Dieses Bild zeigt  Ingrid Weiss

Frau Prof. Dr.

Ingrid Weiss

Abteilungsleiterin
Institut für Biomaterialien und biomolekulare Systeme
Abteilung Biobasierte Materialien

Kontakt

0049 711 685-65080
0049 711 685-55080

Pfaffenwaldring 57
70569 Stuttgart
Deutschland
Raum: 9.544

Publikationen:
  1. Hörning, M., Schertel, A., Schneider, R., Lemloh, M.-L., Schweikert, M.R., Weiss, I.M.: Mineralized scale patterns on the cell periphery of the chrysophyte Mallomonas determined by comparative 3D Cryo-FIB SEM data processing. Journal of Structural Biology. 209, 107403 (2020). https://doi.org/10.1016/j.jsb.2019.10.005.
  2. Weiss, I.M.: Mineral-Chitin Composites in Molluscs. In: Extracellular Sugar-Based Biopolymers Matrices. pp. 57–93. Springer, Cham (2019). https://doi.org/10.1007/978-3-030-12919-4_2.
  3. Eiben, S., Koch, C., Altintoprak, K., Southan, A., Tovar, G., Laschat, S., Weiss, I.M., Wege, C.: Plant virus-based materials for biomedical applications: Trends and prospects. Advanced Drug Delivery Reviews. (2018). https://doi.org/10.1016/j.addr.2018.08.011.
  4. Weiss, I.M., Muth, C., Drumm, R., Kirchner, H.O.K.: Thermal decomposition of the amino acids glycine, cysteine, aspartic acid, asparagine, glutamic acid, glutamine, arginine and histidine. BMC Biophysics. 11, (2018). https://doi.org/10.1186/s13628-018-0042-4.
  5. Lemloh, M.-L., Verch, A., Weiss, I.M.: Aqueous ball milling of nacre constituents facilitates directional self-Assembly of aragonite nanoparticles of the gastropod Haliotis glabra. Journal of the Royal Society Interface. 14, (2017). https://doi.org/10.1098/rsif.2017.0450.
  6. Lemloh, M.-L., Altintoprak, K., Wege, C., Weiss, I.M., Rothenstein, D.: Biogenic and synthetic peptides with oppositely charged amino acids as binding sites for mineralization. Materials. 10, (2017). https://doi.org/10.3390/ma10020119.
  7. Eder, M., Koch, M., Muth, C., Rutz, A., Weiss, I.M.: In vivo modified organic matrix for testing biomineralization-related protein functions in differentiated Dictyostelium on calcite. Journal of Structural Biology. 196, 85–97 (2016). https://doi.org/10.1016/j.jsb.2016.03.015.
  8. Eder, M., Muth, C., Weiss, I.M.: Datasets from a vapor diffusion mineral precipitation protocol for Dictyostelium stalks. Data in Brief. 7, 1396–1404 (2016). https://doi.org/10.1016/j.dib.2016.04.019.
  9. Weber, E., Weiss, I.M., Cölfen, H., Kellermeier, M.: Recombinant perlucin derivatives influence the nucleation of calcium carbonate. CrystEngComm. 18, 8439–8444 (2016). https://doi.org/10.1039/c6ce01878e.
  10. Pohl, A., Weiss, I.M.: Real-time monitoring of calcium carbonate and cationic peptide deposition on carboxylate-SAM using a microfluidic SAW biosensor. Beilstein Journal of Nanotechnology. 5, 1823–1835 (2014). https://doi.org/10.3762/bjnano.5.193.
  11. Lemloh, M.-L., Pohl, A., Weber, E., Zeiger, M., Bauer, P., Weiss, I.M., Schneider, A.S.: Structure-property relationships in mechanically stimulated Sorghum bicolor stalks. Bioinspired Materials. 1, (2014). https://doi.org/10.2478/bima-2014-0001.
  12. Weber, E., Bloch, L., Guth, C., Fitch, A.N., Weiss, I.M., Pokroy, B.: Incorporation of a recombinant biomineralization fusion protein into the crystalline lattice of calcite. Chemistry of Materials. 26, 4925–4932 (2014). https://doi.org/10.1021/cm500450s.
  13. Ghatak, A.S., Koch, M., Guth, C., Weiss, I.M.: Peptide induced crystallization of calcium carbonate on wrinkle patterned substrate: Implications for chitin formation in molluscs. International Journal of Molecular Sciences. 14, 11842–11860 (2013). https://doi.org/10.3390/ijms140611842.
  14. Weiss, I.M., Lüke, F., Eichner, N., Guth, C., Clausen-Schaumann, H.: On the function of chitin synthase extracellular domains in biomineralization. Journal of Structural Biology. 183, 216–225 (2013). https://doi.org/10.1016/j.jsb.2013.04.011.
  15. Weber, E., Guth, C., Weiss, I.M.: GFP Facilitates Native Purification of Recombinant Perlucin Derivatives and Delays the Precipitation of Calcium Carbonate. PLoS ONE. 7, (2012). https://doi.org/10.1371/journal.pone.0046653.
  16. Schneider, A.S., Heiland, B., Peter, N.J., Guth, C., Arzt, E., Weiss, I.M.: Hierarchical super-structure identified by polarized light microscopy, electron microscopy and nanoindentation: Implications for the limits of biological control over the growth mode of abalone sea shells. BMC Biophysics. 5, (2012). https://doi.org/10.1186/2046-1682-5-19.
  17. Tutus, M., Kaufmann, S., Weiss, I.M., Tanaka, M.: Functional coating of porous silica microparticles with native biomembranes towards portable flow-through biochemical microreactors. Advanced Functional Materials. 22, 4873–4878 (2012). https://doi.org/10.1002/adfm.201200570.
  18. Weber, E., Guth, C., Eder, M., Bauer, P., Arzt, E., Weiss, I.M.: Biotechnological mineral composites via vaterite precursors. In: Materials Research Society Symposium Proceedings. pp. 32–38 (2012). https://doi.org/10.1557/opl.2012.1046.
  19. Kaufmann, S., Weiss, I.M., Eckstein, V., Tanaka, M.: Functional expression of Ca2+ dependent mammalian transmembrane gap junction protein Cx43 in slime mold Dictyostelium discoideum. Biochemical and Biophysical Research Communications. 419, 165–169 (2012). https://doi.org/10.1016/j.bbrc.2012.01.126.
  20. Weiss, I.M.: Species-specific shells: Chitin synthases and cell mechanics in molluscs. Zeitschrift für Kristallographie - Crystalline Materials. 227, 723–738 (2012). https://doi.org/10.1524/zkri.2012.1530.
  21. Weiss, I.M., Schmitt, K.P., Kirchner, H.O.: The peacock’s train (Pavo cristatus and Pavo cristatus mut. alba) II. The molecular parameters of feather keratin plasticity. Journal of Experimental Zoology Part A: Ecological Genetics and Physiology. 315 A, 266–273 (2011). https://doi.org/10.1002/jez.671.
  22. Bauer, P., Elbaum, R., Weiss, I.M.: Calcium and silicon mineralization in land plants: Transport, structure and function. Plant Science. 180, 746–756 (2011). https://doi.org/10.1016/j.plantsci.2011.01.019.
  23. Weiss, I.M., Kirchner, H.O.K.: Plasticity of two structural proteins: Alpha-collagen and beta-keratin. Journal of the Mechanical Behavior of Biomedical Materials. 4, 733–743 (2011). https://doi.org/10.1016/j.jmbbm.2011.02.008.
  24. Weiss, I.M.: Biomaterials: Metabolites empowering minerals. Nature Chemical Biology. 7, 192–193 (2011). https://doi.org/10.1038/nchembio.550.
  25. Schönitzer, V., Eichner, N., Clausen-Schaumann, H., Weiss, I.M.: Transmembrane myosin chitin synthase involved in mollusc shell formation produced in Dictyostelium is active. Biochemical and Biophysical Research Communications. 415, 586–590 (2011). https://doi.org/10.1016/j.bbrc.2011.10.109.
  26. Weiss, I.M., Marin, F.: The Role of Enzymes in Biomineralization Processes. (2010). https://doi.org/10.1002/9780470986325.ch3.
  27. Pabisch, S., Puchegger, S., Kirchner, H.O.K., Weiss, I.M., Peterlik, H.: Keratin homogeneity in the tail feathers of Pavo cristatus and Pavo cristatus mut. alba. Journal of Structural Biology. 172, 270–275 (2010). https://doi.org/10.1016/j.jsb.2010.07.003.
  28. Weiss, I.M., Kirchner, H.O.: The peacock’s train (Pavo cristatus and Pavo cristatus mut. alba) I. structure, mechanics, and chemistry of the tail feather coverts. Journal of Experimental Zoology Part A: Ecological Genetics and Physiology. 313 A, 690–703 (2010). https://doi.org/10.1002/jez.641.
  29. Eder, M., Concors, N., Arzt, E., Weiss, I.M.: Micropatterned Polymer surfaces and cellular response of dictyostelium. Advanced Engineering Materials. 12, 405–411 (2010). https://doi.org/10.1002/adem.201000092.
  30. Weiss, I.M., Kirchner, H.O.K.: Quill embroidery: A case study in the mechanics of biological materials. Advanced Engineering Materials. 12, 412–416 (2010). https://doi.org/10.1002/adem.201000105.
  31. Eder, M., Lütz-Meindl, U., Weiss, I.M.: Non-invasive LC-PolScope imaging of biominerals and cell wall anisotropy changes. Protoplasma. 246, 49–64 (2010). https://doi.org/10.1007/s00709-010-0124-x.
  32. Weiss, I.M.: Jewels in the Pearl. ChemBioChem. 11, 297–300 (2010). https://doi.org/10.1002/cbic.200900677.
  33. Weiss, I.M., Kaufmann, S., Heiland, B., Tanaka, M.: Covalent modification of chitin with silk-derivatives acts as an amphiphilic self-organizing template in nacre biomineralisation. Journal of Structural Biology. 167, 68–75 (2009). https://doi.org/10.1016/j.jsb.2009.04.005.
  34. Tanaka, M., Tutus, M., Kaufmann, S., Rossetti, F.F., Schneck, E., Weiss, I.M.: Native supported membranes on planar polymer supports and micro-particle supports. Journal of Structural Biology. 168, 137–142 (2009). https://doi.org/10.1016/j.jsb.2009.05.008.
  35. Weiss, I.M., Marin, F.: The Role of Enzymes in Biomineralization Processes. In: Sigel, A., Sigel, H., and Sigel, R.K.O. (eds.) Biomineralization. pp. 71--126. John Wiley & Sons, Ltd (2008). https://doi.org/10.1002/9780470986325.ch3.
  36. Kaufmann, S., Weiss, I.M., Tanaka, M.: Quantitative in vitro biopolymerization to chitin in native chitosomal membranes supported by silica microparticles. Journal of the American Chemical Society. 129, 10807–10813 (2007). https://doi.org/10.1021/ja072234p.
  37. Schönitzer, V., Weiss, I.M.: The structure of mollusc larval shells formed in the presence of the chitin synthase inhibitor Nikkomycin Z. BMC Structural Biology. 7, (2007). https://doi.org/10.1186/1472-6807-7-71.
  38. Weiss, I.M., Schönitzer, V.: The distribution of chitin in larval shells of the bivalve mollusk Mytilus galloprovincialis. Journal of Structural Biology. 153, 264–277 (2006). https://doi.org/10.1016/j.jsb.2005.11.006.
  39. Weiss, I.M., Schönitzer, V., Eichner, N., Sumper, M.: The chitin synthase involved in marine bivalve mollusk shell formation contains a myosin domain. FEBS Letters. 580, 1846–1852 (2006). https://doi.org/10.1016/j.febslet.2006.02.044.
  40. Weiss, I.M., Tuross, N., Addadi, L., Weiner, S.: Mollusc larval shell formation: Amorphous calcium carbonate is a precursor phase for aragonite. Journal of Experimental Zoology. 293, 478–491 (2002). https://doi.org/10.1002/jez.90004.
  41. Weiner, S., Levi-Kalisman, Y., Raz, S., Weiss, I.M., Addadi, L.: A basic strategy for biomineralization: Taking advantage of disorder. Microscopy and Microanalysis. 8, 164–165 (2002).
  42. Weiss, I.M., Renner, C., Strigl, M.G., Fritz, M.: A simple and reliable method for the determination and localization of chitin in abalone nacre. Chemistry of Materials. 14, 3252–3259 (2002). https://doi.org/10.1021/cm001217v.
  43. Weiss, I.M., Göhring, W., Fritz, M., Mann, K.: Perlustrin, a Haliotis laevigata (abalone) nacre protein, is homologous to the insulin-like growth factor binding protein N-terminal module of vertebrates. Biochemical and Biophysical Research Communications. 285, 244–249 (2001). https://doi.org/10.1006/bbrc.2001.5170.
  44. Weiss, I.M., Kaufmann, S., Mann, K., Fritz, M.: Purification and characterization of perlucin and perlustrin, two new proteins from the shell of the mollusc Haliotis laevigata. Biochemical and Biophysical Research Communications. 267, 17–21 (2000). https://doi.org/10.1006/bbrc.1999.1907.
  45. Kacher, C.M., Weiss, I.M., Stewart, R.J., Schmidt, C.F., Hansma, P.K., Radmacher, M., Fritz, M.: Imaging microtubules and kinesin decorated microtubules using tapping mode atomic force microscopy in fluids. European Biophysics Journal. 28, 611–620 (2000). https://doi.org/10.1007/s002490050001.
  46. Mann, K., Weiss, I.M., André, S., Gabius, H.-J., Fritz, M.: The amino-acid sequence of the abalone (Haliotis laevigata) nacre protein perlucin: Detection of a functional C-type lectin domain with galactose/mannose specificity. European Journal of Biochemistry. 267, 5257–5264 (2000). https://doi.org/10.1046/j.1432-1327.2000.01602.x.
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