@article{RaketteDonatOhlsenetal.2012,
  author    = {Rakette, Sonja and Donat, Stefanie and Ohlsen, Knut and Stehle, Thilo},
  title     = {Structural Analysis of Staphylococcus aureus Serine/Threonine Kinase PknB},
  series = {PLoS One},
  volume    = {7},
  journal   = {PLoS One},
  number    = {6},
  doi       = {10.1371/journal.pone.0039136},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-135369},
  pages     = {e39136},
  year      = {2012},
  abstract  = {Effective treatment of infections caused by the bacterium Staphylococcus aureus remains a worldwide challenge, in part due to the constant emergence of new strains that are resistant to antibiotics. The serine/threonine kinase PknB is of particular relevance to the life cycle of S. aureus as it is involved in the regulation of purine biosynthesis, autolysis, and other central metabolic processes of the bacterium. We have determined the crystal structure of the kinase domain of PknB in complex with a non-hydrolyzable analog of the substrate ATP at 3.0 angstrom resolution. Although the purified PknB kinase is active in solution, it crystallized in an inactive, autoinhibited state. Comparison with other bacterial kinases provides insights into the determinants of catalysis, interactions of PknB with ligands, and the pathway of activation.},
  language  = {en}
}
@article{MakoahNigelArndtPradel2012,
  author    = {Makoah Nigel, Animake and Arndt, Hans-Dieter and Pradel, Gabriele},
  title     = {The proteasome of malaria parasites: A multi-stage drug target for chemotherapeutic intervention?},
  series = {International Journal for Parasitology: Drugs and Drug Resistance},
  volume    = {2},
  journal   = {International Journal for Parasitology: Drugs and Drug Resistance},
  doi       = {10.1016/j.ijpddr.2011.12.001},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-137777},
  pages     = {1-10},
  year      = {2012},
  abstract  = {The ubiquitin/proteasome system serves as a regulated protein degradation pathway in eukaryotes, and is involved in many cellular processes featuring high protein turnover rates, such as cell cycle control, stress response and signal transduction. In malaria parasites, protein quality control is potentially important because of the high replication rate and the rapid transformations of the parasite during life cycle progression. The proteasome is the core of the degradation pathway, and is a major proteolytic complex responsible for the degradation and recycling of non-functional ubiquitinated proteins. Annotation of the genome for Plasmodium falciparum, the causative agent of malaria tropica, revealed proteins with similarity to human 26S proteasome subunits. In addition, a bacterial ClpQ/hslV threonine peptidase-like protein was identified. In recent years several independent studies indicated an essential function of the parasite proteasome for the liver, blood and transmission stages. In this review, we compile evidence for protein recycling in Plasmodium parasites and discuss the role of the 26S proteasome as a prospective multi-stage target for antimalarial drug discovery programs.},
  language  = {en}
}