Source was cell extract of S2 cell line; bait produced from transfected construct; prey produced from transfected construct.

Dcr-2 and Dcr-1 preferentially interact with different isoforms of loqs.

Source was cell extract of S2 cell line; bait produced from transfected construct; prey produced from endogenous gene.

Dcr-2 and Dcr-1 preferentially interact with different isoforms of loqs.

Dcr-2 and Dcr-1 preferentially interact with different loqs isoforms.

Source was cell extract of S2 cell line; bait produced from transfected construct; prey produced from endogenous gene.

Source was cell extract of S2 cell line; bait produced from transfected construct; prey produced from endogenous gene or transfected construct.

The C-terminal fragment of loqs-PD consisting of aa 338-359 can interact with Dcr-2 but does so at a much lesser extent than full-length loqs-PD. An interaction between the C-terminal fragment of isoform loqs-PC and Dcr-2 was not detected.

Source was cell extract of S2 cell line; bait produced from transfected construct; prey produced from transfected construct.

Isoform loqs-PD was used in this experiment.

Interaction in vitro; bait produced as a recombinant fusion protein in bacterial system; prey produced as a recombinant fusion protein in a baculovirus and Sf9 cell system.

A peptide consisting of the C-terminal 22 aa of loqs-PD competes with full length loqs-PD for binding to Dcr-2.

Interaction in vitro; bait produced as a recombinant fusion protein in bacterial system; prey produced as a recombinant fusion protein in a baculovirus and Sf9 cell system.

A single cross-link was identified between K358 of loqs-PD and K501 of Dcr-2.

Interaction in vitro; proteins produced as a recombinant fusion proteins in baculovirus or bacterial system.

The structure of Dcr-2 and loqs in different dsRNA binding states captured by cryo-EM.

Ternary complex consisting of Dcr-2, loqs and r2d2 curated as a series of binary protein-protein interactions.

Interaction in vitro; Dcr-2 produced as a recombinant fusion protein in a baculovirus and insect cell system; loqs produced as a recombinant fusion protein in a bacterial system.

Higher order complexes consisting of multiple Dcr-2 and r2d2 proteins, in addition to loqs bound to siRNA, curated as a series of binary protein-protein interactions.

Interaction in vitro; Dcr-2 produced as a recombinant fusion protein in a baculovirus and insect cell system; loqs produced as a recombinant fusion protein in a bacterial system.

Higher order complexes consisting of multiple Dcr-2 and r2d2 proteins, in addition to loqs bound to dsRNA, curated as a series of binary protein-protein interactions.

Interaction in vitro; proteins produced as recombinant fusion protein in a baculovirus and insect cell system; loqs produced as a recombinant fusion protein in a bacterial system.

Higher order complexes consisting of multiple Dcr-2 and r2d2 proteins, in addition to loqs bound to siRNA, curated as a series of binary protein-protein interactions.

Interaction in vitro; Dcr-2 produced as a recombinant fusion protein in a baculovirus and insect cell system; loqs produced as a recombinant fusion protein in a bacterial system.