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Binding and ubiquitylation assays show that Cand1 is a protein exchange factor that accelerates the rate at which Cul1-Rbx1 equilibrates with multiple F box protein-Skp1 modules.
We suggest that catalyzed protein exchange may be a general feature of dynamic macromolecular machines and propose a hypothesis for how substrates, Nedd8, and Cand1 collaborate to regulate the cellular repertoire of SCF complexes.
Inner membrane motility is an important factor in the "rescue hypothesis" [7], [51] assuming protein exchange within the whole chondriome of a cell to stabilize functionality.
These structural changes correlate with a reduction in transcriptional activity and rate of histone protein exchange that also occurs upon differentiation [11], [13].
These results could imply that KREPA3 is involved in the association of subcomplexes within ∼20S editosomes, the aggregation of subcomplexes, or some dynamic process of editing, such as protein exchange that has been affected by the ZF2 mutation.
Protein exchange kinetics correlate with the level of chromatin condensation and, in many cases, with the level of transcription.
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These individual modular interaction sites, which allow protein exchanges and pathway progression, also provide possible targets for new therapeutic strategies.
The influence of protein exchanging behavior on cellular uptake was also tested to shed a light on the biological significance of the hard and soft protein coronas.
This protein exchanges ADP for ATP across the mitochondrial inner membrane and may also play an important role in the mitochondrial permeability transition pore.
Consumption of 5 energy % from protein at the expense of 5 energy % from fat increased diabetes risk, with an HR of 1.31 (95% CI 1.06 1.61) for each 5 energy % from protein exchanged for 5 energy % from fat in the final model.
Domain swapping occurs when identical proteins exchange segments in reciprocal fashion.
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