@article{WhiteheadOehlschlaegerAlmajhdietal.2014,
  author    = {Whitehead, Mark and {\"O}hlschl{\"a}ger, Peter and Almajhdi, Fahad N. and Alloza, Leonor and Marz{\´a}bal, Pablo and Meyers, Ann E. and Hitzeroth, Inga I. and Rybicki, Edward P.},
  title     = {Human papillomavirus (HPV) type 16 E7 protein bodies cause tumour regression in mice},
  series = {BMC cancer},
  journal   = {BMC cancer},
  number    = {14:367},
  publisher = {BioMed Central},
  address   = {London},
  issn      = {1471-2407},
  doi       = {10.1186/1471-2407-14-367},
  pages     = {1 -- 15},
  year      = {2014},
  language  = {en}
}
@article{KueppersSteffenHellmuthetal.2014,
  author    = {K{\"u}ppers, Tobias and Steffen, Victoria and Hellmuth, Hendrik and O'Connell, Timothy and Bongaerts, Johannes and Maurer, Karl-Heinz and Wiechert, Wolfgang},
  title     = {Developing a new production host from a blueprint: Bacillus pumilus as an industrial enzyme producer},
  series = {Microbial cell factories},
  volume    = {13},
  journal   = {Microbial cell factories},
  publisher = {BioMed Central},
  address   = {London},
  issn      = {1475-2859 (E-Journal)},
  doi       = {10.1186/1475-2859-13-46},
  pages     = {Article No. 46},
  year      = {2014},
  language  = {en}
}
@article{BassamDigelHescheleretal.2013,
  author    = {Bassam, Rasha and Digel, Ilya and Hescheler, J{\"u}rgen and Temiz Artmann, Ayseg{\"u}l and Artmann, Gerhard},
  title     = {Effects of spermine NONOate and ATP on protein aggregation: light scattering evidences},
  series = {BMC Biophysics},
  journal   = {BMC Biophysics},
  publisher = {BioMed Central},
  address   = {London},
  isbn      = {2046-1682},
  url       = {http://nbn-resolving.de/10.1186/2046-1682-6-1},
  pages     = {1 -- 14},
  year      = {2013},
  language  = {en}
}
@article{WiegandDietrichHerteletal.2013,
  author    = {Wiegand, Sandra and Dietrich, Sascha and Hertel, Robert and Bongaerts, Johannes and Evers, Stefan and Volland, Sonja and Daniel, Rolf and Liesegang, Heiko},
  title     = {RNA-Seq of Bacillus licheniformis: active regulatory RNA features expressed within a productive fermentation},
  series = {BMC genomics},
  volume    = {Vol. 14},
  journal   = {BMC genomics},
  publisher = {BioMed Central},
  address   = {London},
  issn      = {1471-2164},
  pages     = {667},
  year      = {2013},
  language  = {en}
}
@article{WiegandVoigtAlbrechtetal.2013,
  author    = {Wiegand, Sandra and Voigt, Birgit and Albrecht, Dirk and Bongaerts, Johannes and Evers, Stefan and Hecker, Michael and Daniel, Rolf and Liesegang, Heiko},
  title     = {Fermentation stage-dependent adaptations of Bacillus licheniformis during enzyme production},
  series = {Microbial Cell Factories},
  volume    = {12},
  journal   = {Microbial Cell Factories},
  publisher = {Biomed Central},
  address   = {London},
  issn      = {1475-2859},
  doi       = {10.1186/1475-2859-12-120},
  pages     = {120},
  year      = {2013},
  language  = {en}
}
@article{BassamHeschelerTemizArtmannetal.2012,
  author    = {Bassam, Rasha and Hescheler, J{\"u}rgen and Temiz Artmann, Ayseg{\"u}l and Artmann, Gerhard and Digel, Ilya},
  title     = {Effects of spermine NONOate and ATP on the thermal stability of hemoglobin},
  series = {BMC Biophysics},
  volume    = {5},
  journal   = {BMC Biophysics},
  publisher = {BioMed Central},
  address   = {London},
  issn      = {2046-1682},
  doi       = {10.1186/2046-1682-5-16},
  pages     = {Art. 16},
  year      = {2012},
  abstract  = {Background Minor changes in protein structure induced by small organic and inorganic molecules can result in significant metabolic effects. The effects can be even more profound if the molecular players are chemically active and present in the cell in considerable amounts. The aim of our study was to investigate effects of a nitric oxide donor (spermine NONOate), ATP and sodium/potassium environment on the dynamics of thermal unfolding of human hemoglobin (Hb). The effect of these molecules was examined by means of circular dichroism spectrometry (CD) in the temperature range between 25°C and 70°C. The alpha-helical content of buffered hemoglobin samples (0.1 mg/ml) was estimated via ellipticity change measurements at a heating rate of 1°C/min. Results Major results were: 1) spermine NONOate persistently decreased the hemoglobin unfolding temperature T u irrespectively of the Na + /K + environment, 2) ATP instead increased the unfolding temperature by 3°C in both sodium-based and potassium-based buffers and 3) mutual effects of ATP and NO were strongly influenced by particular buffer ionic compositions. Moreover, the presence of potassium facilitated a partial unfolding of alpha-helical structures even at room temperature. Conclusion The obtained data might shed more light on molecular mechanisms and biophysics involved in the regulation of protein activity by small solutes in the cell.},
  language  = {en}
}