| Unique identifier for interactor A | uniprotkb:P10997 |
| Unique identifier for interactor B | uniprotkb:P10997 |
| Alternative identifier for interactor A | intact:EBI-8526679 intact:MINT-8074874 uniprotkb:Q14598 uniprotkb:Q0ZD87 ensembl:ENSP00000240652.3 ensembl:ENSP00000437357.1 |
| Alternative identifier for interactor B | intact:EBI-8526679 intact:MINT-8074874 uniprotkb:Q14598 uniprotkb:Q0ZD87 ensembl:ENSP00000240652.3 ensembl:ENSP00000437357.1 |
| Aliases for A | psi-mi:iapp_human(display_long) uniprotkb:IAPP(gene name) psi-mi:IAPP(display_short) uniprotkb:Amylin(gene name synonym) uniprotkb:Diabetes-associated peptide(gene name synonym) uniprotkb:Insulinoma amyloid peptide(gene name synonym) |
| Aliases for B | psi-mi:iapp_human(display_long) uniprotkb:IAPP(gene name) psi-mi:IAPP(display_short) uniprotkb:Amylin(gene name synonym) uniprotkb:Diabetes-associated peptide(gene name synonym) uniprotkb:Insulinoma amyloid peptide(gene name synonym) |
| Interaction detection methods | psi-mi:"MI:0051"(fluorescence technology) |
| First author | Wang et al. (2014) |
| Identifier of the publication | imex:IM-22231 pubmed:24561193 |
| NCBI Taxonomy identifier for interactor A | taxid:9606(human) taxid:9606(Homo sapiens) |
| NCBI Taxonomy identifier for interactor B | taxid:9606(human) taxid:9606(Homo sapiens) |
| Interaction types | psi-mi:"MI:0407"(direct interaction) |
| Source databases and identifiers | psi-mi:"MI:0471"(MINT) |
| Interaction identifier(s) in the corresponding source database | intact:EBI-9119352 imex:IM-22231-1 |
| Confidence score | intact-miscore:0.95 |
| Complex expansion | - |
| Biological role A | Unspecified role |
| Biological role B | Unspecified role |
| Experimental role A | Neutral component |
| Experimental role B | Neutral component |
| Interactor type A | Protein |
| Interactor type B | Protein |
| Annotations for the interaction | figure legend:f1a f3a comment:"\"Firstly, we examined the inhibitory effect of the all-D-amino-acid inhibitor on the assembly of hIAPP in bulk solution. Similarly to the results of previous studies [30], an aggregation process from unstructured monomers to β-sheeted fibrils was observed for hIAPP alone in bulk solution, as indicated by the time-dependence of Thioflavin-T (ThT) fluorescence, transmission electron microscopy (TEM) image and circular dichroism (CD) spectra (Figure 1A-C). The addition of equimolar peptide inhibitor in bulk solution of hIAPP resulted in a complete suppression of ThT fluorescence intensity (Figure 1A) and disappearance of fibrils in TEM image where only small pieces with length around 200-300 nm were left (Figure 1D).\"" comment:"\"We next examined the inhibitory effect of the all-D-amino-acid inhibitor under phospholipid membrane condition. Before addition of the inhibitor, the ThT fluorescence intensity of hIAPP in lipid vesicle solution displayed a rapid increase after ca. 5 min delay (Figure 3A), which is much less than that of hIAPP in bulk solution (corresponding time needed in bulk solution was ca. 2 h). The decrease in the lag time was attributed to the accelerating role of lipid membrane for fibril formation of the amyloid peptide which has been well established [41].\"" full coverage:Only protein-protein interactions curation depth:imex curation |
| NCBI Taxonomy identifier for the host organism | taxid:-1(in vitro) taxid:-1(In vitro) |
| Parameters of the interaction | - |
| Creation date | 2014/02/06 |
| Update date | 2014/10/16 |
| negative Boolean value | false |
| Feature(s) for interactor A | - |
| Feature(s) for interactor B | - |
| Stoichiometry for interactor A | - |
| Stoichiometry for interactor B | - |
| Participant identification method for interactor A | Predetermined participant |
| Participant identification method for interactor B | Predetermined participant |