MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it Tetracysteine-tagged prion protein allows discrimination between the native and converted forms. Tetracysteine-tagged prion protein allows discrimination between the native and converted forms. FEBS J. (1742-464X) 2010 imex curation Gaspersic J., Hafner-Bratkovic I., Stephan M., Veranic P., Bencina M., Vorberg I., Jerala R. Only protein-protein interactions in vitro In vitro fluorescence fluorescence technology fluorescence predetermined predetermined participant predetermined Gaspersic J., Hafner-Bratkovic I., Stephan M., Veranic P., Bencina M., Vorberg I., Jerala R. FEBS J. (1742-464X) 2010 Only protein-protein interactions imex curation Tetracysteine-tagged prion protein allows discrimination between the native and converted forms. Tetracysteine-tagged prion protein allows discrimination between the native and converted forms. FEBS J. (1742-464X) 2010 imex curation Gaspersic J., Hafner-Bratkovic I., Stephan M., Veranic P., Bencina M., Vorberg I., Jerala R. Only protein-protein interactions in vitro In vitro electron microscopy electron microscopy Electron crystallography Electron cryomicroscopy Electron crystallography Electron cryomicroscopy predetermined predetermined participant predetermined Gaspersic J., Hafner-Bratkovic I., Stephan M., Veranic P., Bencina M., Vorberg I., Jerala R. FEBS J. (1742-464X) 2010 Only protein-protein interactions imex curation Tetracysteine-tagged prion protein allows discrimination between the native and converted forms. Tetracysteine-tagged prion protein allows discrimination between the native and converted forms. FEBS J. (1742-464X) 2010 imex curation Gaspersic J., Hafner-Bratkovic I., Stephan M., Veranic P., Bencina M., Vorberg I., Jerala R. Only protein-protein interactions in vitro In vitro cd circular dichroism CD CD cd predetermined predetermined participant predetermined Gaspersic J., Hafner-Bratkovic I., Stephan M., Veranic P., Bencina M., Vorberg I., Jerala R. FEBS J. (1742-464X) 2010 Only protein-protein interactions imex curation prio_mouse Major prion protein PrP27-30 PrP33-35C Prnp Prn-p Prp protein protein mouse Mus musculus Mouse MANLGYWLLALFVTMWTDVGLCKKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGTWGQPHGGGWGQPHGGSWGQPHGGSWGQPHGGGWGQGGGTHNQWNKPSKPKTNLKHVAGAAAAGAVVGGLGGYMLGSAMSRPMIHFGNDWEDRYYRENMYRYPNQVYYRPVDQYSNQNNFVHDCVNITIKQHTVTTTTKGENFTETDVKMMERVVEQMCVTQYQKESQAYYDGRRSSSTVLFSSPPVILLISFLIFLIVG DIP protein P04925 original sequence version: 157 DIP protein P04925 original sequence version: 140 DIP protein P04925 original sequence version: 122 DIP protein P04925 original sequence version: 117 DIP protein P04925 original sequence version: 132 DIP protein P04925 original sequence version: 128 D5331E6321826CC0 prnp-1 1 Prp 4 immunostaining immunostaining predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified fusion protein fusion protein fusion protein undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined direct interaction direct interaction mint mPrP protein forms oligomers when a tetracysteine tag is insert at the disordered N-terminal segment of PrP (TCN) and at the C-terminal segment, which connects PrP to the GPI anchor (TCC). When tetracysteine tag is insert at a position within the PrP structure between helices H2 and H3 that is surface exposed (TCL), prp does not form oligomers. f6a; f6b; f6c; f7b; f7c; f7d prnp-1 3 Prp 4 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified fusion protein fusion protein fusion protein undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined direct interaction direct interaction f4b mint mPrP protein forms oligomers when a tetracysteine tag is insert at the disordered N-terminal segment of PrP (TCN)and at the C-terminal segment, which connects PrP to the GPI anchor (TCC). when tetracysteine tag is insert at a position within the PrP structure between helices H2 and H3 that is surface exposed (TCL), prp does not form oligomers prnp-1 2 Prp 4 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction f4c mint mPrP protein forms oligomers when a tetracysteine tag is insert at the disordered N-terminal segment of PrP (TCN) and at the C-terminal segment, which connects PrP to the GPI anchor (TCC). TCN and TCC fibril formation were also confirmed by TEM (Figure 4C), which showed fibrils similar in size and morphology to wild type mPrP.