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Khan, M. F., Wu, X., Boor, P. J. & Ansari, G. A. Oxidative modification of lipids and proteins in aniline-induced splenic toxicity.
Recent advances in engineered surfaces like zeolites or metal organic frameworks are potentially cytotoxic, due to their ultrahigh surface area and potential for reactive oxygen species generation and/or modification of lipids, membranes, and amino acids.
In this scenario, the oxidative modification of lipids, proteins and nucleic acids in vascular walls contributes to the etiology of cardiovascular disease, implying that consumption or therapeutic use of antioxidants could prevent the onset of such pathological disorders.
Internal membranes form the mazelike endoplasmic reticulum, where cell membrane proteins and lipids are synthesized, and they also form the stacks of flattened sacs called the Golgi apparatus, which is associated with the transport and modification of lipids, proteins, and carbohydrates.
The overall data from the literature suggest that natural modification of lipids leads to the formation of both positive and negative regulators of adaptive immune responses.
A number of genes with higher expression in HR have roles in the transport and modification of lipids.
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Lee, H., Hsu, F. F., Turk, J. & Groisman, E. A. The PmrA-regulated pmrC gene mediates phosphoethanolamine modification of lipid A and polymyxin resistance in Salmonella enterica.
Colistin resistance often arises through covalent modification of lipid A with cationic residues such as phosphoethanolamine as is mediated by Mcr-1 (ref. 2)—which reduce the affinity of polymyxins for lipopolysaccharide3.
Cationic modification of lipid A with 4-amino-4-deoxy-l-arabinopyranose (l-Ara4N) allows the pathogen Klebsiella pneumoniae to resist the antibiotic polymyxin and other cationic antimicrobial peptides.
The modification of lipid A with 4-amino-4-deoxy-L-arabinose (Ara4N) allows gram-negative bacteria to resist the antimicrobial activity of cationic antimicrobial peptides and antibiotics such as polymyxin.
The wing-polymorphic cricket, Gryllus firmus, has been extensively studied with respect to the biochemical basis of life history adaptation, in particular, modification of lipid metabolism that underlies the enhanced accumulation of lipid flight fuel in the dispersing morph [LW(f) = long wings with functional flight muscles] relative to the flightless (SW = short-winged) morph.
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