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The diversity of membrane proteins that are regulated by a given amphiphile suggests that these compounds may alter membrane protein function by mechanisms that do not involve direct binding to the target protein.
Since it was demonstrated that mutations in transmembrane domain 5 [24] and 8 [25] of ENT1 may alter membrane expression of ENT1, we decided to examine whether amino acid changes from isoleucine to threonine in the transmembrane 6 of ENT1 alter membrane expression.
While the reduced inhibitory effect of the C3-diastereomer, epi-cholesterol, on KirBac1.1 activity is suggestive that cholesterol inhibition may be mediated by direct interactions [8], [21], epi-cholesterol and cholesterol orient differently in membranes and may alter membrane properties differently [22], [23].
In addition, ω-3 PUFAs may attenuate delayed depolarization by reducing Na+/Ca2+ exchange currents, which may alter membrane electrical activity [ 39, 40].
One could therefore envisage that the atg32Δ-dependent mutational block of macromitophagy may alter membrane lipid composition not only in mitochondria but also in the ER and the PM.
Na+,K+-ATPase localizes to the inner nuclear membrane as well as to the plasma membrane; nuclear envelope-associated Na+,K+-ATPase activity may alter membrane ionic transport and osmolarity, and thereby, contribute to the ER and perinuclear space expansion observed in autotic cells.
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Disrupted PtdCho synthesis may also alter membrane fluidity and integrity, which can damage hepatocytes.
Deletion of IZH3 may therefore alter membrane composition affecting the ability of polyenes to bind membrane ergosterol leading to enhanced resistance.
However, since non-thermal stressors may also alter membrane fluidity or lead to various types of membrane damage, interactions of Hsp20s with membranes could partly account for the overall stress-responsiveness of the Hsp20 family.
This difference suggests that egress of a combination of ions (Cybulska et al., 1995; Hartsel et al., 1994), or the pore itself may alter the membrane's properties and underlie AmphoB's negation of IFITM3.
The combination of these may alter the membrane permeability of the fungal strains, favoring the intracellular passage of the antifungal, which inhibits the synthesis of ergosterol, causing an increase in death of the microorganisms at a lower concentration.
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