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 In vitro inhibition of transthyretin aggregate-induced cytotoxicity by full and peptide derived forms of the soluble receptor for advanced glycation end products (RAGE). In vitro inhibition of transthyretin aggregate-induced cytotoxicity by full and peptide derived forms of the soluble receptor for advanced glycation end products (RAGE). FEBS Lett. (0014-5793) 2006 imex curation Monteiro FA., Cardoso I., Sousa MM., Saraiva MJ. 2009-01-08 Only protein-protein interactions in vitro In vitro saturation binding saturation binding nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence Monteiro FA., Cardoso I., Sousa MM., Saraiva MJ. FEBS Lett. (0014-5793) 2006 2009-01-08 Only protein-protein interactions imex curation In vitro inhibition of transthyretin aggregate-induced cytotoxicity by full and peptide derived forms of the soluble receptor for advanced glycation end products (RAGE). In vitro inhibition of transthyretin aggregate-induced cytotoxicity by full and peptide derived forms of the soluble receptor for advanced glycation end products (RAGE). FEBS Lett. (0014-5793) 2006 imex curation Monteiro FA., Cardoso I., Sousa MM., Saraiva MJ. 2009-01-08 Only protein-protein interactions in vitro In vitro competition binding competition binding nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence Monteiro FA., Cardoso I., Sousa MM., Saraiva MJ. FEBS Lett. (0014-5793) 2006 2009-01-08 Only protein-protein interactions imex curation rage_human Advanced glycosylation end product-specific receptor AGER RAGE Receptor for advanced glycosylation end products protein protein human Homo sapiens Human MAAGTAVGAWVLVLSLWGAVVGAQNITARIGEPLVLKCKGAPKKPPQRLEWKLNTGRTEAWKVLSPQGGGPWDSVARVLPNGSLFLPAVGIQDEGIFRCQAMNRNGKETKSNYRVRVYQIPGKPEIVDSASELTAGVPNKVGTCVSEGSYPAGTLSWHLDGKPLVPNEKGVSVKEQTRRHPETGLFTLQSELMVTPARGGDPRPTFSCSFSPGLPRHRALRTAPIQPRVWEPVPLEEVQLVVEPEGGAVAPGGTVTLTCEVPAQPSPQIHWMKDGVPLPLPPSPVLILPEIGPQDQGTYSCVATHSSHGPQESRAVSISIIEPGEEGPTAGSVGGSGLGTLALALGILGGLGTAALLIGVILWQRRQRRGEERKAPENQEEEEERAELNQSEEPEAGESSTGGP DIP protein Q15109 original sequence version: 157 0D584C436C30CCE7 tthy_human Transthyretin Prealbumin TBPA ATTR TTR PALB protein protein human Homo sapiens Human MASHRLLLLCLAGLVFVSEAGPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE DIP protein P02766 original sequence version: 114 DIP protein P02766 original sequence version: 163 DIP protein P02766 original sequence version: 174 3A6AEBCBBA56BC44 ager-ttr 2 4 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified undefined mutation mutation disrupting interaction mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain Wed Jul 06 17:04:18 BST 2016 Sequence change details about this feature cannot be ascertained or do not fit with the current version of the referenced protein, so they have been deleted as a result of our quality control procedures. The original label was 'mutation disrupting' Leu55Pro range MINT-2635440: original sequence: 55-55 : AINVAVHVFRKAADDTWEPF Stoichiometry: 1.0 3 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 direct interaction direct interaction F1 Similar results were obtained when mouse TTR was used. we tested several TTR mutants and mouse TTR for non-glycosylated RAGE binding. Among these human mutants, L55P significantly lost a competition effect, showing not, vert, similar10-fold lower affinities to both human (Fig. 1A) and mouse (data not shown) sRAGE, as compared to human wtTTR. FEBS-Letters homomint mint ager-ttr-1 1 3 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 4 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified undefined mutation mutation disrupting interaction mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain Wed Jul 06 17:03:11 BST 2016 Sequence change details about this feature cannot be ascertained or do not fit with the current version of the referenced protein, so they have been deleted as a result of our quality control procedures. The original label was 'mutation disrupting' Leu55Pro range MINT-2635456: original sequence: 55-55 : AINVAVHVFRKAADDTWEPF Stoichiometry: 1.0 direct interaction direct interaction F2A Indeed, 125I-TTR bound to the RAGE peptide in a dose-dependent, specific and saturable manner, with a Kd = 91 ± 44 nM (Fig. 2A). kd 91 nanomolar FEBS-Letters homomint mint