@article{KoshkinaWestmeierLangetal.2016, author = {Koshkina, Olga and Westmeier, Dana and Lang, Thomas and Bantz, Christoph and Hahlbrock, Angelina and W{\"u}rth, Christian and Resch-Genger, Ute and Braun, Ulrike and Thiermann, Raphael and Weise, Christoph and Eravci, Murat and Mohr, Benjamin and Schlaad, Helmut and Stauber, Roland H. and Docter, Dominic and Bertin, Annabelle and Maskos, Michael}, title = {Tuning the Surface of Nanoparticles: Impact of Poly(2-ethyl-2-oxazoline) on Protein Adsorption in Serum and Cellular Uptake}, series = {Macromolecular bioscience}, volume = {16}, journal = {Macromolecular bioscience}, publisher = {Wiley-VCH}, address = {Weinheim}, issn = {1616-5187}, doi = {10.1002/mabi.201600074}, pages = {1287 -- 1300}, year = {2016}, abstract = {Due to the adsorption of biomolecules, the control of the biodistribution of nanoparticles is still one of the major challenges of nanomedicine. Poly(2-ethyl-2-oxazoline) (PEtOx) for surface modification of nanoparticles is applied and both protein adsorption and cellular uptake of PEtOxylated nanoparticles versus nanoparticles coated with poly(ethylene glycol) (PEG) and non-coated positively and negatively charged nanoparticles are compared. Therefore, fluorescent poly(organosiloxane) nanoparticles of 15 nm radius are synthesized, which are used as a scaffold for surface modification in a grafting onto approach. With multi-angle dynamic light scattering, asymmetrical flow field-flow fractionation, gel electrophoresis, and liquid chromatography-mass spectrometry, it is demonstrated that protein adsorption on PEtOxylated nanoparticles is extremely low, similar as on PEGylated nanoparticles. Moreover, quantitative microscopy reveals that PEtOxylation significantly reduces the non-specific cellular uptake, particularly by macrophage-like cells. Collectively, studies demonstrate that PEtOx is a very effective alternative to PEG for stealth modification of the surface of nanoparticles.}, language = {en} } @article{ComparotMossKoettingStettleretal.2010, author = {Comparot-Moss, Sylviane and Koetting, Oliver and Stettler, Michaela and Edner, Christoph and Graf, Alexander and Weise, Sean E. and Streb, Sebastian and Lue, Wei-Ling and MacLean, Daniel and Mahlow, Sebastian and Ritte, Gerhard and Steup, Martin and Chen, Jychian and Zeeman, Samuel C. and Smith, Alison M.}, title = {A putative phosphatase, LSF1, is required for normal starch turnover in Arabidopsis leaves}, issn = {0032-0889}, doi = {10.1104/pp.109.148981}, year = {2010}, abstract = {A putative phosphatase, LSF1 (for LIKE SEX4; previously PTPKIS2), is closely related in sequence and structure to STARCH-EXCESS4 (SEX4), an enzyme necessary for the removal of phosphate groups from starch polymers during starch degradation in Arabidopsis (Arabidopsis thaliana) leaves at night. We show that LSF1 is also required for starch degradation: lsf1 mutants, like sex4 mutants, have substantially more starch in their leaves than wild-type plants throughout the diurnal cycle. LSF1 is chloroplastic and is located on the surface of starch granules. lsf1 and sex4 mutants show similar, extensive changes relative to wild-type plants in the expression of sugar-sensitive genes. However, although LSF1 and SEX4 are probably both involved in the early stages of starch degradation, we show that LSF1 neither catalyzes the same reaction as SEX4 nor mediates a sequential step in the pathway. Evidence includes the contents and metabolism of phosphorylated glucans in the single mutants. The sex4 mutant accumulates soluble phospho- oligosaccharides undetectable in wild-type plants and is deficient in a starch granule-dephosphorylating activity present in wild-type plants. The lsf1 mutant displays neither of these phenotypes. The phenotype of the lsf1/sex4 double mutant also differs from that of both single mutants in several respects. We discuss the possible role of the LSF1 protein in starch degradation.}, language = {en} } @misc{SrivastavaMurugaiyanGarciaetal.2020, author = {Srivastava, Abhishek and Murugaiyan, Jayaseelan and Garcia, Juan A. L. and De Corte, Daniele and Hoetzinger, Matthias and Eravci, Murat and Weise, Christoph and Kumar, Yadhu and Roesler, Uwe and Hahn, Martin W. and Grossart, Hans-Peter}, title = {Combined Methylome, Transcriptome and Proteome Analyses Document Rapid Acclimatization of a Bacterium to Environmental Changes}, series = {Postprints der Universit{\"a}t Potsdam : Mathematisch Naturwissenschaftliche Reihe}, journal = {Postprints der Universit{\"a}t Potsdam : Mathematisch Naturwissenschaftliche Reihe}, number = {1011}, issn = {1866-8372}, doi = {10.25932/publishup-48199}, url = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus4-481993}, pages = {23}, year = {2020}, abstract = {Polynucleobacter asymbioticus strain QLW-P1DMWA-1T represents a group of highly successful heterotrophic ultramicrobacteria that is frequently very abundant (up to 70\% of total bacterioplankton) in freshwater habitats across all seven continents. This strain was originally isolated from a shallow Alpine pond characterized by rapid changes in water temperature and elevated UV radiation due to its location at an altitude of 1300 m. To elucidate the strain's adjustment to fluctuating environmental conditions, we recorded changes occurring in its transcriptomic and proteomic profiles under contrasting experimental conditions by simulating thermal conditions in winter and summer as well as high UV irradiation. To analyze the potential connection between gene expression and regulation via methyl group modification of the genome, we also analyzed its methylome. The methylation pattern differed between the three treatments, pointing to its potential role in differential gene expression. An adaptive process due to evolutionary pressure in the genus was deduced by calculating the ratios of non-synonymous to synonymous substitution rates for 20 Polynucleobacter spp. genomes obtained from geographically diverse isolates. The results indicate purifying selection.}, language = {en} } @article{SrivastavaMurugaiyanGarciaetal.2020, author = {Srivastava, Abhishek and Murugaiyan, Jayaseelan and Garcia, Juan A. L. and De Corte, Daniele and Hoetzinger, Matthias and Eravci, Murat and Weise, Christoph and Kumar, Yadhu and Roesler, Uwe and Hahn, Martin W. and Grossart, Hans-Peter}, title = {Combined Methylome, Transcriptome and Proteome Analyses Document Rapid Acclimatization of a Bacterium to Environmental Changes}, series = {Frontiers in Microbiology}, volume = {11}, journal = {Frontiers in Microbiology}, publisher = {Frontiers Media}, address = {Lausanne}, issn = {1664-302X}, doi = {10.3389/fmicb.2020.544785}, pages = {21}, year = {2020}, abstract = {Polynucleobacter asymbioticus strain QLW-P1DMWA-1T represents a group of highly successful heterotrophic ultramicrobacteria that is frequently very abundant (up to 70\% of total bacterioplankton) in freshwater habitats across all seven continents. This strain was originally isolated from a shallow Alpine pond characterized by rapid changes in water temperature and elevated UV radiation due to its location at an altitude of 1300 m. To elucidate the strain's adjustment to fluctuating environmental conditions, we recorded changes occurring in its transcriptomic and proteomic profiles under contrasting experimental conditions by simulating thermal conditions in winter and summer as well as high UV irradiation. To analyze the potential connection between gene expression and regulation via methyl group modification of the genome, we also analyzed its methylome. The methylation pattern differed between the three treatments, pointing to its potential role in differential gene expression. An adaptive process due to evolutionary pressure in the genus was deduced by calculating the ratios of non-synonymous to synonymous substitution rates for 20 Polynucleobacter spp. genomes obtained from geographically diverse isolates. The results indicate purifying selection.}, language = {en} }