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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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 gene symbol dcxr is consistent with the supplied protein description, dicarbonyl/L-xylulose reductase, in zebrafish (Danio rerio, formerly Brachydanio rerio). Its supplied InterPro/Pfam assignments—L-xylulose/carbonyl reductase, NAD(P)-binding fold, SDR-family signature, and adh_short_C2—are mutually consistent with membership in the short-chain dehydrogenase/reductase (SDR) superfamily.
However, the literature is limited for this specific protein, Q567K5. Searches of the exact accession, gene–organism combination, and protein name found no dedicated zebrafish biochemical, localization, knockout, or phenotype study and no target-specific 2023–2024 publication. Accordingly, the defensible annotation is:
Q567K5 is predicted to be an intracellular NAD(P)H-dependent SDR that reduces L-xylulose to xylitol in the uronate cycle and probably reduces selected α-dicarbonyl compounds. This assignment is strongly supported by family/domain conservation and experiments on bona fide mammalian and nematode DCXR orthologs, but it has not been directly demonstrated for purified zebrafish Q567K5.
No results for DHRS2, DHRS4, CBR1, CBR2, CBR3, or unrelated carbonyl reductases have been treated as direct evidence for zebrafish dcxr.
| Topic | Best-supported annotation | Evidence species/source | Evidence level for zebrafish | Key caveat |
|---|---|---|---|---|
| Identity and domains | dcxr, UniProt Q567K5, from Danio rerio; annotated dicarbonyl/L-xylulose reductase in the SDR family, with L-xylulose/carbonyl-reductase, NAD(P)-binding, SDR-family, and short-chain dehydrogenase/reductase signatures | User-supplied UniProt annotation | Database-supported identity | Protein name is submitted or inferred; no Q567K5-specific biochemical publication was found |
| Primary reaction | Predicted to catalyze L-xylulose + NADPH + H⁺ → xylitol + NADP⁺ | Mammalian DCXR and C. elegans ortholog evidence (kisiela2011bioinformaticandbiochemical pages 2-3, ebert2015humandcxr– pages 5-7, ebert2015humandcxr– pages 2-3) | Strong orthology/domain-based inference; not directly tested | NADPH dependence is established in orthologs, but Q567K5 kinetics and in-vivo directionality are unknown |
| α-Dicarbonyl reduction | Likely reduces α-dicarbonyls; human DCXR directly reduces diacetyl to acetoin and also accepts methylglyoxal, 3,4-hexanedione, 2,3-heptanedione, and 1-phenyl-1,2-propanedione (yang2017diacetyllxylulosereductasemediates pages 3-5, yang2017diacetyllxylulosereductasemediates pages 1-3, yang2017diacetyllxylulosereductasemediates pages 5-6, nakagawa2002molecularcharacterizationof pages 4-5) | Recombinant human and other mammalian DCXR | Moderate-to-strong ortholog-based inference | Substrate efficiencies vary substantially among mammalian species, so the zebrafish substrate spectrum cannot be assumed quantitatively (ebert2015humandcxr– pages 5-7, ebert2015humandcxr– pages 2-3) |
| Cofactor specificity | Predicted pyridine-nucleotide-dependent reductase, probably favoring NADPH physiologically; human assays support both NADPH and NADH, with assay-dependent greater NADH activity (kisiela2011bioinformaticandbiochemical pages 2-3, yang2017diacetyllxylulosereductasemediates pages 8-10, yang2017diacetyllxylulosereductasemediates pages 5-6) | Human DCXR and C. elegans ortholog | Inference; preference unresolved in zebrafish | Ortholog results differ: C. elegans activity was NADPH-specific, whereas one human study found greater NADH-supported activity under its assay conditions |
| SDR architecture and oligomerization | Expected classical SDR fold with a glycine-rich cofactor-binding motif and conserved Ser–Tyr–Lys catalytic machinery; mammalian DCXR forms an approximately 100-kDa homotetramer of approximately 26-kDa subunits (yang2017diacetyllxylulosereductasemediates pages 8-10, kisiela2011bioinformaticandbiochemical pages 1-2, nakagawa2002molecularcharacterizationof pages 4-5, ebert2015humandcxr– pages 3-4) | Human and rodent structural and biochemical studies | Strong family-based structural inference | Motif conservation and tetramerization require direct verification using the Q567K5 sequence and purified zebrafish protein |
| Biochemical pathway | Predicted terminal reductive step of the uronate cycle, converting L-xylulose to xylitol and connecting glucuronate or pentose metabolism with central carbohydrate metabolism (kisiela2011bioinformaticandbiochemical pages 2-3, ebert2015humandcxr– pages 5-7) | Human, other mammalian, and C. elegans DCXR literature | Strong ortholog-based pathway inference | Urate-cycle flux and physiological importance have not been measured in zebrafish dcxr mutants or tissues |
| Cellular localization | Most defensible prediction is an intracellular NAD(P)-dependent enzyme, plausibly cytosolic or associated with intracellular membranes; mammalian DCXR occurs in cytosolic and mitochondrial fractions and at proximal-tubule inner membranes (ebert2015humandcxr– pages 5-7, ebert2015humandcxr– pages 4-5) | Human liver and murine kidney | Low-to-moderate inference | No direct zebrafish immunolocalization, fractionation, or tagged-protein study was found; mammalian sperm-surface and secreted localization cannot be transferred automatically |
| Tissue expression | Zebrafish tissue distribution is unresolved; mammalian DCXR is abundant in kidney, liver, lung, and epididymis, with strong renal and hepatic expression (yang2017diacetyllxylulosereductasemediates pages 1-3, ebert2015humandcxr– pages 5-7) | Human and rodent tissues | No direct zebrafish evidence found | Mammalian expression cannot establish zebrafish tissue specificity; zebrafish RNA-seq, in-situ hybridization, or targeted proteomics needs independent validation |
| Carbonyl detoxification | Likely reduces reactive α-dicarbonyls to less electrophilic hydroxycarbonyl or alcohol products and may limit carbonyl stress or AGE-precursor accumulation (yang2017diacetyllxylulosereductasemediates pages 1-3, kisiela2011bioinformaticandbiochemical pages 1-2, ebert2015humandcxr– pages 5-7) | Human, mouse, rat, and comparative SDR evidence | Moderate functional inference | Whether this is a major zebrafish role, and which endogenous dicarbonyl is dominant, remain untested |
| Moonlighting roles | Mammalian DCXR/P34H has proposed nonenzymatic roles in sperm maturation, sperm–zona-pellucida interaction, and cell adhesion (ebert2015humandcxr– pages 1-2, ebert2015humandcxr– pages 3-4, ebert2015humandcxr– pages 2-3) | Primarily human and other mammalian reproductive or cell studies | Unsupported for zebrafish | These lineage- and tissue-specific functions should not be assigned to Q567K5 without zebrafish expression, localization, interaction, and loss-of-function evidence |
| Overall evidence status | Best current annotation is a conserved SDR dicarbonyl/L-xylulose reductase functioning in L-xylulose metabolism and potentially carbonyl detoxification | UniProt identity plus mammalian and C. elegans ortholog studies | No direct zebrafish biochemical, localization, or phenotype study found | Reaction, substrates, compartment, tissue distribution, oligomeric state, and organismal phenotype all require Q567K5-specific experimental confirmation |
Table: Evidence-grade functional annotation of Danio rerio dcxr/Q567K5, separating database-supported identity from orthology-based biochemical inference. It highlights the absence of direct zebrafish biochemical, localization, and phenotype studies.
The supplied record identifies:
This identity is biologically coherent. Bona fide mammalian DCXR is also designated SDR20C1/L-xylulose reductase and belongs to the SDR superfamily; importantly, the literature warns that the historical label “human carbonyl reductase 2” is misleading because DCXR is distinct from the other carbonyl-reductase families (Ebert et al., February 2015; DOI 10.1111/brv.12108). (ebert2015humandcxr– pages 3-4)
The supplied NAD(P)-binding and SDR annotations also agree with experimentally characterized mammalian DCXR. Mammalian proteins contain an N-terminal glycine-rich SDR cofactor-binding sequence, a conserved Tyr–Lys motif, and catalytic residues including Ser136, Tyr149, and Lys153 in the human numbering used by structural studies. Arg39 contributes to recognition of the 2′-phosphate of NADP(H). (yang2017diacetyllxylulosereductasemediates pages 8-10, nakagawa2002molecularcharacterizationof pages 4-5)
The symbol itself is not problematic when constrained by Q567K5 + Danio rerio. The problem is instead evidence scarcity: most mechanistic literature concerns human or rodent DCXR, with some comparative work in Caenorhabditis elegans. SDR proteins can retain similar folds despite low pairwise sequence identity, so family assignment supports—but does not prove—identical substrate specificity. (kisiela2011bioinformaticandbiochemical pages 1-2, kisiela2011bioinformaticandbiochemical pages 3-6)
The canonical DCXR reaction is:
L-xylulose + NADPH + H⁺ ⇌ xylitol + NADP⁺
DCXR is therefore an oxidoreductase acting on a sugar carbonyl. Mammalian and C. elegans literature places this reaction in the uronate cycle and describes it as NADPH-dependent. (kisiela2011bioinformaticandbiochemical pages 2-3, ebert2015humandcxr– pages 5-7)
For zebrafish Q567K5, this reaction should be regarded as a strong orthology- and domain-based prediction, not a directly measured activity. Neither zebrafish enzyme kinetics nor in-vivo isotopic flux through this reaction was located.
Mammalian DCXR also reduces α-dicarbonyl compounds. The clearest model reaction is:
Diacetyl + NAD(P)H + H⁺ → acetoin + NAD(P)⁺
Recombinant human DCXR directly produced acetoin from diacetyl. Other reported human substrates include methylglyoxal, 3,4-hexanedione, 2,3-heptanedione, and 1-phenyl-1,2-propanedione. (yang2017diacetyllxylulosereductasemediates pages 3-5, yang2017diacetyllxylulosereductasemediates pages 1-3, yang2017diacetyllxylulosereductasemediates pages 5-6)
Earlier mammalian characterization found activity toward diacetyl, 3,4-hexanedione, and other aliphatic or alicyclic α-dicarbonyls, but little or no activity toward tested monocarbonyl compounds. This indicates preference for appropriately spaced paired carbonyl groups rather than unrestricted aldehyde/ketone reduction. (nakagawa2002molecularcharacterizationof pages 4-5, ebert2015humandcxr– pages 2-3)
Substrate transfer to zebrafish must remain qualitative. Mammalian orthologs differ markedly in catalytic efficiency: for diacetyl at pH 6.0, reported specific activities were 0.29, 11, 0.95, 16, and 5.4 U/mg for mouse, rat, human, hamster, and guinea-pig enzymes, respectively. Thus, even close vertebrate orthologs cannot be assumed to have the same substrate ranking or rate. (nakagawa2002molecularcharacterizationof pages 4-5)
The most conservative annotation is NAD(P)H-dependent, probably NADPH-preferring under physiological conditions. Mammalian cloning studies and uronate-cycle assignments emphasize NADPH. A characterized C. elegans DCXR ortholog consumed NADPH, while NADH-supported activity was not detected. (ebert2015humandcxr– pages 2-3, kisiela2011bioinformaticandbiochemical pages 2-3)
A later recombinant-human study found that both NADH and NADPH supported L-xylulose and diacetyl reduction and that NADH was more effective under its assay conditions. This does not establish NADH as the universal in-vivo cofactor; it demonstrates assay- and species-dependent cofactor utilization. Zebrafish cofactor preference therefore remains experimentally unresolved. (yang2017diacetyllxylulosereductasemediates pages 8-10, yang2017diacetyllxylulosereductasemediates pages 5-6)
Human recombinant DCXR reduces L-xylulose with a reported Km of 0.21 mM and kcat/Km of 3.1 s⁻¹ mM⁻¹. Guinea-pig DCXR reached approximately 740 s⁻¹ mM⁻¹, again illustrating major species differences. (ebert2015humandcxr– pages 5-7)
The broader mammalian evidence supports three substrate classes:
For Q567K5, only the first two should be included in a primary functional annotation. Quinone redox cycling is a mechanistic property demonstrated for human DCXR and may generate superoxide and hydrogen peroxide, but its physiological significance—and its occurrence in zebrafish—are uncertain. (yang2017diacetyllxylulosereductasemediates pages 1-3, yang2017diacetyllxylulosereductasemediates pages 14-17)
Mammalian DCXR is a homotetramer, approximately 100 kDa in total, assembled from roughly 26–28-kDa SDR subunits. Each human subunit binds one NADP⁺. (yang2017diacetyllxylulosereductasemediates pages 8-10, nakagawa2002molecularcharacterizationof pages 4-5, ebert2015humandcxr– pages 3-4)
The proposed catalytic architecture is the canonical SDR arrangement:
Docking of human DCXR placed L-xylulose and diacetyl near NADP⁺ and the catalytic Tyr149. (yang2017diacetyllxylulosereductasemediates pages 8-10)
Human DCXR also contains redox-sensitive Cys138 and Cys150. Oxidation-induced disulfide formation reduced catalytic efficiency approximately threefold, while S-cysteinylation reduced activity approximately tenfold; reducing agents reversed the disulfide modification. This suggests that DCXR activity may itself be regulated by cellular redox conditions. This observation has not been tested in zebrafish Q567K5. (ebert2015humandcxr– pages 3-4)
The strongest pathway assignment is the uronate cycle, an alternative route of glucose and glucuronate metabolism. DCXR performs the L-xylulose-to-xylitol step. The pathway has been estimated to account for approximately 5% of daily glucose utilization in humans, although that statistic cannot be extrapolated quantitatively to zebrafish. (ebert2015humandcxr– pages 5-7)
In humans, loss of functional L-xylulose reductase causes essential pentosuria, characterized by accumulation and urinary excretion of L-xylulose. This human genetic evidence strongly validates the enzyme–reaction relationship but does not establish a zebrafish disease or phenotype. (ebert2015humandcxr– pages 1-2, ebert2015humandcxr– pages 2-3)
SDR carbonyl reductases convert electrophilic aldehydes and ketones into generally less reactive, more water-soluble alcohol or hydroxycarbonyl products. Mammalian DCXR has consequently been proposed to limit α-dicarbonyl/carbonyl stress and accumulation of advanced-glycation-end-product precursors. Mouse and rat evidence links DCXR-related activity to reactive-dicarbonyl clearance in kidney. (kisiela2011bioinformaticandbiochemical pages 1-2, ebert2015humandcxr– pages 5-7)
For zebrafish, a role in carbonyl homeostasis is plausible, but the physiologically dominant substrate is unknown. Demonstrating this role would require Q567K5 loss of function followed by targeted measurement of L-xylulose, xylitol, methylglyoxal, diacetyl-related metabolites, and AGE precursors.
DCXR is primarily a metabolic enzyme, not a canonical receptor, kinase, transcription factor, or signaling adaptor. No direct zebrafish signaling pathway was identified. Any effects on oxidative-stress signaling would probably be secondary to altered NAD(P)H balance, dicarbonyl burden, protein glycation, or quinone redox cycling rather than direct signal transduction.
No direct zebrafish immunolocalization, cell fractionation, proximity-labeling, or fluorescent-tag study was found. The most defensible prediction is therefore intracellular localization, likely cytosolic and/or associated with intracellular membranes, where NAD(P)H and soluble carbonyl substrates are available.
Human liver DCXR has been reported in both mitochondrial and cytosolic fractions, with a minor isoform limited to the cytosol. Mammalian DCXR also has a predicted membrane-associated region, but prediction alone does not establish transmembrane topology. (ebert2015humandcxr– pages 5-7, ebert2015humandcxr– pages 4-5)
In mouse kidney, DCXR was localized primarily to inner membranes of proximal renal tubules. Human and rodent DCXR expression is high in kidney and liver, while human studies also report abundance in lung and epididymis. (yang2017diacetyllxylulosereductasemediates pages 1-3, ebert2015humandcxr– pages 5-7)
These findings make renal/hepatic and intracellular-membrane expression reasonable hypotheses for zebrafish, not annotations that should be asserted without zebrafish RNA in-situ hybridization, single-cell transcriptomics, or protein-level validation.
Human DCXR is also known as sperm-surface protein P34H. Reviews have proposed functions in epididymal sperm maturation, sperm–zona-pellucida interaction, fertilization, and cell adhesion. This has led to the description of DCXR as a possible “moonlighting protein,” combining enzymatic and non-catalytic interaction functions. (ebert2015humandcxr– pages 1-2, ebert2015humandcxr– pages 3-4)
These claims must not be transferred to zebrafish Q567K5. They involve mammalian reproductive anatomy, epididymal maturation, and lineage-specific protein localization. Even in mammalian systems, the cell-adhesion and tumor-dissemination interpretations remain less secure than the enzyme activity. (ebert2015humandcxr– pages 2-3)
No 2023–2024 publication directly characterizing zebrafish Q567K5 was identified. This absence is itself important: the current annotation remains driven by curated sequence/domain information and older, high-quality ortholog studies rather than recent target-specific experiments.
Current practical uses of DCXR knowledge are predominantly outside zebrafish:
High confidence
Moderate confidence
Low confidence or unestablished
The most informative validation program would be:
Recommended functional annotation: “Predicted NAD(P)H-dependent dicarbonyl/L-xylulose reductase of the SDR family; likely catalyzes reduction of L-xylulose to xylitol in the uronate cycle and may reduce reactive α-dicarbonyl compounds.”
The qualifier “predicted” is essential: direct experimental evidence for the exact zebrafish protein Q567K5, its cellular location, substrate specificity, and organismal function was not found.
References
(kisiela2011bioinformaticandbiochemical pages 2-3): Michael Kisiela, Yasser El-Hawari, Hans-Jörg Martin, and Edmund Maser. Bioinformatic and biochemical characterization of dcxr and dhrs2/4 from caenorhabditis elegans. Chemico-biological interactions, 191 1-3:75-82, May 2011. URL: https://doi.org/10.1016/j.cbi.2011.01.034, doi:10.1016/j.cbi.2011.01.034. This article has 22 citations and is from a peer-reviewed journal.
(ebert2015humandcxr– pages 5-7): Bettina Ebert, Michael Kisiela, and Edmund Maser. Human dcxr – another ‘moonlighting protein’ involved in sugar metabolism, carbonyl detoxification, cell adhesion and male fertility? Biological Reviews, 90:254-278, Feb 2015. URL: https://doi.org/10.1111/brv.12108, doi:10.1111/brv.12108. This article has 56 citations and is from a domain leading peer-reviewed journal.
(ebert2015humandcxr– pages 2-3): Bettina Ebert, Michael Kisiela, and Edmund Maser. Human dcxr – another ‘moonlighting protein’ involved in sugar metabolism, carbonyl detoxification, cell adhesion and male fertility? Biological Reviews, 90:254-278, Feb 2015. URL: https://doi.org/10.1111/brv.12108, doi:10.1111/brv.12108. This article has 56 citations and is from a domain leading peer-reviewed journal.
(yang2017diacetyllxylulosereductasemediates pages 3-5): Shaojun Yang, Yi-Hua Jan, Vladimir Mishin, Diane E. Heck, Debra L. Laskin, and Jeffrey D. Laskin. Diacetyl/l-xylulose reductase mediates chemical redox cycling in lung epithelial cells. Chemical research in toxicology, 30 7:1406-1418, Jun 2017. URL: https://doi.org/10.1021/acs.chemrestox.7b00052, doi:10.1021/acs.chemrestox.7b00052. This article has 31 citations and is from a domain leading peer-reviewed journal.
(yang2017diacetyllxylulosereductasemediates pages 1-3): Shaojun Yang, Yi-Hua Jan, Vladimir Mishin, Diane E. Heck, Debra L. Laskin, and Jeffrey D. Laskin. Diacetyl/l-xylulose reductase mediates chemical redox cycling in lung epithelial cells. Chemical research in toxicology, 30 7:1406-1418, Jun 2017. URL: https://doi.org/10.1021/acs.chemrestox.7b00052, doi:10.1021/acs.chemrestox.7b00052. This article has 31 citations and is from a domain leading peer-reviewed journal.
(yang2017diacetyllxylulosereductasemediates pages 5-6): Shaojun Yang, Yi-Hua Jan, Vladimir Mishin, Diane E. Heck, Debra L. Laskin, and Jeffrey D. Laskin. Diacetyl/l-xylulose reductase mediates chemical redox cycling in lung epithelial cells. Chemical research in toxicology, 30 7:1406-1418, Jun 2017. URL: https://doi.org/10.1021/acs.chemrestox.7b00052, doi:10.1021/acs.chemrestox.7b00052. This article has 31 citations and is from a domain leading peer-reviewed journal.
(nakagawa2002molecularcharacterizationof pages 4-5): Junichi Nakagawa, Syuhei Ishikura, Jun Asami, Tomoya Isaji, Noriyuki Usami, Akira Hara, Takanobu Sakurai, Katsuki Tsuritani, Koji Oda, Masayoshi Takahashi, Makoto Yoshimoto, Noboru Otsuka, and Kunihiro Kitamura. Molecular characterization of mammalian dicarbonyl/l-xylulose reductase and its localization in kidney*. The Journal of Biological Chemistry, 277:17883-17891, May 2002. URL: https://doi.org/10.1074/jbc.m110703200, doi:10.1074/jbc.m110703200. This article has 127 citations.
(yang2017diacetyllxylulosereductasemediates pages 8-10): Shaojun Yang, Yi-Hua Jan, Vladimir Mishin, Diane E. Heck, Debra L. Laskin, and Jeffrey D. Laskin. Diacetyl/l-xylulose reductase mediates chemical redox cycling in lung epithelial cells. Chemical research in toxicology, 30 7:1406-1418, Jun 2017. URL: https://doi.org/10.1021/acs.chemrestox.7b00052, doi:10.1021/acs.chemrestox.7b00052. This article has 31 citations and is from a domain leading peer-reviewed journal.
(kisiela2011bioinformaticandbiochemical pages 1-2): Michael Kisiela, Yasser El-Hawari, Hans-Jörg Martin, and Edmund Maser. Bioinformatic and biochemical characterization of dcxr and dhrs2/4 from caenorhabditis elegans. Chemico-biological interactions, 191 1-3:75-82, May 2011. URL: https://doi.org/10.1016/j.cbi.2011.01.034, doi:10.1016/j.cbi.2011.01.034. This article has 22 citations and is from a peer-reviewed journal.
(ebert2015humandcxr– pages 3-4): Bettina Ebert, Michael Kisiela, and Edmund Maser. Human dcxr – another ‘moonlighting protein’ involved in sugar metabolism, carbonyl detoxification, cell adhesion and male fertility? Biological Reviews, 90:254-278, Feb 2015. URL: https://doi.org/10.1111/brv.12108, doi:10.1111/brv.12108. This article has 56 citations and is from a domain leading peer-reviewed journal.
(ebert2015humandcxr– pages 4-5): Bettina Ebert, Michael Kisiela, and Edmund Maser. Human dcxr – another ‘moonlighting protein’ involved in sugar metabolism, carbonyl detoxification, cell adhesion and male fertility? Biological Reviews, 90:254-278, Feb 2015. URL: https://doi.org/10.1111/brv.12108, doi:10.1111/brv.12108. This article has 56 citations and is from a domain leading peer-reviewed journal.
(ebert2015humandcxr– pages 1-2): Bettina Ebert, Michael Kisiela, and Edmund Maser. Human dcxr – another ‘moonlighting protein’ involved in sugar metabolism, carbonyl detoxification, cell adhesion and male fertility? Biological Reviews, 90:254-278, Feb 2015. URL: https://doi.org/10.1111/brv.12108, doi:10.1111/brv.12108. This article has 56 citations and is from a domain leading peer-reviewed journal.
(kisiela2011bioinformaticandbiochemical pages 3-6): Michael Kisiela, Yasser El-Hawari, Hans-Jörg Martin, and Edmund Maser. Bioinformatic and biochemical characterization of dcxr and dhrs2/4 from caenorhabditis elegans. Chemico-biological interactions, 191 1-3:75-82, May 2011. URL: https://doi.org/10.1016/j.cbi.2011.01.034, doi:10.1016/j.cbi.2011.01.034. This article has 22 citations and is from a peer-reviewed journal.
(yang2017diacetyllxylulosereductasemediates pages 14-17): Shaojun Yang, Yi-Hua Jan, Vladimir Mishin, Diane E. Heck, Debra L. Laskin, and Jeffrey D. Laskin. Diacetyl/l-xylulose reductase mediates chemical redox cycling in lung epithelial cells. Chemical research in toxicology, 30 7:1406-1418, Jun 2017. URL: https://doi.org/10.1021/acs.chemrestox.7b00052, doi:10.1021/acs.chemrestox.7b00052. This article has 31 citations and is from a domain leading peer-reviewed journal.