneration pages 12-13): Beat THÖNY, Günter AUERBACH, and Nenad BLAU. Tetrahydrobiopterin biosynthesis, regeneration and functions. The Biochemical journal, 347 Pt 1:1-16, Apr 2000. URL: https://doi.org/10.1042/bj3470001, doi:10.1042/bj3470001. This article has 1113 citations.
(breuer2018characterizingthefunction pages 15-19): Maximilian Breuer. Characterizing the function and role of three dihydropteridine reductase homologs qdpra, qdprb1 and qdprb2 in the embryonic development of danio rerio. Text, Jan 2018. URL: https://doi.org/10.11588/heidok.00024357, doi:10.11588/heidok.00024357. This article has 0 citations and is from a peer-reviewed journal.
(cutler1986dihydropteridinereductase pages 58-64): Dihydropteridine reductase This article has 1 citations.
(varughese1992crystalstructureof media 27840a6e): K. Varughese, Matthew M. Skinner, John M. WHITELEYt, David A. MATrHEWS, and N. Xuong. Crystal structure of rat liver dihydropteridine reductase. Proceedings of the National Academy of Sciences of the United States of America, 89 13:6080-4, Jul 1992. URL: https://doi.org/10.1073/pnas.89.13.6080, doi:10.1073/pnas.89.13.6080. This article has 210 citations and is from a highest quality peer-reviewed journal.
(varughese1992crystalstructureof media a6c6b231): K. Varughese, Matthew M. Skinner, John M. WHITELEYt, David A. MATrHEWS, and N. Xuong. Crystal structure of rat liver dihydropteridine reductase. Proceedings of the National Academy of Sciences of the United States of America, 89 13:6080-4, Jul 1992. URL: https://doi.org/10.1073/pnas.89.13.6080, doi:10.1073/pnas.89.13.6080. This article has 210 citations and is from a highest quality peer-reviewed journal.
(smooker1995molecularbasisof pages 1-3): Peter M. Smooker and Richard G. H. Cotton. Molecular basis of dihydropteridine reductase deficiency. Human Mutation, 5:279-284, Jan 1995. URL: https://doi.org/10.1002/humu.1380050402, doi:10.1002/humu.1380050402. This article has 27 citations and is from a domain leading peer-reviewed journal.
(breuer2018characterizingthefunction pages 19-24): Maximilian Breuer. Characterizing the function and role of three dihydropteridine reductase homologs qdpra, qdprb1 and qdprb2 in the embryonic development of danio rerio. Text, Jan 2018. URL: https://doi.org/10.11588/heidok.00024357, doi:10.11588/heidok.00024357. This article has 0 citations and is from a peer-reviewed journal.
(ghanei2023acomprehensivestudy pages 1-2): Mahmoud Ghanei, Seyedeh Helia Sadat Fatemi, and Tayebeh Hamzehlouei. A comprehensive study of disease-causing variants in pah, qdpr, pts, and pcd genes in iranian patients with hyperphenylalaninemia: a systematic review. Human Heredity, 88:8-17, Jan 2023. URL: https://doi.org/10.1159/000529037, doi:10.1159/000529037. This article has 3 citations and is from a peer-reviewed journal.
(tai2024dopaminesynthesisand pages 1-2): Mary Dayne Sia Tai, Gloria Gamiz-Arco, and Aurora Martinez. Dopamine synthesis and transport: current and novel therapeutics for parkinsonisms. Biochemical Society Transactions, 52:1275-1291, May 2024. URL: https://doi.org/10.1042/bst20231061, doi:10.1042/bst20231061. This article has 16 citations and is from a peer-reviewed journal.
(si2017a278cmutationof pages 5-6): Qin Si, Sifan Sun, and Yanting Gu. A278c mutation of dihydropteridine reductase decreases autophagy via mtor signaling. Acta Biochimica et Biophysica Sinica, 49:706–712, Aug 2017. URL: https://doi.org/10.1093/abbs/gmx061, doi:10.1093/abbs/gmx061. This article has 16 citations and is from a peer-reviewed journal.
(breuer2018characterizingthefunction pages 106-108): Maximilian Breuer. Characterizing the function and role of three dihydropteridine reductase homologs qdpra, qdprb1 and qdprb2 in the embryonic development of danio rerio. Text, Jan 2018. URL: https://doi.org/10.11588/heidok.00024357, doi:10.11588/heidok.00024357. This article has 0 citations and is from a peer-reviewed journal.
(thony2024mousemodelsfor pages 8-9): Beat Thöny, Joanne Ng, Manju A. Kurian, Philippa Mills, and Aurora Martinez. Mouse models for inherited monoamine neurotransmitter disorders. Journal of Inherited Metabolic Disease, 47:533-550, Jan 2024. URL: https://doi.org/10.1002/jimd.12710, doi:10.1002/jimd.12710. This article has 9 citations and is from a peer-reviewed journal.
(ghanei2023acomprehensivestudy pages 1-1): Mahmoud Ghanei, Seyedeh Helia Sadat Fatemi, and Tayebeh Hamzehlouei. A comprehensive study of disease-causing variants in pah, qdpr, pts, and pcd genes in iranian patients with hyperphenylalaninemia: a systematic review. Human Heredity, 88:8-17, Jan 2023. URL: https://doi.org/10.1159/000529037, doi:10.1159/000529037. This article has 3 citations and is from a peer-reviewed journal.
(ghanei2023acomprehensivestudy pages 2-3): Mahmoud Ghanei, Seyedeh Helia Sadat Fatemi, and Tayebeh Hamzehlouei. A comprehensive study of disease-causing variants in pah, qdpr, pts, and pcd genes in iranian patients with hyperphenylalaninemia: a systematic review. Human Heredity, 88:8-17, Jan 2023. URL: https://doi.org/10.1159/000529037, doi:10.1159/000529037. This article has 3 citations and is from a peer-reviewed journal.
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