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 The role of the central flexible region on the aggregation and conformational properties of human ataxin-3. The role of the central flexible region on the aggregation and conformational properties of human ataxin-3. FEBS J. (1742-464X) 2012 imex curation Santambrogio C., Frana AM., Natalello A., Papaleo E., Regonesi ME., Doglia SM., Tortora P., Invernizzi G., Grandori R. Only protein-protein interactions in vitro In vitro ms of complexes mass spectrometry studies of complexes ms of complexes predetermined predetermined participant predetermined Santambrogio C., Frana AM., Natalello A., Papaleo E., Regonesi ME., Doglia SM., Tortora P., Invernizzi G., Grandori R. FEBS J. (1742-464X) 2012 Only protein-protein interactions imex curation The role of the central flexible region on the aggregation and conformational properties of human ataxin-3. The role of the central flexible region on the aggregation and conformational properties of human ataxin-3. FEBS J. (1742-464X) 2012 imex curation Santambrogio C., Frana AM., Natalello A., Papaleo E., Regonesi ME., Doglia SM., Tortora P., Invernizzi G., Grandori R. Only protein-protein interactions in vitro In vitro fluorescence fluorescence technology fluorescence predetermined predetermined participant predetermined Santambrogio C., Frana AM., Natalello A., Papaleo E., Regonesi ME., Doglia SM., Tortora P., Invernizzi G., Grandori R. FEBS J. (1742-464X) 2012 Only protein-protein interactions imex curation p54252-1 Ataxin-3 ATXN3 ATX3 MJD MJD1 SCA3 Machado-Joseph disease protein 1 Spinocerebellar ataxia type 3 protein MJD1a protein protein human Homo sapiens Human MESIFHEKQEGSLCAQHCLNNLLQGEYFSPVELSSIAHQLDEEERMRMAEGGVTSEDYRTFLQQPSGNMDDSGFFSIQVISNALKVWGLELILFNSPEYQRLRIDPINERSFICNYKEHWFTVRKLGKQWFNLNSLLTGPELISDTYLALFLAQLQQEGYSIFVVKGDLPDCEADQLLQMIRVQQMHRPKLIGEELAQLKEQRVHKTDLERVLEANDGSGMLDEDEEDLQRALALSRQEIDMEDEEADLRRAIQLSMQGSSRNISQDMTQTSGTNLTSEELRKRREAYFEKQQQKQQQQQQQQQQGDLSGQSSHPCERPATSSGALGSDLGKACSPFIMFATFTLYLTYELHVIFALHYSSFPL Variant in position: 349:YELHVIFALHYSSFPL->Missing (in short isoform 1, due to a stop-gain single nucleotide polymorphism, has reduced half-life due to increased proteasomal degradation, has reduced solubility and increased tendency to form aggregates, increased localization to the nucleus). 4B2477EB67C30EFF atxn3-atxn3 2 Ataxin-3 3 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain Ataxin-3 3 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain direct interaction direct interaction f2a homomint domino mint Altogether, the results presented in this section indicate that both protein variants undergo misfolding and aggregation under the employed experimental conditions, but that the longer fragment has a stronger aggregation propensity, in spite of the lack of APRs in the 183-291 tract. The aggregation kinetics of the two pure proteins AT3/182 and AT3/291 has been monitored by conventional ThT assays atxn3-atxn3-1 2 Ataxin-3 3 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain Ataxin-3 3 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain direct interaction direct interaction f2a homomint domino mint Altogether, the results presented in this section indicate that both protein variants undergo misfolding and aggregation under the employed experimental conditions, but that the longer fragment has a stronger aggregation propensity, in spite of the lack of APRs in the 183-291 tract. The aggregation kinetics of the two pure proteins AT3/182 and AT3/291 has been monitored by conventional ThT assays atxn3-atxn3-2 2 Ataxin-3 3 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain Ataxin-3 3 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain direct interaction direct interaction homomint domino mint f2b f2c f2d Altogether, the results presented in this section indicate that both protein variants undergo misfolding and aggregation under the employed experimental conditions, but that the longer fragment has a stronger aggregation propensity, in spite of the lack of APRs in the 183-291 tract. The aggregation process has also been monitored by FTIR spectroscopy in the Amide-I region, which is sensitive to protein secondary structures atxn3-atxn3-3 2 Ataxin-3 3 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain Ataxin-3 3 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain direct interaction direct interaction homomint domino mint f2b f2c f2d Altogether, the results presented in this section indicate that both protein variants undergo misfolding and aggregation under the employed experimental conditions, but that the longer fragment has a stronger aggregation propensity, in spite of the lack of APRs in the 183-291 tract. The aggregation process has also been monitored by FTIR spectroscopy in the Amide-I region, which is sensitive to protein secondary structures atxn3-4 1 Ataxin-3 3 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain Stoichiometry: 2.0 direct interaction direct interaction f5 mint AT3 aggregation can also be elicited by heat. Thus, ESI-MS spectra at variable temperature were recorded, in order to explore heat-induced changes in protein conformation and/or oligomerization. Fig. 5 shows data acquired after equilibration of the instrument interface at 150-175 °C. By this method, the sample is heated at the entrance of the mass analyzer, although the actual temperature of the ESI droplets can not be controlled. Samples containing 10 μM AT3/182 or AT3/291 in 10 mM ammonium acetate pH 6.5 show bimodal CSDs similar to those observed at high concentrations of acetonitrile. In these spectra, however, also dimer-specific signals can be detected, indicating heat-induced protein aggregation.