@article{KaruwanarintPhonratTungtrongchitretal.2018,
  author    = {Karuwanarint, Piyaporn and Phonrat, Benjaluck and Tungtrongchitr, Anchalee and Suriyaprom, Kanjana and Chuengsamarn, Somlak and Schweigert, Florian J. and Tungtrongchitr, Rungsunn},
  title     = {Vitamin D-binding protein and its polymorphisms as a predictor for metabolic syndrome},
  series = {Biomarkers in medicine},
  volume    = {12},
  journal   = {Biomarkers in medicine},
  number    = {5},
  publisher = {Future Medicine},
  address   = {London},
  issn      = {1752-0363},
  doi       = {10.2217/bmm-2018-0029},
  pages     = {465 -- 473},
  year      = {2018},
  abstract  = {Aim: To investigate the relationship of vitamin D-binding protein (GC) and genetic variation of GC (rs4588, rs7041 and rs2282679) with metabolic syndrome (MetS) in the Thai population. Materials \& methods: GCglobulin concentrations were measured by quantitative western blot analysis in 401 adults. All participants were genotyped using TaqMan allelic discrimination assays. Results: GC-globulin levels were significatly lower in MetS subjects than in control subjects, in which significant negative correlations of GC-globulin levels with systolic blood pressure, glucose and age were found. Male participants who carried the GT genotype for rs4588 showed an increased risk of MetS compared with the GG wild-type (odds ratio: 3.25; p = 0.004). Conclusion: GC-globulin concentrations and variation in GC rs4588 were supported as a risk factor for MetS in Thais.},
  language  = {en}
}
@inproceedings{FunkeuGouadoSchweigertetal.2013,
  author    = {Funkeu, A. D. M. and Gouado, I. and Schweigert, Florian J. and Tchounguep, F.},
  title     = {Serum response to a single dose of dietary carotenoids from steamed, fried and steam-dried squashes pulp (Cucurbita spp)},
  series = {Annals of nutrition \& metabolism : journal of nutrition, metabolic diseases and dietetics ; an official journal of International Union of Nutritional Sciences (IUNS)},
  volume    = {63},
  booktitle = {Annals of nutrition \& metabolism : journal of nutrition, metabolic diseases and dietetics ; an official journal of International Union of Nutritional Sciences (IUNS)},
  number    = {3},
  publisher = {Karger},
  address   = {Basel},
  issn      = {0250-6807},
  pages     = {1501 -- 1501},
  year      = {2013},
  language  = {en}
}
@article{HenzeRailaScholzeetal.2013,
  author    = {Henze, Andrea and Raila, Jens and Scholze, Alexandra and Zidek, Walter and Tepel, Martin and Schweigert, Florian J.},
  title     = {Does N-Acetylcysteine modulate post-translational modifications of transthyretin in hemodialysis patients?},
  series = {Antioxidants \& redox signaling},
  volume    = {19},
  journal   = {Antioxidants \& redox signaling},
  number    = {11},
  publisher = {Liebert},
  address   = {New Rochelle},
  issn      = {1523-0864},
  doi       = {10.1089/ars.2012.5125},
  pages     = {1166 -- 1172},
  year      = {2013},
  abstract  = {It is assumed that effects of the thiol antioxidant N-acetylcysteine (NAC) are mediated by interaction with protein-associated cysteine residues, however, information on protein level in vivo are missing. Therefore, we analyzed NAC-induced modifications of the protein transthyretin (TTR) in plasma of hemodialysis patients in a randomized, placebo-controlled study. TTR was selected due to its low molecular weight and the free cysteine residue in the polypeptide chain, which is known to be extensively modified by formation of mixed disulfides. The intravenous application of NAC during a hemodialysis session resulted in a substantial increase of native TTR from median 15\% (range 8.8\%-30\%) to median 40\% (37-50) and reduction of S-cysteinylated TTR [51\% (44-60) vs. 6.6\% (2.4-10)]. Additionally the pronounced formation of a TTR-NAC adduct was detected. However, all these modifications seemed to be reversible. Additionally, in vitro incubation of plasma with NAC confirmed the in vivo results and indicated that changes in post-translational modification pattern of TTR were a function of NAC concentration. Based on these observations and the essential metabolic and biochemical role of protein-associated cysteine residues we hypothesize that the interaction of NAC with proteins may explain altered protein functions due to modification of cysteine residues. Antioxid. Redox Signal. 19, 1166-1172.},
  language  = {en}
}
@inproceedings{SchweigertRailaMothesetal.2011,
  author    = {Schweigert, Florian J. and Raila, Jens and Mothes, Ralf and Frey, S.},
  title     = {Point of care measurements of Vitamin A in blood and breast milk for low resource settings},
  series = {Annals of nutrition \& metabolism : journal of nutrition, metabolic diseases and dietetics ; an official journal of International Union of Nutritional Sciences (IUNS)},
  volume    = {58},
  booktitle = {Annals of nutrition \& metabolism : journal of nutrition, metabolic diseases and dietetics ; an official journal of International Union of Nutritional Sciences (IUNS)},
  number    = {2},
  publisher = {Karger},
  address   = {Basel},
  issn      = {0250-6807},
  pages     = {382 -- 382},
  year      = {2011},
  language  = {en}
}