@article{HoieSjoholmGuldstrandetal.2006,
  author    = {Hoie, Lars H. and Sjoholm, Ake and Guldstrand, Marie and Zunft, Hans-Joachim Franz and Lueder, Wolfgang and Graubaum, Hans-Joachim and Gr{\"u}nwald, J{\"o}rg},
  title     = {Ultra heat treatment destroys cholesterol-lowering effect of soy protein},
  series = {International journal of food sciences and nutrition},
  volume    = {57},
  journal   = {International journal of food sciences and nutrition},
  publisher = {Taylor \& Francis},
  address   = {Abingdon},
  issn      = {0963-7486},
  doi       = {10.1080/09637480601009059},
  pages     = {512 -- 519},
  year      = {2006},
  abstract  = {A randomized, placebo-controlled, double-blind clinical study was performed to investigate the dose-dependent response of serum cholesterol after consuming an ultra-heat-treated milk containing a soy protein preparation. Eighty hypercholesterolemic subjects were assigned to one of four study groups receiving 12.5 or 25 g soy protein (active treatment) or casein (placebo) daily over a period of 4 weeks. The trial substances were provided as ready-made, ultra-heated milk preparations. Before and after the treatment, serum concentrations of total, low-density lipoprotein, and high-density lipoprotein cholesterol were determined. Unexpectedly, at the end of the study, low-density lipoprotein cholesterol concentrations were significantly increased compared with baseline in all study groups. The magnitude of this increase (17 - 19\%) was similar in all active and placebo study groups. Soy protein supplements previously shown to be effective in reducing serum cholesterol had in this study no such lipid-lowering effect after ultra heat treatment.},
  language  = {en}
}
@article{SchweigertGerickeWolframetal.2006,
  author    = {Schweigert, Florian J. and Gericke, Beate and Wolfram, Wiebke and Kaisers, Udo and Dudenhausen, Joachim W.},
  title     = {Peptide and protein profiles in serum and follicular fluid of women undergoing IVF},
  series = {Human reproduction},
  volume    = {21},
  journal   = {Human reproduction},
  number    = {11},
  publisher = {Univ. Press},
  address   = {Oxford},
  issn      = {0268-1161},
  doi       = {10.1093/humrep/del257},
  pages     = {2960 -- 2968},
  year      = {2006},
  abstract  = {BACKGROUND: Proteins and peptides in human follicular fluid originate from plasma or are produced by follicular structures. Compositional changes reflect oocyte maturation and can be used as diagnostic markers. The aim of the study was to determine protein and peptide profiles in paired serum and follicular fluid samples from women undergoing IVF. METHODS: Surface-enhanced laser desorption and ionization-time of flight-mass spectrometry (SELDI-TOF-MS) was used to obtain characteristic protein pattern. RESULTS: One hundred and eighty-six individual MS signals were obtained from a combination of enrichment on strong anion exchanger (110), weak cation exchanger (52) and normal phase surfaces (24). On the basis of molecular masses, isoelectric points and immunoreactivety, four signals were identified as haptoglobin (alpha(1)- and alpha(2)-chain), haptoglobin 1 and transthyretin (TTR). Immunological and MS characteristics of the TTR : retinol-binding protein (RBP) transport complex revealed no microheterogeneity differences between serum and follicular fluid. Discriminatory patterns arising from decision-tree-based classification and regression analysis distinguished between serum and follicular fluid with a sensitivity and specificity of 100\%. CONCLUSIONS: Quantitative and qualitative differences indicate selective transport processes rather than mere filtration across the blood-follicle barrier. Identified proteins as well as characteristic peptide and/or protein signatures might emerge as potential candidates for diagnostic markers of follicle and/or oocyte maturation and thus oocyte quality.},
  language  = {en}
}
@article{HenzeHomannRohnetal.2016,
  author    = {Henze, Andrea and Homann, Thomas and Rohn, Isabelle and Aschner, Michael A. and Link, Christopher D. and Kleuser, Burkhard and Schweigert, Florian J. and Schwerdtle, Tanja and Bornhorst, Julia},
  title     = {Caenorhabditis elegans as a model system to study post-translational modifications of human transthyretin},
  series = {Scientific reports},
  volume    = {6},
  journal   = {Scientific reports},
  publisher = {Nature Publishing Group},
  address   = {London},
  issn      = {2045-2322},
  doi       = {10.1038/srep37346},
  pages     = {12},
  year      = {2016},
  abstract  = {The visceral protein transthyretin (TTR) is frequently affected by oxidative post-translational protein modifications (PTPMs) in various diseases. Thus, better insight into structure-function relationships due to oxidative PTPMs of TTR should contribute to the understanding of pathophysiologic mechanisms. While the in vivo analysis of TTR in mammalian models is complex, time- and resource-consuming, transgenic Caenorhabditis elegans expressing hTTR provide an optimal model for the in vivo identification and characterization of drug-mediated oxidative PTPMs of hTTR by means of matrix assisted laser desorption/ionization - time of flight - mass spectrometry (MALDI-TOF-MS). Herein, we demonstrated that hTTR is expressed in all developmental stages of Caenorhabditis elegans, enabling the analysis of hTTR metabolism during the whole life-cycle. The suitability of the applied model was verified by exposing worms to D-penicillamine and menadione. Both drugs induced substantial changes in the oxidative PTPM pattern of hTTR. Additionally, for the first time a covalent binding of both drugs with hTTR was identified and verified by molecular modelling.},
  language  = {en}
}