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We discuss how these cells subsequently gain access to the paracortex of draining lymph nodes; a location that allows for efficient interaction between both cell populations, providing the right environment for the induction of immunity as well as tolerance.
We show that a proper folding of the ubiquitin-binding domain, termed NOA/UBAN/NUB, into a stable coiled-coil dimer is required but not sufficient for efficient interaction with poly-Ub.
Since the biological activities of carbonyl compounds 8a, 8b, and 8c were similar to or weaker than those of the parent hydroxyl compounds 3a, 7a, and 7b, it seems to be necessary to have not only a hydrogen bonding acceptor, but also a hydrogen bonding donor adjacent to the hydroxymethyl group of 3a for efficient interaction with hAR LBD.
These results suggest that proper multimerization, most probably in a tetramer formation of IN, might be required for efficient interaction with SIP1.
The apparent discrepancy between the in vivo and in vitro binding assays could be due to different folding of the protein under the two different conditions, suggesting that the Y15A, K186Q, or LL241 242AA mutations might affect the conformation or the higher-order structure of HIV-1 IN that is required for efficient interaction with SIP1 in vivo.
Thus, our studies indicated that 24RKRNRSP30, by itself, was not sufficient for efficient interaction with the nuclear import machinery nor was it able to induce the nuclear localization of a cargo protein too large to easily diffuse across the nuclear pore.
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Thus, split-spGFP fragments likely resist aggregation, which allows for efficient interaction-dependent reassembly.
Hence Fhit can be in close proximity to Gαq subunits for efficient interactions.
Because donor groups are organized by sector, an intersectoral approach to ECD creates challenges for efficient interactions with funders.
Within the context of an intact nucleosome, the H4-R36 residirectlycontactsthets the DNA (Luger et al. 1997; Luger and Richmond 1998) and thus it is possible that this DNA−histone interaction is an important feature of the nucleosome required for efficient interactions between yFACT and chromatin.
The affinity of LIR-1 for UL18 is 1000-fold sthanger than for HLA-A2, and might therefore allow for an efficient interaction despite the low surface expression of UL18.
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CEO of Professional Science Editing for Scientists @ prosciediting.com