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The fact that substoichiometric amounts of apoE (1 200 apoE Aβ) affect Aβ aggregation (see Figure 1) indicates that apoE either does not bind or binds only poorly to the monomeric form of Aβ.
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It is possible that HSV-2 glycoprotein D-specific neutralizing antibodies bind avidly to the virus but only poorly to glycoprotein D expressed on virus-infected cells, and thus are weak inducers of natural killer cell ADCC.
Specificity of interactions may account for these observations: Bak binds tightly to Mcl-1 and Bcl-xL but only poorly to Bcl-2, whereas Bax binds avidly to all the pro-survival proteins.
They bound only to PLAP.
The ternary complex bound only to SUMO.
This was lent further credence by the fact that CoA binds extremely poorly to CoaE.
Second, BH3-only reagents bind poorly to recombinant Bak and Bax in the absence of membranes, although detergents and liposomes may substitute for the MOM.
Glycopeptides 4 and 7 are Aq-specific, i.e. they both displayed affinity for Aq but bound poorly to DR4.
Nonsulfated CCK 58) [CCK(58)(ns)] has not been considered to be of biological importance because CCK 58)(ns) binds poorly to the CCK(A) receptor and has only been identified once in intestinal extracts.
Interestingly, Lp(a) binds poorly to LDLR, and is not decreased in response to statin treatment.
Both cohesins in the chimaeric Scaf·BF specifically bound to their respective dockerin and did not bind (or bound very poorly) to other non-matching dockerin-bearing proteins (data not shown).
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Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com