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Concomitantly, platelets undergo a change in morphology and expose negatively charged phospholipids on their surface membrane.
In a simplified view, these cationic amphipathic peptides will exhibit a higher affinity to cell membranes that expose negatively charged lipids on their outer membrane leaflet.
Proteoheparan sulphate macromolecules, anchored in the plasma membrane, expose negatively charged glycosamin-oglycan side chains with binding sites for inorganic cations.
Microbial membranes expose negatively charged phospholipids, e.g. lipopolysaccharide or teichoic acids, on their surface while mammalian cells segregate into the inner leaflet the lipids with negatively charged headgroups, thus explaining the poor binding of anti-microbial peptides to mammalian cells [ 28, 29].
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Nucleosomes become accessible on the cell surface, exposing negatively charged nucleic acid containing complexes.
Definitely, PS constitutes an Achilles' heel of cancer cells, because the anionic lipid represents a cancer type independent target for host defense peptides that rapidly kill cells exposing negatively charged lipids.
This exposed negatively charged PS acted as a binding site of urine microcrystalline on the cell surface and increased the adhesion and aggregation of microcrystallines, thereby increasing the risk of stone formation.
This is likely due to local adhesive contact between some of the (positively charged) avidin molecules with the exposed (negatively charged) mica patches on the opposing surface, again consistent with the picture of layer interpenetration, although the net interaction between the surfaces remains repulsive.
Cancer cells expose more negatively charged phospholipids [45] as well as more glycolipids and glycoproteins [46], [47] on the outer plasma membrane than do normal cells.
These two proteins expose both negatively and positively charged residues in ADIPOQ (i.e. Lys 169, Arg 221, Asp 170, Asp 187, Asp 227 and Glu 191, Glu 218) and two positively charged residues in ADIPOR1 (i.e. Lys 170 and Arg 235).
Growth factor activated and proliferating HUVEC overexpress the αvβ3-integrin, while Jurkat cells exposed to anti-Fas become apoptotic and expose the negatively charged phospholipid phosphatidylserine (PS) at the outer layer of the cell membrane.
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