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. 2011 Mar 15;124(6):921–932. doi: 10.1242/jcs.078055

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© 2011.

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial Share Alike License, which permits unrestricted non-commercial use, distribution and reproduction in any medium provided that the original work is properly cited and all further distributions of the work or adaptation are subject to the same Creative Commons License terms.

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Fig. 1. — Identification of RNF41 as a LR-complex-interacting protein. (A) Schematic outline of the MAPPIT technique using a chimeric EpoR-LR bait receptor (ELR-F3). (B) HEK293T cells transfected with an RNF41 prey arising from a MAPPIT screen and the indicated baits, were stimulated with Epo or left untreated. Luciferase data of triplicate measurements from a representative experiment are expressed as fold induction (stimulated/non stimulated) ± s.d. FLAG-tagged prey expression was verified by western blotting. (C) Human RNF41 structure and sequence of its RING domain. Arrows indicate in-frame fusion positions with gp130 in the RNF41 prey constructs identified in MAPPIT screens. The eight residues constituting a functional RING domain are underlined.