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 D-strand perturbation and amyloid propensity in beta-2 microglobulin. D-strand perturbation and amyloid propensity in beta-2 microglobulin. FEBS J. (1742-464X) 2011 Azinas S., Colombo M., Barbiroli A., Santambrogio C., Giorgetti S., Raimondi S., Bonomi F., Grandori R., Bellotti V., Ricagno S., Bolognesi M. in vitro In vitro ms of complexes mass spectrometry studies of complexes ms of complexes ms participant Identification by mass spectrometry ms participant Azinas S., Colombo M., Barbiroli A., Santambrogio C., Giorgetti S., Raimondi S., Bonomi F., Grandori R., Bellotti V., Ricagno S., Bolognesi M. FEBS J. (1742-464X) 2011 D-strand perturbation and amyloid propensity in beta-2 microglobulin. D-strand perturbation and amyloid propensity in beta-2 microglobulin. FEBS J. (1742-464X) 2011 Azinas S., Colombo M., Barbiroli A., Santambrogio C., Giorgetti S., Raimondi S., Bonomi F., Grandori R., Bellotti V., Ricagno S., Bolognesi M. in vitro In vitro fluorescence fluorescence technology fluorescence predetermined predetermined participant predetermined Azinas S., Colombo M., Barbiroli A., Santambrogio C., Giorgetti S., Raimondi S., Bonomi F., Grandori R., Bellotti V., Ricagno S., Bolognesi M. FEBS J. (1742-464X) 2011 D-strand perturbation and amyloid propensity in beta-2 microglobulin. D-strand perturbation and amyloid propensity in beta-2 microglobulin. FEBS J. (1742-464X) 2011 Azinas S., Colombo M., Barbiroli A., Santambrogio C., Giorgetti S., Raimondi S., Bonomi F., Grandori R., Bellotti V., Ricagno S., Bolognesi M. in vitro In vitro electron microscopy electron microscopy Electron crystallography Electron cryomicroscopy Electron crystallography Electron cryomicroscopy predetermined predetermined participant predetermined Azinas S., Colombo M., Barbiroli A., Santambrogio C., Giorgetti S., Raimondi S., Bonomi F., Grandori R., Bellotti V., Ricagno S., Bolognesi M. FEBS J. (1742-464X) 2011 b2mg_human Beta-2-microglobulin B2M CDABP0092 HDCMA22P protein protein human Homo sapiens Human MSRSVALAVLALLSLSGLEAIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM DIP protein P61769 original sequence version: null DIP protein P61769 original sequence version: 138 DIP protein P61769 original sequence version: 134 DIP protein P61769 original sequence version: 135 DIP protein P61769 original sequence version: 116 DIP protein P61769 original sequence version: 60 DIP protein P61769 original sequence version: 79 DIP protein P61769 original sequence version: 87 DIP protein P61769 original sequence version: 93 DIP protein P61769 original sequence version: 94 DIP protein P61769 original sequence version: 91 DIP protein P61769 original sequence version: 106 DIP protein P61769 original sequence version: 111 AFD2DBEF07DCEF27 b2m-b2m-4 3 Beta-2-microglobulin 4 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Beta-2-microglobulin 4 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction f3b homomint mint The amyloid aggregation propensity observed for the D53P mutant was also rather surprising. The D53P variant, compared with w.t. protein, displays the same kinetics of fibril formation at low pH, whereas in 20% TFE at neutrality, fibril formation is partly delayed, but at completion of the aggregation process the amount of fibrils is similar (Fig. 3a-b). b2m-b2m-5 2 Beta-2-microglobulin 4 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Beta-2-microglobulin 4 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction f3a homomint mint The amyloid aggregation propensity observed for the D53P mutant was also rather surprising. The D53P variant, compared with w.t. protein, displays the same kinetics of fibril formation at low pH, whereas in 20% TFE at neutrality, fibril formation is partly delayed, but at completion of the aggregation process the amount of fibrils is similar (Fig. 3a-b). b2m-1 1 Beta-2-microglobulin 4 ms participant Identification by mass spectrometry ms participant predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 2.0 direct interaction direct interaction f3c mint The nano-ESI-MS data indicate that the Asp 53Pro mutation does not prevent the formation of β2m soluble oligomers. Indeed, comparison of the spectra shown in Fig. 3c with those of w.t. β2m and the mutated variants previously reported [22], shows that the aggregation propensity of the mutant under non-denaturing conditions is somewhat decreased, but not at all abolished b2m-1 1 Beta-2-microglobulin 4 ms participant Identification by mass spectrometry ms participant predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 3.0 direct interaction direct interaction f3c mint The nano-ESI-MS data indicate that the Asp 53Pro mutation does not prevent the formation of β2m soluble oligomers. Indeed, comparison of the spectra shown in Fig. 3c with those of w.t. β2m and the mutated variants previously reported [22], shows that the aggregation propensity of the mutant under non-denaturing conditions is somewhat decreased, but not at all abolished b2m-1 1 Beta-2-microglobulin 4 ms participant Identification by mass spectrometry ms participant predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 4.0 direct interaction direct interaction f3c mint The nano-ESI-MS data indicate that the Asp 53Pro mutation does not prevent the formation of β2m soluble oligomers. Indeed, comparison of the spectra shown in Fig. 3c with those of w.t. β2m and the mutated variants previously reported [22], shows that the aggregation propensity of the mutant under non-denaturing conditions is somewhat decreased, but not at all abolished