@article{TabatabaeiAlseekhShahidetal.2022,
  author    = {Tabatabaei, Iman and Alseekh, Saleh and Shahid, Mohammad and Leniak, Ewa and Wagner, Mateusz and Mahmoudi, Henda and Thushar, Sumitha and Fernie, Alisdair R. and Murphy, Kevin M. and Schm{\"o}ckel, Sandra M. and Tester, Mark and M{\"u}ller-R{\"o}ber, Bernd and Skirycz, Aleksandra and Balazadeh, Salma},
  title     = {The diversity of quinoa morphological traits and seed metabolic composition},
  series = {Scientific data},
  volume    = {9},
  journal   = {Scientific data},
  number    = {1},
  publisher = {Nature Research},
  address   = {Berlin},
  issn      = {2052-4463},
  doi       = {10.1038/s41597-022-01399-y},
  pages     = {7},
  year      = {2022},
  abstract  = {Quinoa (Chenopodium quinoa Willd.) is an herbaceous annual crop of the amaranth family (Amaranthaceae). It is increasingly cultivated for its nutritious grains, which are rich in protein and essential amino acids, lipids, and minerals. Quinoa exhibits a high tolerance towards various abiotic stresses including drought and salinity, which supports its agricultural cultivation under climate change conditions. The use of quinoa grains is compromised by anti-nutritional saponins, a terpenoid class of secondary metabolites deposited in the seed coat; their removal before consumption requires extensive washing, an economically and environmentally unfavorable process; or their accumulation can be reduced through breeding. In this study, we analyzed the seed metabolomes, including amino acids, fatty acids, and saponins, from 471 quinoa cultivars, including two related species, by liquid chromatography - mass spectrometry. Additionally, we determined a large number of agronomic traits including biomass, flowering time, and seed yield. The results revealed considerable diversity between genotypes and provide a knowledge base for future breeding or genome editing of quinoa.},
  language  = {en}
}
@article{DortaySchmoeckelFettkeetal.2011,
  author    = {Dortay, Hakan and Schm{\"o}ckel, Sandra M. and Fettke, J{\"o}rg and M{\"u}ller-R{\"o}ber, Bernd},
  title     = {Expression of human c-reactive protein in different systems and its purification from Leishmania tarentolae},
  series = {Protein expression and purification},
  volume    = {78},
  journal   = {Protein expression and purification},
  number    = {1},
  publisher = {Elsevier},
  address   = {San Diego},
  issn      = {1046-5928},
  doi       = {10.1016/j.pep.2011.03.010},
  pages     = {55 -- 60},
  year      = {2011},
  abstract  = {With its homo-pentameric structure and calcium-dependent specificity for phosphocholine (PCh), human c-reactive protein (CRP) is produced by the liver and secreted in elevated quantities in response to inflammation. CRP is widely accepted as a cardiac marker, e.g. in point-of-care diagnostics, however, its heterologous expression has proven difficult. Here, we demonstrate the expression of CRP in different Escherichia coli strains as well as by in vitro transcription/translation. Although expression in these systems was straightforward, most of the protein that accumulated was insoluble. We therefore expanded our study to include the expression of CRP in two eukaryotic hosts, namely the yeast Kluyveromyces lactis and the protozoon Leishmania tarentolae. Both expression systems are optimized for secretion of recombinant proteins and here allowed successful expression of soluble CRP. We also demonstrate the purification of recombinant CRP from Leishmania growth medium; the purification of protein expressed from K. lactis was not successful. Functional and intact CRP pentamer is known to interact with PCh in Ca(2+)-dependent manner. In this report we verify the binding specificity of recombinant CRP from L tarentolae (2 mu g/mL culture medium) for PCh.},
  language  = {en}
}
@article{AlshareefOtterbachAlluetal.2022,
  author    = {Alshareef, Nouf Owdah and Otterbach, Sophie L. and Allu, Annapurna Devi and Woo, Yong H. and de Werk, Tobias and Kamranfar, Iman and M{\"u}ller-R{\"o}ber, Bernd and Tester, Mark and Balazadeh, Salma and Schm{\"o}ckel, Sandra M.},
  title     = {NAC transcription factors ATAF1 and ANAC055 affect the heat stress response in Arabidopsis},
  series = {Scientific reports},
  volume    = {12},
  journal   = {Scientific reports},
  number    = {1},
  publisher = {Nature Research},
  address   = {Berlin},
  issn      = {2045-2322},
  doi       = {10.1038/s41598-022-14429-x},
  pages     = {15},
  year      = {2022},
  abstract  = {Pre-exposing (priming) plants to mild, non-lethal elevated temperature improves their tolerance to a later higher-temperature stress (triggering stimulus), which is of great ecological importance. 'Thermomemory' is maintaining this tolerance for an extended period of time. NAM/ATAF1/2/ CUC2 (NAC) proteins are plant-specific transcription factors (TFs) that modulate responses to abiotic stresses, including heat stress (HS). Here, we investigated the potential role of NACs for thermomemory. We determined the expression of 104 Ara bidopsis NAC genes after priming and triggering heat stimuli, and found ATAF1 expression is strongly induced right after priming and declines below control levels thereafter during thermorecovery. Knockout mutants of ATAF1 show better thermomemory than wild type, revealing a negative regulatory role. Differential expression analyses of RNA-seq data from ATAF1 overexpressor, ataf1 mutant and wild-type plants after heat priming revealed five genes that might be priming-associated direct targets of ATAF1: AT2G31260 (ATG9), AT2G41640 (GT61), AT3G44990 (XTH31), AT4G27720 and AT3G23540. Based on co-expression analyses applied to the aforementioned RNA-seq profiles, we identified ANAC055 to be transcriptionally co-regulated with ATAF1. Like atafl, anac055 mutants show improved thermomemory, revealing a potential co-control of both NACTFs over thermomemory. Our data reveals a core importance of two NAC transcription factors, ATAF1 and ANAC055, for thermomemory.},
  language  = {en}
}