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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.
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.
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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.
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.
In summary, two of the three known members of the hAG family of proteins show clear relevance to breast cancer that is strengthened by their roles in Xenopus development, a significant association with ER, and putative protein-binding partners that are not only linked with cancer progression but provide opportunities for those interactions to be targeted in the development of cancer therapies.
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.
Whether CstF-64 has a binding partner that is functionally homologous to Hrp1 to facilitate an A-rich sequence preference has not been determined.
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