| Unique identifier for interactor A | uniprotkb:P10997 |
| Unique identifier for interactor B | uniprotkb:P10997 |
| Alternative identifier for interactor A | intact:EBI-8526679 uniprotkb:Q14598 intact:MINT-8074874 uniprotkb:Q0ZD87 ensembl:ENSP00000240652.3 ensembl:ENSP00000437357.1 |
| Alternative identifier for interactor B | intact:EBI-8526679 uniprotkb:Q14598 intact:MINT-8074874 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:0872"(atomic force microscopy) |
| 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-9119414 imex:IM-22231-4 |
| 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:f3b f3c f3d comment:"\"As show in Figure 3B-D, whereas abundant fibrils were formed at lipid membrane in the absence of the inhibitor, the amyloid fibrils were remarkably decreased when hIAPP was incubated with equimolar inhibitor. The fibrillation was even completely inhibited and a large amount of oligomers were present when threefold inhibitor was added. It was noted that very thin and elongated fibers are clearly present in AFM image at a molar ratio of hIAPP:inhibitor = 1:1 but there is no observable increase in the fluorescence intensity at the same hIAPP:inhibitor ratio. This was because the fluorescence experiments were performed at a molar ratio of lipid:hIAPP = 150:1, while the ratio used in AFM experiments was 25:1. Lower lipid:hIAPP ratio (or higher concentration of hIAPP at membrane surface) used in the AFM experiments caused more rapid aggregation of hIAPP and thus less effective inhibition for fibril formation. We also measured the AFM image of the inhibitor alone in the presence of phospholipids after the same incubation time (see Figure S1 in the Supporting Information). No any apparent aggregates were observed on the AFM image, confirming that the oligomers appearing in the AFM image of hIAPP in the presence of inhibitor result from the amyloid peptides but not the inhibitor.\"" 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 |