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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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 provided is UniProt I1H6U0, annotated as UDP-glucuronate decarboxylase / UDP-xylose synthase (UXS; EC 4.1.1.35) from Brachypodium distachyon, encoded by ORF BRADI_1g66227v3 (as supplied in the prompt). In the tool-retrieved literature corpus, no paper explicitly mentioning BRADI_1g66227v3 or UniProt I1H6U0 was found; therefore, gene-level conclusions for Brachypodium are necessarily inference-based, grounded in (i) conserved UXS biochemistry and (ii) strong functional genetics and cell-wall phenotypes from experimentally characterized plant UXS orthologs (principally Arabidopsis). This report clearly labels evidence-supported statements vs inference. (kuang2016roleofudpglucuronic pages 12-16, kuang2016roleofudpglucuronic pages 5-9)
Plant UXS (also called UDP-glucuronic acid decarboxylase) catalyzes the conversion of UDP-glucuronic acid (UDP-GlcA) → UDP-xylose (UDP-Xyl). (kuang2016roleofudpglucuronic pages 1-5, harper2002biosynthesisofudpxylose. pages 1-2, li2023comprehensiveanalysisof pages 9-12)
This reaction is described as an irreversible decarboxylation in plant studies. (kuang2016roleofudpglucuronic pages 1-5, kuang2016roleofudpglucuronic pages 5-9, li2023comprehensiveanalysisof pages 9-12)
Functional implication: UDP-Xyl is a key nucleotide-sugar donor used in biosynthesis of plant cell-wall polysaccharides (notably xylan/heteroxylan and xyloglucan) and is also relevant to glycosylation of plant metabolites and glycoproteins. (kuang2016roleofudpglucuronic pages 1-5, li2023comprehensiveanalysisof pages 9-12)
In the plant nucleotide-sugar network, UDP-Xyl is produced from UDP-GlcA by UXS and then consumed by Golgi-localized glycosyltransferases that build xylan and other glycans; UDP-Xyl supply is thus tightly coupled to cell-wall biosynthetic flux. (kuang2016roleofudpglucuronic pages 1-5, pattathil2005biosynthesisofudpxylose pages 8-10)
A key concept for interpreting UXS function is compartmentalization: production of UDP-Xyl can occur in different cellular compartments (cytosol vs Golgi/endomembrane system), and UDP-Xyl can be transported into the Golgi lumen by UDP-Xyl transporters (UXTs) for luminal glycosylation. (kuang2016roleofudpglucuronic pages 12-16, pattathil2005biosynthesisofudpxylose pages 8-10)
Experimentally studied plant UXS proteins carry a conserved GxxGxxG motif (described as ADP/NAD(P)-binding-related) and a conserved YxxxK motif; Kuang et al. further describe a Ser–Tyr–Lys catalytic triad in UXS proteins. (kuang2016roleofudpglucuronic pages 5-9, li2023comprehensiveanalysisof pages 9-12)
Inference for BRADI_1g66227v3: Because the UniProt entry (provided by the user) places I1H6U0 in a NAD(P)-dependent epimerase/dehydratase-like superfamily, and plant UXS orthologs show NAD(P)-binding-related motifs, it is reasonable to infer that BRADI_1g66227v3 encodes a functional UXS-like enzyme with similar catalytic architecture; however, direct cofactor usage and enzyme kinetics have not been demonstrated for the Brachypodium protein in the retrieved literature. (kuang2016roleofudpglucuronic pages 5-9, li2023comprehensiveanalysisof pages 9-12)
Multiple studies support that plant UXS enzymes segregate into cytosolic (soluble) isoforms and Golgi/endomembrane-associated isoforms:
- Early Arabidopsis gene family work concluded that UDP-Xyl synthesis occurs in both cytosolic and membrane-bound compartments, with some UXS predicted as type II membrane proteins oriented toward the lumen and one class likely cytosolic. (Harper & Bar-Peled, 2002-12, Plant Physiology, https://doi.org/10.1104/pp.009654) (harper2002biosynthesisofudpxylose. pages 1-2)
- Biochemical and imaging work on AtUXS2 supports Golgi/endomembrane localization for a membrane-associated UXS isoform and discusses potential substrate channeling to Golgi xylosyltransferases. (Pattathil et al., 2005-01, Planta, https://doi.org/10.1007/s00425-004-1471-7) (pattathil2005biosynthesisofudpxylose pages 8-10)
- In Arabidopsis, Kuang et al. report AtUXS1/2/4 are Golgi-localized, whereas AtUXS3/5/6 are cytosolic, supporting functional partitioning of UDP-Xyl production. (Kuang et al., 2016-08, Molecular Plant, https://doi.org/10.1016/j.molp.2016.04.013) (kuang2016roleofudpglucuronic pages 1-5)
- A 2023 tobacco study experimentally localized NtUXS16 to the medial-Golgi and used protease digestion/protection to argue for a topology that contradicts a simple “type II membrane protein” prediction, highlighting that UXS membrane association/topology can be more complex than motif-only predictions. (Li et al., 2023-11, BMC Plant Biology, https://doi.org/10.1186/s12870-023-04575-3) (li2023comprehensiveanalysisof pages 9-12)
Without gene-specific localization experiments, BRADI_1g66227v3 can only be assigned a probable localization class by comparative logic: in plants, a UXS-like enzyme either contributes to a cytosolic UDP-Xyl pool (supporting transporter-mediated delivery into the Golgi) or is itself Golgi/endomembrane associated, potentially more directly coupled to luminal glycosyltransferases. (kuang2016roleofudpglucuronic pages 1-5, pattathil2005biosynthesisofudpxylose pages 8-10)
Across plant studies, the best-supported primary reaction is:
- UDP-GlcA → UDP-Xyl catalyzed by UXS. (kuang2016roleofudpglucuronic pages 1-5, harper2002biosynthesisofudpxylose. pages 1-2, kuang2016roleofudpglucuronic pages 9-12)
No alternative substrates/products for plant UXS are supported in the retrieved evidence; thus, the safest annotation for BRADI_1g66227v3 is UDP-glucuronic acid decarboxylase producing UDP-xylose.
Kuang et al. provide kinetic constants for soluble Arabidopsis isoforms using UDP-GlcA as substrate:
- Km (UDP-GlcA): AtUXS5 0.40 mM, AtUXS3 0.48 mM, AtUXS6 0.54 mM; assay optima reported at pH 6.0 and 30°C. (Kuang et al., 2016-08, Molecular Plant, https://doi.org/10.1016/j.molp.2016.04.013) (kuang2016roleofudpglucuronic pages 5-9, kuang2016roleofudpglucuronic pages 9-12)
They also report higher measured activity for a cytosolic isoform compared with a Golgi-localized one under their assay conditions (example values):
- AtUXS3 ~475 nmol UDP-Xyl min⁻¹ mg⁻¹ vs AtUXS2 ~53 nmol UDP-Xyl min⁻¹ mg⁻¹. (kuang2016roleofudpglucuronic pages 9-12)
Inference for BRADI_1g66227v3: these values cannot be transferred quantitatively to Brachypodium I1H6U0, but they support the expectation that cytosolic soluble UXS enzymes can generate substantial UDP-Xyl flux in vivo. (kuang2016roleofudpglucuronic pages 9-12)
Kuang et al. performed reverse genetics in Arabidopsis and concluded that cytosolic UXS has a major role in supplying UDP-Xyl for xylan/heteroxylan biosynthesis; the uxs3 uxs5 uxs6 (cytosolic) triple mutant displayed strong cell-wall-associated phenotypes compared with the Golgi-localized triple mutant. (Kuang et al., 2016-08, Molecular Plant, https://doi.org/10.1016/j.molp.2016.04.013) (kuang2016roleofudpglucuronic pages 12-16, kuang2016roleofudpglucuronic pages 9-12)
Reported quantitative and structural impacts in the stronger mutant background include:
- ~21% lower wall xylose (Xyl) and 42% lower GlcA; ~30% lower heteroxylan; changes in xylem/fiber wall anatomy; and altered non-cellulosic polymer molecular weight. (kuang2016roleofudpglucuronic pages 9-12)
Kuang et al. also report increased saccharification in the cytosolic UXS triple mutant background, with up to ~18% increased glucose release during saccharification assays, linking UXS-dependent cell-wall structure to biomass processing traits. (kuang2016roleofudpglucuronic pages 12-16)
Inference for BRADI_1g66227v3 in grasses: because grasses rely heavily on heteroxylan/arabinoxylan-rich walls, a functional UXS in Brachypodium is plausibly a determinant of hemicellulose biosynthesis and, by extension, digestibility/saccharification properties—though this remains untested for BRADI_1g66227v3 specifically in the retrieved evidence. (kuang2016roleofudpglucuronic pages 12-16, kuang2016roleofudpglucuronic pages 1-5)
A 2023 BMC Plant Biology study performed a genome-wide analysis of tobacco UXS genes (17 family members) and experimentally localized NtUXS16 to the medial-Golgi. Notably, protease-based topology analysis suggested NtUXS16 is not a canonical type II membrane protein as previously predicted, refining current thinking about UXS membrane association. (Li et al., 2023-11, BMC Plant Biology, https://doi.org/10.1186/s12870-023-04575-3) (li2023comprehensiveanalysisof pages 9-12)
The same study reported that ectopic expression of NtUXS16 in Arabidopsis significantly altered seedling morphology in darkness (longer hypocotyls and roots), supporting that UXS perturbation can impact growth programs (likely via cell-wall or glycosylation-related mechanisms). (li2023comprehensiveanalysisof pages 9-12)
A 2024 ACS Synthetic Biology review summarizes progress in engineering nucleotide-sugar metabolism in Saccharomyces cerevisiae and specifically reports that integrating Arabidopsis UGD (to make UDP-GlcA) together with Arabidopsis UXS (to make UDP-Xyl) enabled production of UDP-D-Xyl in yeast, facilitating downstream xylosylation steps toward triterpenoid saponins such as notoginsenoside R1/R2 (with UGT94Q13 identified for the xylosylation step). (Crowe et al., 2024-05, ACS Synthetic Biology, https://doi.org/10.1021/acssynbio.3c00737) (crowe2024advancesinengineering pages 6-7)
This constitutes a concrete, real-world implementation of plant UXS as a modular “glycosyl-donor supply” enzyme for heterologous natural product glycosylation. (crowe2024advancesinengineering pages 6-7)
Functional genetics in Arabidopsis indicates that reducing cytosolic UXS function can decrease xylan/xylose in cell walls and improve saccharification yield (up to ~18% increased glucose release), motivating UXS-pathway manipulation as a lever for biomass processing traits. (kuang2016roleofudpglucuronic pages 12-16, kuang2016roleofudpglucuronic pages 9-12)
Engineering UDP-Xyl biosynthesis (AtUGD + AtUXS) in yeast provides UDP-D-Xyl to support xylosyltransferase reactions in heterologous pathways, relevant to production of xylosylated triterpenoids and other glycosylated products. (crowe2024advancesinengineering pages 6-7)
| Annotation aspect | Best-supported statement | Evidence/citation id(s) | Key source (authors year, journal) and URL |
|---|---|---|---|
| Gene/protein identity for BRADI_1g66227v3 | Direct literature on BRADI_1g66227v3 / UniProt I1H6U0 in Brachypodium distachyon was not found in the retrieved evidence. Functional annotation is therefore inferred from the UniProt description (UDP-glucuronate decarboxylase / UXS-like) together with conserved plant UXS literature; this should be treated as inference rather than gene-specific experimental proof. | (kuang2016roleofudpglucuronic pages 12-16, kuang2016roleofudpglucuronic pages 5-9) | Kuang et al. 2016, Molecular Plant — https://doi.org/10.1016/j.molp.2016.04.013 |
| Reaction | Plant UXS/UDP-glucuronate decarboxylase catalyzes conversion of UDP-glucuronic acid (UDP-GlcA) to UDP-xylose (UDP-Xyl). | (kuang2016roleofudpglucuronic pages 1-5, harper2002biosynthesisofudpxylose. pages 1-2, kuang2016roleofudpglucuronic pages 9-12, li2023comprehensiveanalysisof pages 9-12) | Harper & Bar-Peled 2002, Plant Physiology — https://doi.org/10.1104/pp.009654; Kuang et al. 2016, Molecular Plant — https://doi.org/10.1016/j.molp.2016.04.013; Li et al. 2023, BMC Plant Biology — https://doi.org/10.1186/s12870-023-04575-3 |
| EC number | The enzyme class discussed in the plant UXS literature corresponds to UDP-glucuronic acid decarboxylase / UDP-xylose synthase (EC 4.1.1.35), matching the UniProt annotation for I1H6U0. | (kuang2016roleofudpglucuronic pages 1-5, li2023comprehensiveanalysisof pages 9-12) | Kuang et al. 2016, Molecular Plant — https://doi.org/10.1016/j.molp.2016.04.013; Li et al. 2023, BMC Plant Biology — https://doi.org/10.1186/s12870-023-04575-3 |
| Substrate | Best-supported substrate is UDP-GlcA. | (kuang2016roleofudpglucuronic pages 1-5, harper2002biosynthesisofudpxylose. pages 1-2, kuang2016roleofudpglucuronic pages 9-12) | Harper & Bar-Peled 2002, Plant Physiology — https://doi.org/10.1104/pp.009654; Kuang et al. 2016, Molecular Plant — https://doi.org/10.1016/j.molp.2016.04.013 |
| Product | Best-supported product is UDP-Xyl, the nucleotide sugar donor used for multiple glycosylation reactions in plants. | (kuang2016roleofudpglucuronic pages 1-5, pattathil2005biosynthesisofudpxylose pages 8-10, li2023comprehensiveanalysisof pages 9-12) | Kuang et al. 2016, Molecular Plant — https://doi.org/10.1016/j.molp.2016.04.013; Pattathil et al. 2005, Planta — https://doi.org/10.1007/s00425-004-1471-7; Li et al. 2023, BMC Plant Biology — https://doi.org/10.1186/s12870-023-04575-3 |
| Reversibility | The reaction is described in the evidence as irreversible decarboxylation of UDP-GlcA to UDP-Xyl. | (kuang2016roleofudpglucuronic pages 1-5, kuang2016roleofudpglucuronic pages 5-9, li2023comprehensiveanalysisof pages 9-12) | Kuang et al. 2016, Molecular Plant — https://doi.org/10.1016/j.molp.2016.04.013; Li et al. 2023, BMC Plant Biology — https://doi.org/10.1186/s12870-023-04575-3 |
| Cofactor / catalytic features | The retrieved evidence supports conserved GxxGxxG (ADP/NAD(P)-binding-related) and YxxxK motifs, with a Ser-Tyr-Lys catalytic triad in plant UXS proteins. Direct cofactor usage is not explicitly demonstrated in the gathered snippets for BRADI_1g66227v3; NAD(P)-dependence should therefore be stated as inferred from motif/family annotation, not as direct gene-specific proof. | (kuang2016roleofudpglucuronic pages 5-9, li2023comprehensiveanalysisof pages 9-12) | Kuang et al. 2016, Molecular Plant — https://doi.org/10.1016/j.molp.2016.04.013; Li et al. 2023, BMC Plant Biology — https://doi.org/10.1186/s12870-023-04575-3 |
| Subcellular localization classes | Plant UXS proteins occur in at least two localization classes: cytosolic/soluble isoforms and Golgi-associated or endomembrane-associated isoforms. This suggests BRADI_1g66227v3 may belong to one of these compartmentalized UXS pools, but its exact localization was not found directly for Brachypodium. | (kuang2016roleofudpglucuronic pages 1-5, pattathil2005biosynthesisofudpxylose pages 8-10, harper2002biosynthesisofudpxylose. pages 1-2, li2023comprehensiveanalysisof pages 9-12) | Harper & Bar-Peled 2002, Plant Physiology — https://doi.org/10.1104/pp.009654; Pattathil et al. 2005, Planta — https://doi.org/10.1007/s00425-004-1471-7; Li et al. 2023, BMC Plant Biology — https://doi.org/10.1186/s12870-023-04575-3 |
| Likely localization inference for BRADI_1g66227v3 | Because UniProt I1H6U0 is described as a UXS-like member of the NAD(P)-dependent epimerase/dehydratase family, its most likely cellular role is in a compartmentalized UDP-Xyl supply pathway in either the cytosol or Golgi-associated system; however, no direct BRADI_1g66227v3 localization experiment was identified. | (kuang2016roleofudpglucuronic pages 1-5, pattathil2005biosynthesisofudpxylose pages 8-10) | Kuang et al. 2016, Molecular Plant — https://doi.org/10.1016/j.molp.2016.04.013; Pattathil et al. 2005, Planta — https://doi.org/10.1007/s00425-004-1471-7 |
| Pathway / biological role | UXS supplies UDP-Xyl, a key donor for synthesis of xylan, xyloglucan, and other cell-wall glycans; UDP-Xyl can also be interconverted by UXE toward UDP-arabinose-related pathways. This places BRADI_1g66227v3 most plausibly in nucleotide-sugar metabolism supporting cell-wall biosynthesis. | (kuang2016roleofudpglucuronic pages 1-5, pattathil2005biosynthesisofudpxylose pages 8-10, li2023comprehensiveanalysisof pages 9-12) | Kuang et al. 2016, Molecular Plant — https://doi.org/10.1016/j.molp.2016.04.013; Pattathil et al. 2005, Planta — https://doi.org/10.1007/s00425-004-1471-7; Li et al. 2023, BMC Plant Biology — https://doi.org/10.1186/s12870-023-04575-3 |
| Transport coupling | Arabidopsis evidence supports a model in which cytosolic UDP-Xyl is imported into the Golgi by UXT transporters, indicating that UXS function is integrated with nucleotide-sugar transport to luminal glycosylation. This strengthens the inference that BRADI_1g66227v3 participates in a broader UDP-Xyl supply network rather than acting in isolation. | (kuang2016roleofudpglucuronic pages 12-16, kuang2016roleofudpglucuronic pages 9-12) | Kuang et al. 2016, Molecular Plant — https://doi.org/10.1016/j.molp.2016.04.013 |
| Mutant / phenotype evidence | In Arabidopsis, cytosolic UXS triple mutants (uxs3 uxs5 uxs6) show stronger defects than Golgi-localized triple mutants: reduced wall xylose/xylan, collapsed xylem, thinner fiber walls, lower non-cellulosic polymer molecular weight, and improved saccharification. This is strong orthology-based evidence that BRADI_1g66227v3, if an active UXS, would be expected to affect grass cell-wall xylan/hemicellulose metabolism. | (kuang2016roleofudpglucuronic pages 12-16, kuang2016roleofudpglucuronic pages 1-5, kuang2016roleofudpglucuronic pages 9-12) | Kuang et al. 2016, Molecular Plant — https://doi.org/10.1016/j.molp.2016.04.013 |
| Quantitative phenotype data | Reported Arabidopsis quantitative effects include ~21% lower wall Xyl, 42% lower GlcA, ~30% lower heteroxylan, and up to ~18% increased glucose release during saccharification in the stronger cytosolic UXS mutant background. | (kuang2016roleofudpglucuronic pages 12-16, kuang2016roleofudpglucuronic pages 9-12) | Kuang et al. 2016, Molecular Plant — https://doi.org/10.1016/j.molp.2016.04.013 |
| Quantitative enzyme data | For Arabidopsis soluble UXS isoforms, reported Km values for UDP-GlcA are 0.40 mM (AtUXS5), 0.48 mM (AtUXS3), and 0.54 mM (AtUXS6), with assay optima around pH 6.0 and 30°C. | (kuang2016roleofudpglucuronic pages 5-9, kuang2016roleofudpglucuronic pages 9-12) | Kuang et al. 2016, Molecular Plant — https://doi.org/10.1016/j.molp.2016.04.013 |
| Relative activity by localization class | In Arabidopsis assays, cytosolic Group I UXS enzymes showed higher measured UDP-Xyl production than Golgi-localized Group II isoforms; one example given is AtUXS3 ~475 nmol UDP-Xyl min^-1 mg^-1 versus AtUXS2 ~53 nmol UDP-Xyl min^-1 mg^-1. | (kuang2016roleofudpglucuronic pages 9-12) | Kuang et al. 2016, Molecular Plant — https://doi.org/10.1016/j.molp.2016.04.013 |
| Grasses / monocot relevance | The retrieved evidence mentions that UXS genes have been cloned from rice and barley, and comparative genomics notes single Group I members in barley and rice; however, no direct experimental characterization of BRADI_1g66227v3 in Brachypodium was found. | (kuang2016roleofudpglucuronic pages 12-16, kuang2016roleofudpglucuronic pages 5-9) | Kuang et al. 2016, Molecular Plant — https://doi.org/10.1016/j.molp.2016.04.013 |
| Recent developments (2023) | A 2023 study in tobacco identified 17 NtUXS genes and showed that NtUXS16 localizes to the medial Golgi; overexpression in Arabidopsis significantly increased hypocotyl and root elongation in darkness. This supports ongoing functional diversification studies of plant UXS genes beyond Arabidopsis. | (li2023comprehensiveanalysisof pages 9-12) | Li et al. 2023, BMC Plant Biology — https://doi.org/10.1186/s12870-023-04575-3 |
| Recent applications (2024) | A 2024 synthetic biology review reports that Arabidopsis UGD + AtUXS were introduced into yeast to generate UDP-D-Xyl, enabling xylosylation steps toward notoginsenoside R1 and R2. This is a real-world implementation of UXS as a metabolic engineering module for glycosyl donor supply. | (crowe2024advancesinengineering pages 6-7) | Crowe et al. 2024, ACS Synthetic Biology — https://doi.org/10.1021/acssynbio.3c00737 |
| Broader application significance | Recent plant glycoengineering literature emphasizes that UDP-Xyl is an important donor not only for wall polysaccharides but also for specialized metabolite glycosylation, making UXS genes attractive engineering targets. For BRADI_1g66227v3, this expands likely relevance from cell-wall biology to engineered biosynthesis platforms, although this has not been tested directly for the Brachypodium gene. | (crowe2024advancesinengineering pages 6-7, li2023comprehensiveanalysisof pages 9-12) | Crowe et al. 2024, ACS Synthetic Biology — https://doi.org/10.1021/acssynbio.3c00737; Li et al. 2023, BMC Plant Biology — https://doi.org/10.1186/s12870-023-04575-3 |
Table: This table summarizes the best-supported functional annotation for BRADI_1g66227v3 (UniProt I1H6U0) by combining the UniProt identity with experimentally characterized plant UXS literature and recent engineering studies. It distinguishes direct evidence from inference and highlights the strongest citations for reaction chemistry, localization classes, pathway role, phenotypes, and applications.
Proposed function (orthology-based): BRADI_1g66227v3 (UniProt I1H6U0) most plausibly encodes a UDP-glucuronic acid decarboxylase/UDP-xylose synthase (UXS; EC 4.1.1.35) producing UDP-Xyl from UDP-GlcA, thereby contributing to nucleotide-sugar supply for cell-wall hemicellulose (xylan/heteroxylan) biosynthesis. (kuang2016roleofudpglucuronic pages 1-5, kuang2016roleofudpglucuronic pages 9-12)
Proposed localization (inference): likely cytosolic soluble or Golgi/endomembrane-associated, consistent with known plant UXS compartmentalization; specific compartment for BRADI_1g66227v3 remains unverified. (kuang2016roleofudpglucuronic pages 1-5, pattathil2005biosynthesisofudpxylose pages 8-10, li2023comprehensiveanalysisof pages 9-12)
Pathway and phenotype expectations (inference guided by strong evidence in orthologs): perturbation would be expected to alter xylan content and secondary wall properties and could impact digestibility/saccharification, as demonstrated for cytosolic UXS triple mutants in Arabidopsis. (kuang2016roleofudpglucuronic pages 12-16, kuang2016roleofudpglucuronic pages 9-12)
References
(kuang2016roleofudpglucuronic pages 12-16): Beiqing Kuang, Xianhai Zhao, Chun Zhou, Wei Zeng, Junli Ren, Berit Ebert, Cherie T. Beahan, Xiaomei Deng, Qingyin Zeng, Gongke Zhou, Monika S. Doblin, Joshua L. Heazlewood, Antony Bacic, Xiaoyang Chen, and Ai-Min Wu. Role of udp-glucuronic acid decarboxylase in xylan biosynthesis in arabidopsis. Molecular Plant, 9:1119-1131, Aug 2016. URL: https://doi.org/10.1016/j.molp.2016.04.013, doi:10.1016/j.molp.2016.04.013. This article has 93 citations and is from a highest quality peer-reviewed journal.
(kuang2016roleofudpglucuronic pages 5-9): Beiqing Kuang, Xianhai Zhao, Chun Zhou, Wei Zeng, Junli Ren, Berit Ebert, Cherie T. Beahan, Xiaomei Deng, Qingyin Zeng, Gongke Zhou, Monika S. Doblin, Joshua L. Heazlewood, Antony Bacic, Xiaoyang Chen, and Ai-Min Wu. Role of udp-glucuronic acid decarboxylase in xylan biosynthesis in arabidopsis. Molecular Plant, 9:1119-1131, Aug 2016. URL: https://doi.org/10.1016/j.molp.2016.04.013, doi:10.1016/j.molp.2016.04.013. This article has 93 citations and is from a highest quality peer-reviewed journal.
(kuang2016roleofudpglucuronic pages 1-5): Beiqing Kuang, Xianhai Zhao, Chun Zhou, Wei Zeng, Junli Ren, Berit Ebert, Cherie T. Beahan, Xiaomei Deng, Qingyin Zeng, Gongke Zhou, Monika S. Doblin, Joshua L. Heazlewood, Antony Bacic, Xiaoyang Chen, and Ai-Min Wu. Role of udp-glucuronic acid decarboxylase in xylan biosynthesis in arabidopsis. Molecular Plant, 9:1119-1131, Aug 2016. URL: https://doi.org/10.1016/j.molp.2016.04.013, doi:10.1016/j.molp.2016.04.013. This article has 93 citations and is from a highest quality peer-reviewed journal.
(harper2002biosynthesisofudpxylose. pages 1-2): April D Harper and M. Bar-Peled. Biosynthesis of udp-xylose. cloning and characterization of a novel arabidopsis gene family, uxs, encoding soluble and putative membrane-bound udp-glucuronic acid decarboxylase isoforms. Plant Physiology, 130:2188-2198, Dec 2002. URL: https://doi.org/10.1104/pp.009654, doi:10.1104/pp.009654. This article has 226 citations and is from a highest quality peer-reviewed journal.
(li2023comprehensiveanalysisof pages 9-12): Zhimin Li, Runping Chen, Yufang Wen, Hanxiang Liu, Yangyang Chen, Xiaoyu Wu, Youxin Yang, Xinru Wu, Yong Zhou, and Jianping Liu. Comprehensive analysis of the udp-glucuronate decarboxylase (uxs) gene family in tobacco and functional characterization of ntuxs16 in golgi apparatus in arabidopsis. BMC Plant Biology, Nov 2023. URL: https://doi.org/10.1186/s12870-023-04575-3, doi:10.1186/s12870-023-04575-3. This article has 3 citations and is from a peer-reviewed journal.
(pattathil2005biosynthesisofudpxylose pages 8-10): Sivakumar Pattathil, April D. Harper, and Maor Bar-Peled. Biosynthesis of udp-xylose: characterization of membrane-bound atuxs2. Planta, 221:538-548, Jan 2005. URL: https://doi.org/10.1007/s00425-004-1471-7, doi:10.1007/s00425-004-1471-7. This article has 92 citations and is from a peer-reviewed journal.
(kuang2016roleofudpglucuronic pages 9-12): Beiqing Kuang, Xianhai Zhao, Chun Zhou, Wei Zeng, Junli Ren, Berit Ebert, Cherie T. Beahan, Xiaomei Deng, Qingyin Zeng, Gongke Zhou, Monika S. Doblin, Joshua L. Heazlewood, Antony Bacic, Xiaoyang Chen, and Ai-Min Wu. Role of udp-glucuronic acid decarboxylase in xylan biosynthesis in arabidopsis. Molecular Plant, 9:1119-1131, Aug 2016. URL: https://doi.org/10.1016/j.molp.2016.04.013, doi:10.1016/j.molp.2016.04.013. This article has 93 citations and is from a highest quality peer-reviewed journal.
(crowe2024advancesinengineering pages 6-7): Samantha A. Crowe, Yuzhong Liu, Xixi Zhao, Henrik V. Scheller, and Jay D. Keasling. Advances in engineering nucleotide sugar metabolism for natural product glycosylation in saccharomyces cerevisiae. ACS Synthetic Biology, 13:1589-1599, May 2024. URL: https://doi.org/10.1021/acssynbio.3c00737, doi:10.1021/acssynbio.3c00737. This article has 15 citations and is from a domain leading peer-reviewed journal.