Zobrazeno 1 - 10
of 48
pro vyhledávání: '"Eva M. Egelseer"'
Autor:
Magdalena Pleschberger, Florian Hildner, Harald F. Mayer, Nicola Gelbmann, Dominik Rünzler, Uwe B. Sleytr, Eva M. Egelseer
Publikováno v:
Archives of Microbiology. 195:323-337
The S-layer protein SbpA of Lysinibacillus sphaericus CCM 2177 assembles into a square (p4) lattice structure and recognizes a pyruvylated secondary cell wall polymer (SCWP) as the proper anchoring structure to the rigid cell wall layer. Sequencing o
Autor:
Tea Pavkov-Keller, Walter Keller, Manfred Tesarz, Anđela Đordić, Eva M. Egelseer, Uwe B. Sleytr
Publikováno v:
Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Three different truncation constructs of the S-layer protein SbsC containing domains crucial for self-assembly could be crystallized. Native data were collected for the three crystal forms from crystals that diffracted to 3.4, 2.8 and 1.5 Å resoluti
Publikováno v:
Current Opinion in Biotechnology
Highlights ► Bacterial S-layer proteins have a great potential as nanoscale building blocks. ► By genetic engineering, functional domains were incorporated into S-layers. ► Recombinant fusion proteins were functional and maintained self-assembl
Autor:
Eva M. Egelseer, Nicola Ilk, Judith Ferner-Ortner-Bleckmann, Angelika Schrems, Bernhard Schuster, Uwe B. Sleytr
Publikováno v:
Biointerphases. 6:63-72
Methods for organizing functional materials at the nanometer scale are essential for the development of novel fabrication techniques. One of the most relevant areas of research in nanobiotechnology concerns technological utilization of self-assembly
Autor:
Eva M. Egelseer, Judith Ferner-Ortner-Bleckmann, Christoph Mader, Tea Pavkov, Walter Keller, Nicola Ilk, Carina Huber-Gries, Uwe B. Sleytr
Publikováno v:
Molecular Microbiology. 72:1448-1461
The complete nucleotide sequence encoding the high-molecular-mass amylase (HMMA) of Geobacillus stearothermophilus ATCC 12980 was established by PCR techniques. Based on the hmma gene sequence, the full-length rHMMA, four N- or C-terminal rHMMA trunc
Autor:
Christine Völlenkle, Uwe B. Sleytr, Eva M. Egelseer, Dietmar Pum, Nicola Ilk, Birgit Kainz, Helga Badelt-Lichtblau
Publikováno v:
Bioconjugate Chemistry. 20:895-903
The mesophilic organism Lysinibacillus sphaericus CCM 2177 produces the surface (S)-layer protein SbpA, which after secretion completely covers the cell surface with a crystalline array exhibiting square lattice symmetry. Because of its excellent in
Publikováno v:
Structure. 16(8):1226-1237
Summary Surface layers (S-layers) comprise the outermost cell envelope component of most archaea and many bacteria. Here we present the structure of the bacterial S-layer protein SbsC from Geobacillus stearothermophilus , showing a very elongated and
Autor:
Marianne Gerstmayr, Nicola Ilk, Irma Schabussova, Uwe B. Sleytr, Eva M. Egelseer, Beatrice Jahn-Schmid, Barbara Bohle, Christof Ebner
Publikováno v:
The Journal of Immunology. 179:7270-7275
An ideal vaccine for allergen-specific immunotherapy of type I allergies should display reduced mediator-releasing capacity, induce maturation of APC, and modify the disease-eliciting Th2-dominated allergen-specific response to a more physiological r
Publikováno v:
FEBS Journal. 274:323-334
Crystalline arrays of protein or glycoprotein subunits forming surface layers (S-layers) are the most common outermost envelope components of prokaryotic organisms (archaea and bacteria). The wealth of information on the structure, chemistry, genetic
Publikováno v:
Microelectronic Engineering. 83:1589-1593
Crystalline bacterial cell surface layer (S-layer) proteins represent the outermost envelope component of many bacteria and archaea. Isolated S-layer proteins frequently show the ability to recrystallize into monomolecular protein lattices on solid s