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New discoveries revealed that fundamental steps in biomineralization are enzyme driven, not only during hydroxyapatite deposition, but also during initial bioseed formation, involving the transient deposition and subsequent transformation of calcium carbonate to calcium phosphate mineral.
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Thus, for the entire PTS, each enzyme drives a step of the reaction and is then regenerated in the subsequent phosphorylation step.
Terminase possesses ATPase catalytic sites that modulate the nuclease activity of the enzyme, drive its strand-separation activity, and power translocation during active DNA packaging [ 27].
These complexes were shown to incorporate numerous cytosolic TCR signalling adaptors and enzymes, driven by TCR activation-induced tyrosine phosphorylations [ 7].
Enzymes drive myriads of chemical reactions that otherwise would almost never happen.
As the major players in metabolic pathways, enzymes drive the desirable reactions but also regulate metabolic pathways positively or negatively to maintain the energy homeostasis within the cells.
Here, we explore an emerging concept that lysine acetyltransferase (KAT) enzymes drive cellular plasticity in the context of somatic cell reprogramming and tumorigenesis.
Furthermore, under physiological conditions, the C3 convertase enzymes drive the deposition of C3b molecules close to the surface and it has been proposed that nascent C3b molecules deposit on the surface within a 600 Å radius around the C3 convertase, creating hotspots with C3b molecules at a high density [ 11].
As an homologous mechanism has been shown to regulate the cell-specificity of gene expression in both NADP-ME and NAD-ME gene families in independent lineages (Brown et al., 2011), it is unlikely that mechanisms underlying the recruitment of these enzymes drove the evolution of distinct sub-types.
Titration of inactive catalytic serine-to-alanine mutants into wild type monomeric enzyme drives dimerization and activates the wild type monomer of the heterodimeric species.
Nuclear magnetic resonance (NMR) relaxation experiments have shown that the conformational dynamics of the enzyme drive the structural transitions from the open to closed conformation and play a key role in substrate recognition and turnover.
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Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com