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 eremeeva-2016-1 in vitro In vitro bifc bimolecular fluorescence complementation bifc tag fluorescence tag visualisation by fluorescence tag fluorescence Eremeeva EV., van Berkel WJ., Vysotski ES. eugene_vysotski@ibp.ru FEBS letters 2016 Only protein-protein interactions imex curation imex curation d7pm04_clygr GFP1 protein protein Phialidium gregarium Clytia gregaria MTALTEGAKLFEKEIPYITELEGDVEGMKFIIKGEGTGDATTGTIKAKYICTTGDLPVPWATILSSLSYGVFCFAKYPRHIADFFKSTQPDGYSQDRIISFDNDGQYDVKAKVTCENGTLYNRVTVKGTGFKSNGNILGMRVLYHSPPHAVYILPDRKNGGMKIEYNKAFDVMGGGHQMARHAQFNKPLGAWEEDYPLYHHLTVWTSFGKDPDDDETDHLNIVEVIKAVDLETYR clyt_clygr Clytin Phialidin protein protein Phialidium gregarium Clytia gregaria MADTASKYAVKLRPNFDNPKWVNRHKFMFNFLDINGDGKITLDEIVSKASDDICAKLGATPEQTKRHQDAVEAFFKKIGMDYGKEVEFPAFVDGWKELANYDLKLWSQNKKSLIRDWGEAVFDIFDKDGSGSISLDEWKAYGRISGICSSDEDAEKTFKHCDLDNSGKLDVDEMTRQHLGFWYTLDPNADGLYGNFVP clyt_clygr-gfp1-1 1929540 N/A 1929541 acceptor acceptor unspecified role unspecified role purified purified N/A 1929542 donor donor unspecified role unspecified role purified purified direct interaction direct interaction false false false f1 f2 f3 f5 f6 t2 In this work, we used the stopped-flow technique [29] to characterize the clytin/cgreGFP interaction. On the basis of the analysis of bioluminescence kinetics at different wavelengths, we propose that cgreGFP forms a transient complex with the reaction intermediates arising after Ca2+ binding with a photoprotein before the excited singlet state of product is formed.