Pub. Date : 2007 Feb 23
PMID : 17317623
5 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | We found that PIP(3) binding disrupted the association of calmodulin (CaM) with TRPC6. | pip(3) | transient receptor potential cation channel subfamily C member 6 | Homo sapiens |
| 2 | We identified the PIP(3)-binding site and found that mutations that increased or decreased the affinity of the PIP(3)/TRPC6 interaction enhanced or reduced the TRPC6-dependent current, respectively. | pip(3) | transient receptor potential cation channel subfamily C member 6 | Homo sapiens |
| 3 | We identified the PIP(3)-binding site and found that mutations that increased or decreased the affinity of the PIP(3)/TRPC6 interaction enhanced or reduced the TRPC6-dependent current, respectively. | pip(3) | transient receptor potential cation channel subfamily C member 6 | Homo sapiens |
| 4 | We identified the PIP(3)-binding site and found that mutations that increased or decreased the affinity of the PIP(3)/TRPC6 interaction enhanced or reduced the TRPC6-dependent current, respectively. | pip(3) | transient receptor potential cation channel subfamily C member 6 | Homo sapiens |
| 5 | We identified the PIP(3)-binding site and found that mutations that increased or decreased the affinity of the PIP(3)/TRPC6 interaction enhanced or reduced the TRPC6-dependent current, respectively. | pip(3) | transient receptor potential cation channel subfamily C member 6 | Homo sapiens |