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The USP7-NTD has been shown to be sufficient for binding both p53 and EBNA1 [33], [33].
Interestingly, a peptide corresponding to the GH3 domain alone was able to precipitate MFN2, suggesting that the GH3 domain might be sufficient for binding of Reaper to MFN2 at the mitochondria.
On RBCs heavily coated with immunoglobulin, the amount of antigen-antibody complex can be sufficient for binding complement protein complex C1 and, thereby, for activation of the classical complement pathway [ 30– 30].
The activation of CaMKII is highly cooperative (Gaertner et al., 2004; Rosenberg et al., 2005), so low levels of Ca2+/CaM that are insufficient for autophosphorylation of an unactivated holoenzyme may be sufficient for binding the target subunit and enhancing its autophosphorylation in holoenzymes that contain some activated subunits through exchange.
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Together, these data allow to conclude that the presence of a single copy of H2 is sufficient for binding of COE proteins to bind DNA as dimers.
Products are not consumed when they bind; thus the product from a single gene is sufficient for binding the regulatory regions of several genes (effectively, we ignore quantities of gene products).
Using limited proteolysis and mass spectrometry, we show that distinct regions of human eIF3 are sufficient for binding to the HCV IRES RNA and the 40S subunit.
F2 alone is sufficient for binding to erythrocytes [4].
Three Xin repeats are sufficient for binding actin [6], [8] and six repeats are sufficient for binding and cross-linking actin filaments [6], [8].
The observation that the VH of VC2.2.2 is sufficient for binding to VEGF-C is intriguing.
Neither the N-terminus (aa 1 144) nor the C-terminus (aa 529 861) of Orc1 alone were sufficient for binding.
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