Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Probing the diversity of the Arabidopsis glutathione S-transferase gene family.
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Survey defining the Arabidopsis GST classes; family-level statements on cytoplasmic location and detoxification. UniProt cites it for the alternative name AtGSTF6, but early phi-class numbering differs between papers.
"the large phi (GSTF) and tau (GSTU) classes are plant specific"
Aluminum induces oxidative stress genes in Arabidopsis thaliana.
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An aluminium-induced GST cDNA (identified by sequence identity to a Kiyosue et al. 1993 GST) is reported; its link to oxidative stress is by citation.
"The genes encoded peroxidase, glutathione-S-transferase, blue copper-binding protein, and a protein homologous to the reticuline:oxygen oxidoreductase enzyme."
Omics-based identification of Arabidopsis Myb transcription factors regulating aliphatic glucosinolate biosynthesis.
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GSTF11 (At3g03190) and GSTU20 (At1g78370) are MYB28-regulated together with aliphatic glucosinolate pathway genes.
"Transcriptome analyses of myb28 and Myb28 -overexpressing cell cultures indicated that both of them are regulated by Myb28"
Enzyme activities and subcellular localization of members of the Arabidopsis glutathione transferase superfamily.
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GSTF11 could not be expressed as soluble recombinant protein, so it was not assayed.
"GSTF11, GSTF12, and GSTF13 could not be cloned, or only expressed as insoluble proteins"
Production of the cancer-preventive glucoraphanin in tobacco.
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Engineering of the glucoraphanin pathway into tobacco by coupling chain-elongation enzymes to glucosinolate core-pathway enzymes; cited by Zhang et al. 2022 as showing GSTF11 can increase, but is not essential for, heterologous glucosinolate production.
"by coupling the five enzymes of the chain-elongation pathway to eight enzymes of the glucosinolate pathway, we show production of glucoraphanin"
The Role of the GSTF11 Gene in Resistance to Powdery Mildew Infection and Cold Stress.
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Constitutive expression of Arabidopsis GSTF11 in Brassica napus increased total leaf GST activity by about 30%.
"A higher GSTF11 mRNA content in transgenic plants was accompanied by an increase in the activity of the GST enzyme by an average of 30%"
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Transgenic plants were more resistant to powdery mildew and the transgene was cold-responsive.
"In most of transgenic plants, mycelium growth was inhibited"
Glutathione Transferase U13 Functions in Pathogen-Triggered Glucosinolate Metabolism.
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Comparator for the NEW-term decision. GSTU13 is required for the PEN2 indole glucosinolate pathway and carries a TAIR IMP annotation to indole glucosinolate catabolic process (acts_upstream_of_or_within), a precedent for mutant-based glucosinolate process annotations on GSTs.
"Glutathione-S-Transferase class-tau member 13 (GSTU13) as an indispensable component of the PEN2 immune pathway for IG metabolism"
Arabidopsis Glutathione-S-Transferases GSTF11 and GSTU20 Function in Aliphatic Glucosinolate Biosynthesis.
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CRISPR gstf11 knockouts reduce several aliphatic, but not indolic, glucosinolates; effects are weaker than gstu20 and additive in the double mutant.
"no significant changes in the abundance of indolic GSLs were noted in gstf11 (Figures 4A,B) and gstu20 (Figures 5A,B) mutants"
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GSTF11 enzymatic activity was not measured because the protein could not be purified.
"The enzymatic activity of GSTF11 was undetectable because of the protein could not be isolated and purified in vitro due to the rare abundance."
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The double mutant still makes aliphatic glucosinolates.
"the double mutation of GSTF11 and GSTU20 caused a dramatic decrease but did not completely abolish the formation of aliphatic GSLs"
GSTF11 pairwise identity to the Kiyosue et al. 1993 GSTs (ERD11, ERD13)