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 N-terminal domain of Pyrococcus furiosus l-asparaginase functions as a non-specific, stable, molecular chaperone. N-terminal domain of Pyrococcus furiosus l-asparaginase functions as a non-specific, stable, molecular chaperone. FEBS J. (1742-464X) 2013 Tomar R., Garg DK., Mishra R., Thakur AK., Kundu B. suggested by lperfetto in vitro In vitro fluorescence fluorescence technology fluorescence peptide synthesis peptide synthesis Tomar R., Garg DK., Mishra R., Thakur AK., Kundu B. suggested by lperfetto FEBS J. (1742-464X) 2013 N-terminal domain of Pyrococcus furiosus l-asparaginase functions as a non-specific, stable, molecular chaperone. N-terminal domain of Pyrococcus furiosus l-asparaginase functions as a non-specific, stable, molecular chaperone. FEBS J. (1742-464X) 2013 Tomar R., Garg DK., Mishra R., Thakur AK., Kundu B. suggested by lperfetto in vitro In vitro anti tag coip anti tag coimmunoprecipitation anti tag coip experimental particp experimental participant identification experimental particp Tomar R., Garg DK., Mishra R., Thakur AK., Kundu B. suggested by lperfetto FEBS J. (1742-464X) 2013 N-terminal domain of Pyrococcus furiosus l-asparaginase functions as a non-specific, stable, molecular chaperone. N-terminal domain of Pyrococcus furiosus l-asparaginase functions as a non-specific, stable, molecular chaperone. FEBS J. (1742-464X) 2013 Tomar R., Garg DK., Mishra R., Thakur AK., Kundu B. suggested by lperfetto in vitro In vitro light scattering light scattering predetermined predetermined participant predetermined Tomar R., Garg DK., Mishra R., Thakur AK., Kundu B. suggested by lperfetto FEBS J. (1742-464X) 2013 N-terminal domain of Pyrococcus furiosus l-asparaginase functions as a non-specific, stable, molecular chaperone. N-terminal domain of Pyrococcus furiosus l-asparaginase functions as a non-specific, stable, molecular chaperone. FEBS J. (1742-464X) 2013 Tomar R., Garg DK., Mishra R., Thakur AK., Kundu B. suggested by lperfetto in vitro In vitro tem transmission electron microscopy tem peptide synthesis peptide synthesis Tomar R., Garg DK., Mishra R., Thakur AK., Kundu B. suggested by lperfetto FEBS J. (1742-464X) 2013 masz_ecoli Malate synthase G glcB glc b2976 JW2943 protein protein ecoli Escherichia coli (strain K12) MSQTITQSRLRIDANFKRFVDEEVLPGTGLDAAAFWRNFDEIVHDLAPENRQLLAERDRIQAALDEWHRSNPGPVKDKAAYKSFLRELGYLVPQPERVTVETTGIDSEITSQAGPQLVVPAMNARYALNAANARWGSLYDALYGSDIIPQEGAMVSGYDPQRGEQVIAWVRRFLDESLPLENGSYQDVVAFKVVDKQLRIQLKNGKETTLRTPAQFVGYRGDAAAPTCILLKNNGLHIELQIDANGRIGKDDPAHINDVIVEAAISTILDCEDSVAAVDAEDKILLYRNLLGLMQGTLQEKMEKNGRQIVRKLNDDRHYTAADGSEISLHGRSLLFIRNVGHLMTIPVIWDSEGNEIPEGILDGVMTGAIALYDLKVQKNSRTGSVYIVKPKMHGPQEVAFANKLFTRIETMLGMAPNTLKMGIMDEERRTSLNLRSCIAQARNRVAFINTGFLDRTGDEMHSVMEAGPMLRKNQMKSTPWIKAYERNNVLSGLFCGLRGKAQIGKGMWAMPDLMADMYSQKGDQLRAGANTAWVPSPTAATLHALHYHQTNVQSVQANIAQTEFNAEFEPLLDDLLTIPVAENANWSAQEIQQELDNNVQGILGYVVRWVEQGIGCSKVPDIHNVALMEDRATLRISSQHIANWLRHGILTKEQVQASLENMAKVVDQQNAGDPAYRPMAGNFANSCAFKAASDLIFLGVKQPNGYTEPLLHAWRLREKESH DIP protein P37330 original sequence version: null 820F177D3FE02632 asgx_pyrfu Putative L-asparaginase L-asparagine amidohydrolase PF0142 protein protein pyrfu Pyrococcus furiosus MVAIIVHGGAGTIRKEERIPKIIEGVREAVLTGWRELKKGSALDAVEEAVKVLEDNPLFNAGTGSVLTLDGKVEMDAAIMRGKTLDAGAVAGIWGVKNPISVARKVMEKTDHVLLIGEGAVKFARLMGFPEYDPTTEERRKQWEELRKKLLETGEIRHWKKLSELIKEYPEVLRSTVGAVAFDGEEIVAGTSTGGVFLKMFGRVGDTPIIGAGTYANEVAGASCTGLGEVAIKLSLAKTATDFVRLGLDAQAASEAAIRLATKYFGPDTMGIIMVDSNGNVGFAKNTKHMSYAFMKEGMKEPEAGV mint 68410D8FE6DE9EE2 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 amyp_pig Pancreatic alpha-amylase AMY2 1,4-alpha-D-glucan glucanohydrolase protein protein pig Sus scrofa (Pig) Pig MKLFLLLSAFGFCWAQYAPQTQSGRTSIVHLFEWRWVDIALECERYLGPKGFGGVQVSPPNENIVVTNPSRPWWERYQPVSYKLCTRSGNENEFRDMVTRCNNVGVRIYVDAVINHMCGSGAAAGTGTTCGSYCNPGNREFPAVPYSAWDFNDGKCKTASGGIESYNDPYQVRDCQLVGLLDLALEKDYVRSMIADYLNKLIDIGVAGFRIDASKHMWPGDIKAVLDKLHNLNTNWFPAGSRPFIFQEVIDLGGEAIQSSEYFGNGRVTEFKYGAKLGTVVRKWSGEKMSYLKNWGEGWGFMPSDRALVFVDNHDNQRGHGAGGASILTFWDARLYKVAVGFMLAHPYGFTRVMSSYRWARNFVNGQDVNDWIGPPNNNGVIKEVTINADTTCGNDWVCEHRWRQIRNMVWFRNVVDGQPFANWWANGSNQVAFGRGNRGFIVFNNDDWQLSSTLQTGLPGGTYCDVISGDKVGNSCTGIKVYVSSDGTAQFSISNSAEDPFIAIHAESKL mint 117489E020807378 cah2_bovin Carbonic anhydrase 2 CA2 Carbonic anhydrase II Carbonate dehydratase II protein protein bovin Bos taurus (Bovine) Bovine MSHHWGYGKHNGPEHWHKDFPIANGERQSPVDIDTKAVVQDPALKPLALVYGEATSRRMVNNGHSFNVEYDDSQDKAVLKDGPLTGTYRLVQFHFHWGSSDDQGSEHTVDRKKYAAELHLVHWNTKYGDFGTAAQQPDGLAVVGVFLKVGDANPALQKVLDALDSIKTKGKSTDFPNFDPGSLLPNVLDYWTYPGSLTTPPLLESVTWIVLKEPISVSSQQMLKFRTLNFNAEGEPELLMLANWRPAQPLKNRQVRGFPK mint Essential for bone resorption and osteoclast differentiation (By similarity). Reversible hydration of carbon dioxide A89412C23FFD19A7 ca2-ca2 3 BCA II 9 predetermined predetermined participant predetermined experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component purified purified BCA II 9 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 mint f2a f3a Substrate proteins like bovine carbonic anhydrase (BCA II), porcine pancreas α-amylase and E. coli malate synthase G (MSG), were subjected to aggregation conditions both in the presence and in the absence of NPfA. Aggregation was induced either by heating or by refolding from chemically denatured state. Each substrate protein when heated alone, showed increased scattering indicating increased aggregation. amy2-amy2 3 alpha-amylase 8 predetermined predetermined participant predetermined experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component purified purified alpha-amylase 8 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 mint f2b f3b Substrate proteins like bovine carbonic anhydrase (BCA II), porcine pancreas α-amylase and E. coli malate synthase G (MSG), were subjected to aggregation conditions both in the presence and in the absence of NPfA. Aggregation was induced either by heating or by refolding from chemically denatured state. Each substrate protein when heated alone, showed increased scattering indicating increased aggregation. glcb-glcb 3 MSG 5 predetermined predetermined participant predetermined experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component purified purified MSG 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 f2c mint Substrate proteins like bovine carbonic anhydrase (BCA II), porcine pancreas α-amylase and E. coli malate synthase G (MSG), were subjected to aggregation conditions both in the presence and in the absence of NPfA. Aggregation was induced either by heating or by refolding from chemically denatured state. Each substrate protein when heated alone, showed increased scattering indicating increased aggregation. asgx-ca2 2 BCA II 9 western blot western blot Immuno blot Immuno blot experimental particp experimental participant identification experimental particp unspecified role unspecified role prey prey purified purified NPfa 6 anti tag western anti tag western blot anti tag western experimental particp experimental participant identification experimental particp unspecified role unspecified role bait bait purified purified his tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined direct interaction direct interaction f4c mint app-app-36 4 Aβ amyloid 1-42 7 peptide synthesis peptide synthesis 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 Aβ amyloid 1-42 7 peptide synthesis peptide synthesis 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 f5d homomint mint Following incubation, as mentioned in the previous section, samples of both Aβ and polyQ in the absence or presence of NPfA were adsorbed on copper grids, air dried and negatively stained with 1% uranyl acetate. Samples were observed on a transmission electron microscope (Philips CM12) operated at 100KV. app-app-37 1 Aβ amyloid 1-42 7 peptide synthesis peptide synthesis 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 Aβ amyloid 1-42 7 peptide synthesis peptide synthesis 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 f5b homomint mint Control experiment in the presence of BSA resulted in marginal change in ThT fluorescence indicating that dissociation of preformed Aβ amyloid fibrils is specifically mediated by NPfA (Figure 5B).