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 Respiratory complexes III and IV can each bind two molecules of cytochrome c at low ionic strength. Respiratory complexes III and IV can each bind two molecules of cytochrome c at low ionic strength. FEBS Lett. (0014-5793) 2015 imex curation Moreno-Beltrán B., Díaz-Moreno I., González-Arzola K., Guerra-Castellano A., Velázquez-Campoy A., De la Rosa M.A., Díaz-Quintana A. idiazmoreno@us.es Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Moreno-Beltrán B., Díaz-Moreno I., González-Arzola K., Guerra-Castellano A., Velázquez-Campoy A., De la Rosa M.A., Díaz-Quintana A. idiazmoreno@us.es Accepted 2015-FEB-23 by LUANA FEBS Lett. (0014-5793) 2015 Only protein-protein interactions imex curation Respiratory complexes III and IV can each bind two molecules of cytochrome c at low ionic strength. Respiratory complexes III and IV can each bind two molecules of cytochrome c at low ionic strength. FEBS Lett. (0014-5793) 2015 imex curation Moreno-Beltrán B., Díaz-Moreno I., González-Arzola K., Guerra-Castellano A., Velázquez-Campoy A., De la Rosa M.A., Díaz-Quintana A. idiazmoreno@us.es Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Moreno-Beltrán B., Díaz-Moreno I., González-Arzola K., Guerra-Castellano A., Velázquez-Campoy A., De la Rosa M.A., Díaz-Quintana A. idiazmoreno@us.es Accepted 2015-FEB-23 by LUANA FEBS Lett. (0014-5793) 2015 Only protein-protein interactions imex curation Respiratory complexes III and IV can each bind two molecules of cytochrome c at low ionic strength. Respiratory complexes III and IV can each bind two molecules of cytochrome c at low ionic strength. FEBS Lett. (0014-5793) 2015 imex curation Moreno-Beltrán B., Díaz-Moreno I., González-Arzola K., Guerra-Castellano A., Velázquez-Campoy A., De la Rosa M.A., Díaz-Quintana A. idiazmoreno@us.es Only protein-protein interactions in vitro In vitro dls dynamic light scattering dls predetermined predetermined participant predetermined Moreno-Beltrán B., Díaz-Moreno I., González-Arzola K., Guerra-Castellano A., Velázquez-Campoy A., De la Rosa M.A., Díaz-Quintana A. idiazmoreno@us.es Accepted 2015-FEB-23 by LUANA FEBS Lett. (0014-5793) 2015 Only protein-protein interactions imex curation cyc1b_arath Cytochrome c1 2, heme protein, mitochondrial CYC1-2 Complex III subunit 4-2 Complex III subunit IV-2 Cytochrome b-c1 complex subunit 4-2 Ubiquinol-cytochrome c reductase complex cytochrome c1 subunit 2 MHK7.4 At5g40810 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MVGGGVIRQLLRRKLHSQSVATPVLSWLSSKKANEDAGSAGLRAFALMGAGITGLLSFSTVASADEAEHGLECPNYPWPHEGILSSYDHASIRRGHQVYQQVCASCHSMSLISYRDLVGVAYTEEEAKAMAAEIEVVDGPNDEGEMFTRPGKLSDRLPEPYSNESAARFANGGAYPPDLSLVTKARHNGQNYVFALLTGYRDPPAGISIREGLHYNPYFPGGAIAMPKMLNDEAVEYEDGTPATEAQMGKDVVSFLSWAAEPEMEERKLMGFKWIFLLSLALLQAAYYRRLKWSVLKSRKLVLDVVN 3F807D081F788ED3 cyc_human Cytochrome c CYCS CYC protein protein human Homo sapiens Human MGDVEKGKKIFIMKCSQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGYSYTAANKNKGIIWGEDTLMEYLENPKKYIPGTKMIFVGIKKKEERADLIAYLKKATNE DIP protein P99999 original sequence version: 59 8EE9689E0102506B cox1_bovin Cytochrome c oxidase subunit 1 MT-CO1 COI COXI Cytochrome c oxidase polypeptide I MTCO1 protein protein bovin Bos taurus (Bovine) Bovine MFINRWLFSTNHKDIGTLYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVMITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMMWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDTWAKIHFAIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTMWNTISSMGSFISLTAVMLMVFIIWEAFASKREVLTVDLTTTNLEWLNGCPPPYHTFEEPTYVNLK DIP protein P00396 original sequence version: 124 0D7C807D7FA3996C cyc12-cycs 1 4 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified 5 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction f2 sf2 sf4 cyc12-cycs-1 2 5 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified 4 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction t1 f3 sf5 ITC binding experiments corresponding to the reduced hCc–pCc1 complexes cycs-mt_co1 2 5 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified 6 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction f4 mt-co1 3 6 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction sf6