The Sorghum bicolor genome and the diversification of grasses.Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J., Gundlach H., Haberer G., Hellsten U., Mitros T.[...], Rokhsar D.S.View abstractCited forNUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]Straincv. BTx623CategorySequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCNature 457:551-556 (2009)Cited in6099+
The Sorghum bicolor reference genome: improved assembly, gene annotations, a transcriptome atlas, and signatures of genome organization.McCormick R.F., Truong S.K., Sreedasyam A., Jenkins J., Shu S., Sims D., Kennedy M., Amirebrahimi M., Weers B.D.[...], Mullet J.E.View abstractCited forGENOME REANNOTATIONStraincv. BTx623CategorySequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCPlant J. 93:338-354 (2018)Cited in5999+
Structure and function of the cytochrome P450 monooxygenase cinnamate 4- hydroxylase from Sorghum bicolor.Zhang B., Lewis K.M., Abril A., Davydov D.R., Vermerris W., Sattler S.E., Kang C.View abstractCited forFUNCTION, CATALYTIC ACTIVITYCategoryFunctionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCPlant Physiol. 183:957-973 (2020)Cited in2
Functional and structural insight into the flexibility of cytochrome P450 reductases from Sorghum bicolor and its implications for lignin composition.Zhang B., Munske G.R., Timokhin V.I., Ralph J., Davydov D.R., Vermerris W., Sattler S.E., Kang C.View abstractCategoryStructureSourcePDB: 7SUX, PDB: 7SUZ, PDB: 7SV0PubMedEurope PMCJ Biol Chem 298:101761-101761 (2022)Mapped to1