Every reference with a DOI in the deposited reference list resolved to a known
work in Crossref or DataCite at the dated check, and none carried a retraction,
withdrawal, or removal notice.
The 33 checked references that resolve
resolves10.1002/prot.21715QMEAN: A comprehensive scoring function for model quality assessment
resolves10.1093/nar/gku340SWISS-MODEL: modelling protein tertiary and quaternary structure using evolutionary information
resolves10.1073/pnas.0706421104Characterization and engineering of the bifunctional
<i>N</i>
- and
<i>O</i>
-glucosyltransferase involved in xenobiotic metabolism in plants
resolves10.1111/j.1365-313X.2011.04853.xA genome‐wide phylogenetic reconstruction of family 1 UDP‐glycosyltransferases revealed the expansion of the family during the adaptation of plants to life on land
resolves10.1093/nar/gkh340MUSCLE: multiple sequence alignment with high accuracy and high throughput
resolves10.1039/c3np20111bA global approach to analysis and interpretation of metabolic data for plant natural product discovery
resolves10.1073/pnas.1604828113The biosynthetic pathway of the nonsugar, high-intensity sweetener mogroside V from
<i>Siraitia grosvenorii</i>
resolves10.1385/MB:19:2:201Isolation of High Quality RNA from Bilberry (Vaccinium myrtillus L.) Fruit
resolves10.1093/molbev/msw054MEGA7: Molecular Evolutionary Genetics Analysis Version 7.0 for Bigger Datasets
resolves10.1074/jbc.M109287200The Activity of ArabidopsisGlycosyltransferases toward Salicylic Acid, 4-Hydroxybenzoic Acid, and Other Benzoates
resolves10.1074/jbc.M007263200Identification of Glucosyltransferase Genes Involved in Sinapate Metabolism and Lignin Synthesis in Arabidopsis
resolves10.1002/bit.20154<i>Arabidopsis</i> glycosyltransferases as biocatalysts in fermentation for regioselective synthesis of diverse quercetin glucosides
resolves10.1016/j.jmb.2009.08.017Crystal Structures of Glycosyltransferase UGT78G1 Reveal the Molecular Basis for Glycosylation and Deglycosylation of (Iso)flavonoids
resolves10.1111/tpj.12645Purification, molecular cloning and functional characterization of flavonoid <i><scp>C</scp></i>‐glucosyltransferases from <i><scp>F</scp>agopyrum esculentum </i><scp>M</scp>. (buckwheat) cotyledon
resolves10.1038/sj.emboj.7600970Structure of a flavonoid glucosyltransferase reveals the basis for plant natural product modification
resolves10.1007/s00425-012-1706-yEstablishment of pomegranate (Punica granatum) hairy root cultures for genetic interrogation of the hydrolyzable tannin biosynthetic pathway
resolves10.1111/j.1744-7909.2011.01073.xExploring the Transcriptome Landscape of Pomegranate Fruit Peel for Natural Product Biosynthetic Gene and SSR Marker DiscoveryF
resolves10.1371/journal.pone.0156319Two UGT84 Family Glycosyltransferases Catalyze a Critical Reaction of Hydrolyzable Tannin Biosynthesis in Pomegranate (Punica granatum)
resolves10.1016/j.phytochem.2008.12.009Substrate specificity of plant UDP-dependent glycosyltransferases predicted from crystal structures and homology modeling
resolves10.3389/fpls.2012.00015Metabolomics as a Hypothesis-Generating Functional Genomics Tool for the Annotation of Arabidopsis thaliana Genes of “Unknown Function”
resolves10.3389/fpls.2017.02085Characterization of UGT716A1 as a Multi-substrate UDP:Flavonoid Glucosyltransferase Gene in Ginkgo biloba
resolves10.1002/jcc.21334AutoDock Vina: Improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading
resolves10.1021/acs.biochem.7b00946Characterization of a UGT84 Family Glycosyltransferase Provides New Insights into Substrate Binding and Reactivity of Galloylglucose Ester-Forming UGTs
resolves10.1007/s00425-009-0902-xRecombinant expression and functional characterisation of regiospecific flavonoid glucosyltransferases from Hieracium pilosella L.
resolves10.3390/molecules22101606Diverse Phytochemicals and Bioactivities in the Ancient Fruit and Modern Functional Food Pomegranate (Punica granatum)
resolves10.1111/tpj.12580A flavonoid 3‐<i>O</i>‐glucoside:2″‐<i>O</i>‐glucosyltransferase responsible for terminal modification of pollen‐specific flavonols in <i><scp>A</scp>rabidopsis thaliana</i>
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