A5012502174- Prion Diseases and Protein Misfolding
- Marine Biology and Environmental Chemistry
- Neurological diseases and metabolism
- Enzyme Structure and Function
- Polymer Surface Interaction Studies
- Protein Structure and Dynamics
- Escherichia coli research studies
- Bone and Dental Protein Studies
- Knee injuries and reconstruction techniques
- Catalytic Alkyne Reactions
- Immune Response and Inflammation
- Trace Elements in Health
- Protein Hydrolysis and Bioactive Peptides
- Immunotherapy and Immune Responses
- Alzheimer's disease research and treatments
- biodegradable polymer synthesis and properties
- Heat shock proteins research
- Calcium Carbonate Crystallization and Inhibition
- Fungal and yeast genetics research
- Trauma, Hemostasis, Coagulopathy, Resuscitation
- Synthetic Organic Chemistry Methods
- Aquaculture Nutrition and Growth
- Chemical Synthesis and Analysis
- Microplastics and Plastic Pollution
- Collagen: Extraction and Characterization
University of Bayreuth
2008-2019
Technical University of Munich
2005-2006
Institute of Medical Microbiology and Hygiene
2006
Cationic triphenylphosphinegold(I) complexes are excellent catalysts for a cascade reaction of propargyl-Claisen rearrangement and heterocyclization to synthesize tri- tetrasubstituted furans. Starting from easily accessed propargyl vinyl ethers, the furans obtained in 72−99% yield.
Prions are infectious, self-propagating amyloid-like protein aggregates of mammals and fungi. We have studied aggregation propensities a yeast prion domain in cell culture to gain insights into general mechanisms replication mammalian cells. Here, we report the artificial transmission across phylogenetic kingdom. HA epitope-tagged Sup35p NM was stably expressed murine neuroblastoma Although cytosolically NM-HA remained soluble, addition fibrils bacterially produced Sup35NM medium efficiently...
Prions are self-templating protein conformers that replicate by recruitment and conversion of homotypic proteins into growing aggregates. Originally identified as causative agents transmissible spongiform encephalopathies, increasing evidence now suggests prion-like phenomena more common in nature than previously anticipated. In contrast to fungal prions the cytoplasm, propagation mammalian derived from precursor PrP is confined cell membrane or endocytic vesicles. Here we demonstrate...
In mammalian prion diseases, an abnormally folded, aggregated form of the protein (PrP(Sc)) appears to catalyze a conformational switch its cellular isoform (PrP(C)) state. A similar prion-like phenomenon has been reported for Saccharomyces cerevisiae translation termination factor Sup35p that can adopt self-propagating conformation. We have compared aggregation propensities chimeric proteins derived from domain NM and PrP in vitro cytosol cells. Sup35p-NM displayed strikingly different...
In order to deal with the dynamic ocean environment, blue mussels adhere various surfaces via their collagenous byssal threads. PTMP1 (proximal thread matrix protein 1) is one identified residing in proximal and capable of collagen binding. Its sequence comprises two von Willebrand factor type A-like repeats. characterize structure domain architecture PTMP1, recombinant was crystallized by vapour diffusion. The obtained crystals diffracted 1.95 Å resolution belonged space group P2₁,...
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