Exact(3)
Many interacting proteins have been identified, many of which are associated with ribosome biogenesis.
Many interacting proteins have been reported to bind to their N-terminal region by biochemical interaction assay [ 14].
Because of the essential nature of AHA1 and AHA2 and the number of important plant processes in which they are hypothesized to function, we hypothesize that many interacting proteins, including protein kinases important in the regulation of AHA by phosphorylation at multiple sites in the C-terminal regulatory region, are yet to be identified.
Similar(57)
We expect to see the identification of many such interacting proteins in the immediate future, and many of these binding events will undoubtedly have effects on the cellular physiology of the protein.
While the functional relevance and specificity of the interactions remains to be fully understood (e.g. many 5hmC interacting proteins also have significant affinities for 5mC) these readers might recruit chromatin regulatory complexes to their targets and support activated transcription.
Many potential interacting proteins for USP19 were identified, but none appeared to be putative ubiquitin protein ligases or known modulators of G1 to S progression.
Several recent studies [14], [15] have suggested that viral proteins have evolved to preferentially interact with protein hubs (proteins with many interacting partners) and bottlenecks (proteins that lie in shortest paths between many pairs of proteins) in the human PPI network.
Although many structures of interacting proteins have been determined by X-ray crystallography and Nuclear Magnetic Resonance spectroscopy, the structures of many protein complexes have still not been determined experimentally because of cost and technical limitations.
As the described protocol is very straightforward and robust it may be suitable for many pairs of interacting proteins.
Many of the interacting proteins occupy essential hub positions in cellular protein networks, with key roles in chromatin organization, transcription, translation, maintenance of cell architecture and protein quality control.
While the former network from cues to intracellular signals operate through signal transduction mechanisms, such as protein phosphorylation and involve significant cross-talk between different pathways with many layers of interacting proteins, the network from signals to responses often include transcriptional events with much smaller number of components.
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