These data suggest that not all heat shock proteins can interact with uPAR and the interactions between uPAR and HSP70/MRJ are specific.
The interactions with purified proteins show that they proteins can interact directly, but Figure 2E suggests that in cells any direct interaction is too weak to detect.
However, a crucial problem regarding Self-interactions Proteins (SIPs) is whether proteins can interact with their partners.
In an examination of the evolutionary conservation of the Nse3-Nse4 interactions, we find that several MAGE proteins can interact with at least one of the NSE4/EID proteins.
To test the possibility that Sam68 could affect U2AF binding by protein-protein interaction, we initially tested whether the two proteins can interact in vitro.
During complex formation, proteins can interact via covalent, surface surface or peptide surface contacts.
Costameric proteins can interact with many components of both the sarcolemma and cytoskeleton.
Biochemical analysis further shows that the five USH1 proteins can interact with each other in vitro.
The data suggest that the proteins can interact with each other.
Additionally, MAGUK proteins can interact with AKAP5, which brings PKA and calcineurin into these AMPA receptor complexes [7], [8], [44].
Although these two highly homologous proteins can interact with the same cis-elements on RNAs, nPTB is a significantly weaker silencer of splicing than PTB [41].
