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Importantly, the EBP family ligands share structural homology with MAEBL in the extracellular carboxyl cysteine-rich domain and in the presence of transmembrane and cytoplasmic domains, but do not appear to interact with the glideosome in the same way as TRAP or its homologues.
Similar effects were also seen in mutants P378A, A430S, and Y431A, respectively, although P378 was predicted to interact with both types H and A oligosaccharides, while A430 and Y431 do not appear to interact with either of the two oligosaccharides [13], [15].
Many of these proteins do not appear to interact directly with the protostome TACCs, but would be expected to be in the same protein complex (Fig. 6C,6D).
Although the role of AMPK-related kinases is largely unknown, they do not appear to interact with the regulatory β and γ subunits of AMPK [ 5].
The other universal SSU proteins are found largely on the SSU surface and do not appear to interact with the decoding function.
Additional results suggest that HydG is unable to displace HydE when it is bound to HydF and that HydG and HydE do not appear to interact with one another.
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Specifically, Chz1 does not appear to interact with Htz1 in the cytoplasm, rather Nap1 interactions with Htz1 H2B dimers maintain a soluble pool of Htz1 for transport to the nucleus where Chz1 Htz1 interactions can occur [ 30].
The interaction between GSTs and isothiocyanates does not appear to interact to affect breast cancer risk in humans or the variations in the urinary metabolites of isothiocyanates in our data (Steck et al. 2007a, 2007b).
However, the AuNPs did not appear to interact with the cells and instead were suspended in the medium.
An exception is MAGEF1, which does not appear to interact with either paralog (Figure 7E).
In contrast, wild type Lhp1 is imported by Kap108 and does not appear to interact with Kap121 in vivo.
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