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By altering the affinity of the receptor using pharmacological means one may be able to modify the biological activity of human PMNs.
Promising research has shown that allosteric modulators of GPCRs can be used to treat addiction by altering the affinity of the GPCR to its ligand or impacting its downstream signaling responses [ 72].
Therefore, the results obtained in this study provide support for the hypothesis that H2O2-induced methionine oxidation results in global and/or localized conformational changes that contribute to CN inactivation, by impairing the interaction between CNA and CNB, Ca2+ and CNB, or/and CaM and CNA, or/and by altering the affinity between AI and the catalytic center.
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In this system, the exchange of the macrocycle between stations could be controlled by the introduction of a barrier in the middle of the thread (kinetic control) as well as by altering the binding affinity of the macrocycle to the two different stations (thermodynamic control).
Therefore, the exchange of phenylalanine to another aromatic amino acid only slightly affects binding by reducing the affinity to phospholipids but not altering the affinity for galactolipids, whereas removal of the aromatic amino acid at this position significantly enhances affinity for galactolipids without significant alterations of the affinity for phospholipids.
Transitional-phase inversions are caused by changes in the phase behaviour of a non-ionic surfactant oil water system and are induced by altering the surfactant's affinity for the oil and water phases.
This could be due to a number of factors including the possibility that fusion to the GAL4 DNA-binding domain obscured identification of an activation domain at the amino-terminus, or that CRTR-1 lacks a classical activation domain and acts by altering the DNA-binding affinity or conformation of partner proteins within the DNA-binding heteromer to elicit activation or repression.
This model does not rule out the possibility that APN increases the transporter's substrate affinity by altering the thermodynamics of substrate binding, whether through direct (BAT1 binding site) or allosteric means.
It is assumed that the conformation-labile (i.e. molecule-dynamic) property of the polypeptides favorably modulates the binding affinities by altering the side-chain positions with respect to the targets, which might lead to higher-affinity interactions of the helical polypeptides with Au III), Au(I) and/or Au(0) surfaces [ 30, 31].
It was found that the affinity of BCRP to substrates can be modulated by altering the substrate specificity of multi-drug transporters.
Non-enzymatic glycation increases hemoglobin-oxygen affinity and reduces oxygen delivery to tissues by altering the structure and function of hemoglobin.
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