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As Ku has many binding partners that contribute to its multitude of functions, it is highly plausible that its telomeric protein interactions negatively regulate Ku to maintain genomic stability.
The V regions have been most intensively studied in syndecan-2 and syndecan-4, and have specific binding partners that contribute to cell signaling that regulates cytoskeletal structures [ 3, 4, 15].
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DOI: http://dx.doi.org/10.7554/eLife.01374.008 As an unbiased approach to isolate binding partners that might contribute to biorientation we purified Sgo1 from cycling cells or cells arrested in mitosis by microtubule perturbation (using a cold-sensitive tubulin mutant; tub2-401 [ Huffaker et al., 1988]).
There are binding partners that demonstrate preference for each of the known arrestin conformations: free, receptor-bound, and microtubule-bound.
These co-factors can have other binding partners that are themselves regulated by different signalling pathways.
There are no known binding partners that would interact with the periplasmic domain of AmtB.
Likely it requires binding partners that aid in vesicle nucleation, localization, targeting and recycling.
Other binding partners may additionally contribute to the anti-apoptotic function of survivin-ΔEx3.
Interactions between E6 and its many cellular binding partners contribute to viral propagation and the possible progression to cancer.
The C-terminal fusion partners are cellular transcription factors that contribute a sequence-specific DNA-binding domain, which determines the tumour phenotype (Lee, 2007).
A number of studies have revealed unsuspecting binding partners of Fhit that may provide linkages to processes that contribute to tumor eradication such as cellular oxidation and apoptosis.
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