124 lines
7.8 KiB
Turtle
124 lines
7.8 KiB
Turtle
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<http://treatment.plazi.org/id/03F41955FFBDF74FFCD0F987FC5EFC51>
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cito:cites <http://dx.doi.org/10.5281/zenodo.10491220>, <http://dx.doi.org/10.5281/zenodo.10491222>, <http://dx.doi.org/10.5281/zenodo.10491226>, <http://dx.doi.org/10.5281/zenodo.10491224>, <http://dx.doi.org/10.5281/zenodo.10491230> ;
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dc:creator "Rodríguez-Rodríguez, Manuel Fernando; Salas, Joaquín J.; Garcés, Rafael; Martínez-Force, Enrique" ;
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dc:title "Camelina sativa Crantz" ;
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trt:publishedIn <http://dx.doi.org/10.1016/j.phytochem.2014.08.014> ;
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trt:treatsTaxonName <http://taxon-name.plazi.org/id/Plantae/Camelina_sativa> ;
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a trt:Treatment .
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<http://dx.doi.org/10.1016/j.phytochem.2014.08.014>
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bibo:endPage "15" ;
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bibo:journal "Phytochemistry" ;
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bibo:pubDate "2014-11-30" ;
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bibo:startPage "7" ;
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bibo:volume "107" ;
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dc:creator "Rodríguez-Rodríguez, Manuel Fernando; Salas, Joaquín J.; Garcés, Rafael; Martínez-Force, Enrique" ;
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dc:date "2014" ;
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dc:title "Acyl-ACP thioesterases from Camelina sativa: Cloning, enzymatic characterization and implication in seed oil fatty acid composition" ;
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fabio:hasPart <http://dx.doi.org/10.5281/zenodo.10491220>, <http://dx.doi.org/10.5281/zenodo.10491222>, <http://dx.doi.org/10.5281/zenodo.10491226>, <http://dx.doi.org/10.5281/zenodo.10491224>, <http://dx.doi.org/10.5281/zenodo.10491230> ;
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a fabio:JournalArticle .
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<http://taxon-name.plazi.org/id/Plantae/Camelina_sativa>
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dwc:class "Magnoliopsida" ;
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dwc:family "Brassicaceae" ;
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dwc:genus "Camelina" ;
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dwc:kingdom "Plantae" ;
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dwc:order "Brassicales" ;
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dwc:phylum "Tracheophyta" ;
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dwc:rank "species" ;
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dwc:species "sativa" ;
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trt:hasParentName <http://taxon-name.plazi.org/id/Plantae/Camelina> ;
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a dwcFP:TaxonName .
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<http://taxon-name.plazi.org/id/Plantae/Camelina>
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dwc:class "Magnoliopsida" ;
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dwc:family "Brassicaceae" ;
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dwc:genus "Camelina" ;
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dwc:kingdom "Plantae" ;
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dwc:order "Brassicales" ;
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dwc:phylum "Tracheophyta" ;
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dwc:family "Brassicaceae" ;
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dwc:kingdom "Plantae" ;
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dwc:kingdom "Plantae" ;
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<http://dx.doi.org/10.5281/zenodo.10491220>
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dc:description "Fig. 1. Alignment of the deduced amino acid sequences of acyl-ACP thioesterase A enzymes from C. sativa (CsFatA1, AFQ60947.1; CsFatA2, AFQ60948.1; CsFatA3, AFQ60946.1), Arabidopsis thaliana (AtFatA1, NP_189147.1; AtFatA2, NP_193041.1) and Zea mays (ZmFatA, DAA40472.1). Identical amino acids are shaded in black, whereas conserved residues are shaded in grey. The amino acids considered to constitute the signal peptide are boxed. The three conserved residues that constitute the catalytic triad are indicated with an star (Asn-273; His-275; Gln-311), and the residues involved in specific substrate recognition and related with the thioesterase activity are indicated by the arrowheads (Gly-135; Ala-137; Arg-143; Lys-144; Thr-182; Arg-184; Arg-212; Arg-213; Lys-216). The conservative changes in the amino acid sequence between the three CsFatA alleles are marked by closed circles and the semi-conservative changes between them by open circles." ;
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fabio:hasRepresentation <https://zenodo.org/record/10491220/files/figure.png> ;
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a fabio:Figure .
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<http://dx.doi.org/10.5281/zenodo.10491222>
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dc:description "Fig. 2. Alignment of the deduced amino acid sequences of the acyl-ACP thioesterase B enzymes from C. sativa (CsFatB1, AFQ60949.1; CsFatB2, AFQ60950.1; CsFatB3, AFQ60951.1), Arabidopsis thaliana (AtFatB, CAA85388.1) and Zea mays (ZmFatB, AFW85914.1). Identical amino acids are shaded in black, whereas conserved residues are shaded in grey. The amino acids considered to constitute the signal peptide are boxed and the hydrophobic region in FatB is underlined. The three conserved residues that constitute the catalytic triad are indicated by an star (Asn-319; His-321; Cys-383), and the residues involved in the specific substrate recognition and related with the thioesterase activity are indicated by the arrowheads (Asp-186; Gly-189; Met-233; Arg-235; Lys-267; Glu-270). The conservative changes in the amino acid sequence between the three CsFatB alleles are indicated by open circles." ;
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fabio:hasRepresentation <https://zenodo.org/record/10491222/files/figure.png> ;
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a fabio:Figure .
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<http://dx.doi.org/10.5281/zenodo.10491226>
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dc:description "Fig. 3. Coomassie blue stained SDS–PAGE showing recombinant C. sativa acyl-ACP thioesterase A (panel A) and acyl-ACP thioesterase B (panel B). Lane 1, soluble fraction, 15 µg protein; lane 2, soluble fraction not retained on the Ni–NTA Agarose column (Qiagen), 15 µg protein; lane 3, Ni–NTA Agarose wash, 1.5 µg protein; lane 4, purified acyl- ACP thioesterase 1.5 µg protein." ;
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fabio:hasRepresentation <https://zenodo.org/record/10491226/files/figure.png> ;
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a fabio:Figure .
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<http://dx.doi.org/10.5281/zenodo.10491224>
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dc:description "Fig. 4. Substrate specificity of C. sativa acyl-ACP thioesterases expressed in E. coli. The activity was measured with the purified His-tagged CsFatA (black columns) and His-tagged CsFatB (white columns) enzymes, testing different acyl-ACP substrates. The data represent the mean (±SD) from three independent assays." ;
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fabio:hasRepresentation <https://zenodo.org/record/10491224/files/figure.png> ;
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a fabio:Figure .
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<http://dx.doi.org/10.5281/zenodo.10491230>
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dc:description "Fig. 5. Expression of the CsFatA (black columns) and CsFatB (white columns) genes in vegetative tissues and developing seeds from C. sativa determined by QRT-PCR. The data represent the mean values ± SD of three independent assays." ;
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fabio:hasRepresentation <https://zenodo.org/record/10491230/files/figure.png> ;
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a fabio:Figure .
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dwc:collectionCode "L" ;
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trt:httpUri <https://treatment.plazi.org/id/03F41955FFBDF74FFCD0F987FC5EFC51#3B35A21EFFBEF749FCABF942FDE4F9C3> ;
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a dwc:MaterialCitation .
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