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Phosphorylation of the RD following receptor tyrosine kinase ras/MAPK signalling has been shown to activate LAP*/C/EBPβ1 by inducing a structural change that affects interaction and composition of associated Mediator complex (Mo et al, 2004).
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In this report, however, we present evidences to propose another mechanism of the fibrillation process in which the oligomeric granular species of α-synuclein turn into the amyloid fibrils through concerted lateral association of the preformed granules by inducing structural distortion of the preformed structures with a physical influence of shear stress.
Atomic force microscopy studies indicated that alkyl chains bind to and retain segregated interfacial surfactant phases at low surface tensions by inducing 3D structural transitions in the monolayer's fluid-like phase, forming surfactant-associated reservoirs.
We speculated that all the 3 candidates and the control bound with CDK2 protein successfully and inhibited the activity of CDK2 by inducing its structural component change.
In the ferric state cytochrome c also binds NO; the corresponding ferrous NO complex can be formed only by inducing major structural changes in the molecule, classically by high pH [8] and more recently by binding to cardiolipin [9,10].
The consequent release of pro-inflammatory mediators such as IL-1β, IL-6, TNF-α and IL-18 [ 6] may interfere with peritoneal adequacy by inducing both structural and functional in the peritoneal membrane.
This was shown biochemically using an extrachromosomal plasmid and determining the state of DNA by inducing structural deformation by chloroquine-infused gel electrophoresis.
We thus hypothesize that the mechanism of inhibition by HMA is also allosteric, either by restricting movement of helices needed for ion flow or by inducing structural rearrangements that block ion conduction, or both.
Another critical component of NPQ formation, capacity and kinetics is the PsbS protein, originally thought to be required for qE formation but now considered to be mainly involved in the enhancement of the capacity and rate of formation of qE by inducing structural changes in the thylakoid (Johnson and Ruban 2010).
RNA chaperones are nonspecific RBPs that bind diverse RNA substrates and help RNAs fold by inducing structural rearrangement of misfolded RNAs [ 25, 32, 33].
Together, our results demonstrate a farnesyl-dependent mechanism in which progerin expression interrupts complex stem cell processes by inducing structural alterations in the nucleus that interfere with critical, basic stem cell functions that are required for vascular repair: self-renewal, proliferation, membrane fluidity and cell migration.
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