@article{LehnhardtLietzBaumann1999,
  author    = {Lehnhardt, Lothar and Lietz, Alexander and Baumann, Guido},
  title     = {Mass spectrometry of ubiquitin-ribulose-1,5-bisphosphate carboxylase/oxygenase large-subunit conjugates in callus cultures of sugar beet (Beta vulgaris L.)},
  year      = {1999},
  language  = {en}
}
@article{HinzLehnhardtZakrzewskietal.2012,
  author    = {Hinz, Justyna and Lehnhardt, Lothar and Zakrzewski, Silke and Zhang, Gong and Ignatova, Zoya},
  title     = {Polyglutamine expansion alters the dynamics and molecular architecture of aggregates in dentatorubropallidoluysian atrophy},
  series = {The journal of biological chemistry},
  volume    = {287},
  journal   = {The journal of biological chemistry},
  number    = {3},
  publisher = {American Society for Biochemistry and Molecular Biology},
  address   = {Bethesda},
  issn      = {0021-9258},
  doi       = {10.1074/jbc.M111.318915},
  pages     = {2068 -- 2078},
  year      = {2012},
  abstract  = {Preferential accumulation of mutant proteins in the nucleus has been suggested to be the molecular culprit that confers cellular toxicity in the neurodegenerative disorders caused by polyglutamine (polyQ) expansion. Here, we use dynamic imaging approaches, orthogonal cross-seeding, and composition analysis to examine the dynamics and structure of nuclear and cytoplasmic inclusions of atrophin-1, implicated in dentatorubropallidoluysian atrophy, a polyQ-based disease with complex clinical features. Our results reveal a large heterogeneity in the dynamics of the nuclear inclusions compared with the compact and immobile cytoplasmic aggregates. At least two types of inclusions of expanded atrophin-1 with different mobility of the molecular species and ability to exchange with the surrounding monomer pool coexist in the nucleus. Intriguingly, the enrichment of nuclear inclusions with slow dynamics parallels changes in the aggregate core architecture that are dominated by the polyQ stretch. We propose that the observed complexity in the dynamics of the nuclear inclusions provides a molecular explanation for the enhanced cellular toxicity of the nuclear aggregates in polyQ-based neurodegeneration.},
  language  = {en}
}
@article{LehnhardtPufeBaumanetal.2004,
  author    = {Lehnhardt, Lothar and Pufe, Heidrun and Bauman, Ingrid and Baumann, Guido},
  title     = {Responses of chloroplast thylakoid composition to low temperature and high light stress in callus cultures and in leaves of sugar beet},
  year      = {2004},
  language  = {en}
}
@article{FedyuninLehnhardtBoehmeretal.2012,
  author    = {Fedyunin, Ivan and Lehnhardt, Lothar and B{\"o}hmer, Nadine and Kaufmann, Paul and Zhang, Gong and Ignatov, Zoya},
  title     = {tRNA concentration fine tunes protein solubility},
  year      = {2012},
  language  = {en}
}
@article{FedyuninLehnhardtBoehmeretal.2012,
  author    = {Fedyunin, Ivan and Lehnhardt, Lothar and B{\"o}hmer, Nadine and Kaufmann, Paul and Zhang, Gong and Ignatova, Zoya},
  title     = {tRNA concentration fine tunes protein solubility},
  series = {FEBS letters : the journal for rapid publication of short reports in molecular biosciences},
  volume    = {586},
  journal   = {FEBS letters : the journal for rapid publication of short reports in molecular biosciences},
  number    = {19},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {0014-5793},
  doi       = {10.1016/j.febslet.2012.07.012},
  pages     = {3336 -- 3340},
  year      = {2012},
  abstract  = {Clusters of codons pairing to low-abundance tRNAs synchronize the translation with co-translational folding of single domains in multidomain proteins. Although proven with some examples, the impact of the ribosomal speed on the folding and solubility on a global, cell-wide level remains elusive. Here we show that upregulation of three low-abundance tRNAs in Escherichia coil increased the aggregation propensity of several cellular proteins as a result of an accelerated elongation rate. Intriguingly, alterations in the concentration of the natural tRNA pool compromised the solubility of various chaperones consequently rendering the solubility of some chaperone-dependent proteins.},
  language  = {en}
}
@article{KummerLehnhardtKlopfer1992,
  author    = {Kummer, Volker and Lehnhardt, Lothar and Klopfer, Klaus},
  title     = {Untersuchungen zur Fremdbesatzproblematik bei 5 Gerstensorten mittels {\"A}hrennachkommenschaftspr{\"u}fung und Hordeinelektrophorese},
  year      = {1992},
  language  = {de}
}