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 Transient-state kinetic analysis of complex formation between photoprotein clytin and GFP from jellyfish Clytia gregaria. Transient-state kinetic analysis of complex formation between photoprotein clytin and GFP from jellyfish Clytia gregaria. FEBS letters 2016 imex curation Eremeeva EV., van Berkel WJ., Vysotski ES. eugene_vysotski@ibp.ru 11-Apr-2016: Contacted by IntAct-Help. Only protein-protein interactions imex curation 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 Accepted 2016-MAR-31 AT 09:40 BST AT 09:40 BST by MARTA FEBS letters 2016 Only protein-protein interactions imex curation imex curation clyt_clygr Clytin Phialidin protein protein Phialidium gregarium Clytia gregaria MADTASKYAVKLRPNFDNPKWVNRHKFMFNFLDINGDGKITLDEIVSKASDDICAKLGATPEQTKRHQDAVEAFFKKIGMDYGKEVEFPAFVDGWKELANYDLKLWSQNKKSLIRDWGEAVFDIFDKDGSGSISLDEWKAYGRISGICSSDEDAEKTFKHCDLDNSGKLDVDEMTRQHLGFWYTLDPNADGLYGNFVP 23F1E399667F9059 d7pm04_clygr GFP1 protein protein Phialidium gregarium Clytia gregaria MTALTEGAKLFEKEIPYITELEGDVEGMKFIIKGEGTGDATTGTIKAKYICTTGDLPVPWATILSSLSYGVFCFAKYPRHIADFFKSTQPDGYSQDRIISFDNDGQYDVKAKVTCENGTLYNRVTVKGTGFKSNGNILGMRVLYHSPPHAVYILPDRKNGGMKIEYNKAFDVMGGGHQMARHAQFNKPLGAWEEDYPLYHHLTVWTSFGKDPDDDETDHLNIVEVIKAVDLETYR E89AF992BB5B8DF1 clyt_clygr-gfp1-1 1 3 acceptor acceptor unspecified role unspecified role purified purified 2 donor donor unspecified role unspecified role purified purified direct interaction direct interaction 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.