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 http://mint.bio.uniroma2.it/mint golub-2007-1 Evidence for the formation of start aggregates as an initial stage of protein aggregation. in vitro In vitro light scattering light scattering predetermined predetermined participant predetermined Golub N., Meremyanin A., Markossian K., Eronina T., Chebotareva N., Asryants R., Muronets V., Kurganov B. FEBS Lett. (0014-5793) 2007 2009-01-08 Only protein-protein interactions imex curation g3p_rabit Glyceraldehyde-3-phosphate dehydrogenase GAPDH GAPD Peptidyl-cysteine S-nitrosylase GAPDH protein protein rabit Oryctolagus cuniculus (Rabbit) Rabbit MVKVGVNGFGRIGRLVTRAAFNSGKVDVVAINDPFIDLHYMVYMFQYDSTHGKFHGTVKAENGKLVINGKAITIFQERDPANIKWGDAGAEYVVESTGVFTTMEKAGAHLKGGAKRVIISAPSADAPMFVMGVNHEKYDNSLKIVSNASCTTNCLAPLAKVIHDHFGIVEGLMTTVHAITATQKTVDGPSGKLWRDGRGAAQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTPNVSVVDLTCRLEKAAKYDDIKKVVKQASEGPLKGILGYTEDQVVSCDFNSATHSSTFDAGAGIALNDHFVKLISWYDNEFGYSNRVVDLMVHMASKE kpb1_rabit Phosphorylase b kinase regulatory subunit alpha, skeletal muscle isoform PHKA1 protein protein rabit Oryctolagus cuniculus (Rabbit) Rabbit MRSRSNSGVRLDSYARLVQQTILCHQNPVTGLLPASYDQKDAWVRDNVYSILAVWGLGLAYRKNADRDEDKAKAYELEQSVVKLMRGLLHCMIRQVDKVESFKYSQSTKDSLHAKYNTKTCATVVGDDQWGHLQLDATSVYLLFLAQMTASGLHIIHSLDEVNFIQNLVFYIEAAYKTADFGIWERGDKTNQGISELNASSVGMAKAALEALDELDLFGVKGGPQSVIHVLADEVQHCQSILNSLLPRASTSKEVDASLLSVISFPAFAVEDSKLVEITKQEIITKLQGRYGCCRFLRDGYKTPKEDPNRLYYEPAELKLFENIECEWPLFWTYFILDGVFSGNAEQVQEYREALEAVLIKGKNGVPLLPELYSVPPDKVDEEYQNPHTVDRVPMGKLPHMWGQSLYILGSLMAEGFLAPGEIDPLNRRFSTVPKPDVVVQVSILAETEEIKAILKDKGINVETIAEVYPIRVQPARILSHIYSSLGCNNRMKLSGRPYRHMGVLGTSKLYDIRKTIFTFTPQFIDQQQFYLALDNKMIVEMLRTDLSYLCSRWRMTGQPTITFPISQTMLDEDGTSLNSSILAALRKMQDGYFGGARIQTGKLSEFLTTSCCTHLSFMDPGPEGKLYSEDYDDNYDELESGDWMDGYNSTSTARCGDEVARYLDHLLAHTAPHPKLAPASQKGGLNRFRAAVQTTCDLMSLVTKAKELHVQNVHMYLPTKLFQASRPSLNLLDSSHPSQEDQVPTVRVEVHLPRDQSGEVDFQALVLQLKETSSLQEQADILYMLYTMKGPDWDTELYEEGSATVRELLTELYGKVGKIRHWGLIRYISGILRKKVEALDEACTDLLSHQKHLTVGLPPEPREKTISAPLPYEALTRLIEEACEGDMNISILTQEIMVYLAMYMRTQPGLFAEMFRLRIGLIIQVMATELAHSLRCSAEEATEGLMNLSPSAMKNLLHHILSGKEFGVERSVRPTDSNVSPAISIHEIGAVGATKTERTGIMQLKSEIKQVEFRRLSISTESQPNGGHSLGADLMSPSFLSPGTSVTPSSGSFPGHHTSKDSRQGQWQRRRRLDGALNRVPIGFYQKVWKVLQKCHGLSVEGFVLPSSTTREMTPGEIKFSVHVESVLNRVPQPEYRQLLVEAILVLTMLADIEIHSIGSIIAVEKIVHIANDLFLQEQKTLGADDIMLAKDPASGICTLLYDSAPSGRFGTMTYLSKAAATYVQEFLPHSICAMQ mint Phosphorylase b kinase catalyzes the phosphorylation of serine in certain substrates, including troponin I. The alpha chain may bind calmodulin gapdh-2 673644 g3p_rabit GAPDH 673645 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction false false false F4 The experiment describes protein aggregation mint phka1 673644 kpb1_rabit Phb 673646 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction false false false F1 The experiment describes protein aggregation mint