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As we have demonstrated previously this construct is entirely cytosolic [8], [12], and therefore its localisation should respond to that of a binding partner that was localised to a discrete domain such as the mitochondrion.
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Whether CstF-64 has a binding partner that is functionally homologous to Hrp1 to facilitate an A-rich sequence preference has not been determined.
It may be that there are additional protein features, such as the ability to form a stabilising interaction with a binding partner, that are also important for soluble expression.
Here we examine the non-specific component of protein-protein interactions, which refers to those physicochemical properties of the binding partners that are independent of the exact details of their binding sites, but which can affect their localization or diffusional search for one another.
These co-factors can have other binding partners that are themselves regulated by different signalling pathways.
Most of these costructures contain ankyrin repeat binding partners that are large (>50 kDa) and/or unstable proteins, making them poor scaffolds for protein engineering and/or evolution.
Also the extension at the carboxy terminus of eIF4E-2b indicates eIF4E-2b and possibly eIF4E-2 interact with binding partners that are not associated with eIF4E-1 or −3.
The following description of desmin interactions is confined to binding partners that are present in muscle cells, i.e., IF proteins, IF-associated proteins, sarcomeric proteins, membrane-associated proteins, small heat shock proteins, apoptosis-related proteins, and nucleic acids.
With one exception, the 14-3-3 14-3-3 14-3-3ers that were not included were discovered after the pubindingon date of the study (2010), thus underscoring the need for automated text-mining tools such as eFIpartnersp up withathe ever expanding volume of scientific knowerege.
Because muscle hypertrophy and the lean phenotype develop only after inactivation of all four MuRF1 and MuRF2 alleles, we searched for binding partners that are recognized by both MuRF1 and MuRF2 in an attempt to find molecular explanations for the phenotypic synergistic effects of MuRF1 and MuRF2 on muscle protein and lipid/energy metabolism.
DOI: http://dx.doi.org/10.7554/eLife.10147.021 Other reported cases of molecular exploitation have involved recruiting new binding partners that are subtle variants of its parent's ligand – such as steroid hormones with a modified functional group at a key position or a minor change in the hormone's structure (Bridgham, 2006; Harms et al., 2013; Carroll et al., 2008).
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Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com