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 Protease-activated alpha-2-macroglobulin can inhibit amyloid formation via two distinct mechanisms. Protease-activated alpha-2-macroglobulin can inhibit amyloid formation via two distinct mechanisms. FEBS Lett. (0014-5793) 2013 Wyatt AR., Constantinescu P., Ecroyd H., Dobson CM., Wilson MR., Kumita JR., Yerbury JJ. in vitro In vitro electron microscopy electron microscopy Electron crystallography Electron cryomicroscopy Electron crystallography Electron cryomicroscopy predetermined predetermined participant predetermined Wyatt AR., Constantinescu P., Ecroyd H., Dobson CM., Wilson MR., Kumita JR., Yerbury JJ. FEBS Lett. (0014-5793) 2013 Protease-activated alpha-2-macroglobulin can inhibit amyloid formation via two distinct mechanisms. Protease-activated alpha-2-macroglobulin can inhibit amyloid formation via two distinct mechanisms. FEBS Lett. (0014-5793) 2013 Wyatt AR., Constantinescu P., Ecroyd H., Dobson CM., Wilson MR., Kumita JR., Yerbury JJ. in vitro In vitro fluorescence fluorescence technology fluorescence predetermined predetermined participant predetermined Wyatt AR., Constantinescu P., Ecroyd H., Dobson CM., Wilson MR., Kumita JR., Yerbury JJ. FEBS Lett. (0014-5793) 2013 Protease-activated alpha-2-macroglobulin can inhibit amyloid formation via two distinct mechanisms. Protease-activated alpha-2-macroglobulin can inhibit amyloid formation via two distinct mechanisms. FEBS Lett. (0014-5793) 2013 Wyatt AR., Constantinescu P., Ecroyd H., Dobson CM., Wilson MR., Kumita JR., Yerbury JJ. in vitro In vitro light scattering light scattering predetermined predetermined participant predetermined Wyatt AR., Constantinescu P., Ecroyd H., Dobson CM., Wilson MR., Kumita JR., Yerbury JJ. FEBS Lett. (0014-5793) 2013 a4_human Amyloid-beta precursor protein APP A4 AD1 Alzheimer disease amyloid protein ABPP PreA4 Cerebral vascular amyloid peptide Protease nexin-II APPI Amyloid precursor protein Amyloid-beta A4 protein Alzheimer disease amyloid A4 protein homolog Amyloid-beta (A4) precursor protein protein protein human Homo sapiens Human MLPGLALLLLAAWTARALEVPTDGNAGLLAEPQIAMFCGRLNMHMNVQNGKWDSDPSGTKTCIDTKEGILQYCQEVYPELQITNVVEANQPVTIQNWCKRGRKQCKTHPHFVIPYRCLVGEFVSDALLVPDKCKFLHQERMDVCETHLHWHTVAKETCSEKSTNLHDYGMLLPCGIDKFRGVEFVCCPLAEESDNVDSADAEEDDSDVWWGGADTDYADGSEDKVVEVAEEEEVAEVEEEEADDDEDDEDGDEVEEEAEEPYEEATERTTSIATTTTTTTESVEEVVREVCSEQAETGPCRAMISRWYFDVTEGKCAPFFYGGCGGNRNNFDTEEYCMAVCGSAMSQSLLKTTQEPLARDPVKLPTTAASTPDAVDKYLETPGDENEHAHFQKAKERLEAKHRERMSQVMREWEEAERQAKNLPKADKKAVIQHFQEKVESLEQEAANERQQLVETHMARVEAMLNDRRRLALENYITALQAVPPRPRHVFNMLKKYVRAEQKDRQHTLKHFEHVRMVDPKKAAQIRSQVMTHLRVIYERMNQSLSLLYNVPAVAEEIQDEVDELLQKEQNYSDDVLANMISEPRISYGNDALMPSLTETKTTVELLPVNGEFSLDDLQPWHSFGADSVPANTENEVEPVDARPAADRGLTTRPGSGLTNIKTEEISEVKMDAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIATVIVITLVMLKKKQYTSIHHGVVEVDAAVTPEERHLSKMQQNGYENPTYKFFEQMQN DIP protein P05067 original sequence version: 160 DIP protein P05067 original sequence version: 207 DIP protein P05067 original sequence version: 185 DIP protein P05067 original sequence version: 188 A12EE761403740F5 lysc_human Lysozyme C LYZ LZM 1,4-beta-N-acetylmuramidase C protein protein human Homo sapiens Human MKALIVLGLVLLSVTVQGKVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLSCSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV 8ECFD276BEB2678A lalba_bovin Alpha-lactalbumin LALBA ALACTA Lactose synthase B protein protein protein bovin Bos taurus (Bovine) Bovine MMSFVSLLLVGILFHATQAEQLTKCEVFRELKDLKGYGGVSLPEWVCTTFHTSGYDTQAIVQNNDSTEYGLFQINNKIWCKDDQNPHSSNICNISCDKFLDDDLTDDIMCVKKILDKVGINYWLAHKALCSEKLDQWLCEKL mint homomint Regulatory subunit of lactose synthase, changes the substrate specificity of galactosyltransferase in the mammary gland making glucose a good acceptor substrate for this enzyme. This enables LS to synthesize lactose, the major carbohydrate component of milk. In other tissues, galactosyltransferase transfers galactose onto the N-acetylglucosamine of the oligosaccharide chains in glycoproteins 810CDB1145901405 app-app-32 2 A beta 1-42 4 predetermined predetermined participant predetermined experimental particp experimental participant identification experimental particp 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 A beta 1-42 4 predetermined predetermined participant predetermined experimental particp experimental participant identification experimental particp 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 f2b homomint mint Under the conditions used here, aggregation of A1-42 shows a lag of ca. 70 minutes, followed by a rapid growth phase and a plateau at ca. 150 minutes (Fig. 2a, black line). Consistent with previous studies [12], the presence of native 2M at a 10:1 (A1-42-to-2M) molar ratio dramatically reduces the time-dependent increase in ThT fluorescence (Fig. 1a; red line). At the same molar ratio, the presence of trypsin-2M also results in a suppression of ThT fluorescence (Fig 2a, solid blue line). This suppression in ThT signal is over 80% for both the presence of native 2M and trypsin-2M at the endpoint of the assay (Fig 2b). lyz-lyz-2 2 I59T lysozyme 5 predetermined predetermined participant predetermined experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component purified purified I59T lysozyme 5 predetermined predetermined participant predetermined experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction f1a f1b homomint mint In this study, the kinetics of the aggregation show a lag phase of ca. 50 minutes, followed by a rapid growth phase that reaches a plateau after ca. 150 minutes (Fig. 1a, black line). 2M, present at a molar ratio of 10:1 (lysozyme-to-2M), shows a dramatic decrease in thioflavin-T (ThT) fluorescence over the course of the assay (Fig. 1a; red line). When trypsin-2M is incubated with 159T lysozyme the ThT fluorescence is again, significantly suppressed (Fig. 1a; blue line). At the endpoint of the fibril formation, the presence of both native 2M and trypsin-2M results in over a 90% decrease in ThT signal relative to the I59T lysozyme sample alone (Fig. 1b). lalba-lalba 2 Alpha-lactalbumin 6 predetermined predetermined participant predetermined experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component purified purified Alpha-lactalbumin 6 predetermined predetermined participant predetermined experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction sf3a homomint mint In vitro fibril formation (37°C, pH 7.4) of α-lactalbumin (α-lact) alone (black) or in the presence of native α2M (red) or trypsin-α2M (blue) as monitored by ThT fluorescence. app-app-33 1 A beta 1-42 4 predetermined predetermined participant predetermined experimental particp experimental participant identification experimental particp 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 A beta 1-42 4 predetermined predetermined participant predetermined experimental particp experimental participant identification experimental particp 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 f2c homomint mint Transmission electron microscopy (TEM) images of the ThT assay endpoint samples show that fibrillar aggregates are formed by A1-42 incubated alone; however, in the presence of either native 2M or trypsin-2M, the number of well-defined fibrils is reduced and aggregates appear amorphous (Fig. 2c). lyz-lyz-3 1 I59T lysozyme 5 predetermined predetermined participant predetermined experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component purified purified I59T lysozyme 5 predetermined predetermined participant predetermined experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction homomint mint TEM images of the ThT assay endpoint samples demonstrate that while I59T lysozyme alone forms fibrillar structures there is no evidence for such structures when I59T lysozyme is incubated under the same conditions with native 2M or trypsin-2M (Fig. 1c). f1c lyz-lyz-4 3 I59T lysozyme 5 predetermined predetermined participant predetermined experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component purified purified I59T lysozyme 5 predetermined predetermined participant predetermined experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction sf2b homomint mint In vitro fibril formation (60°C, pH 5.0) of I59T lysozyme (solid line) in the absence or presence of trypsin (dashed line) at a 1:10 (trypsin-to-lysozyme) molar ratio as monitored by light scattering