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Fig. 2 Images (a e) are the prepared PVB/dyes colorful NFMs on aluminum foil substrates, where a is the pure PVB NFM, b PVB/X-GRL NFM, c PVB/X-10GFF NFM, d PVB/X-GB NFM, and e PVB/X-2RL NFM.
The results proved that cathodic ion sheath adjacent to the substrates, where a large potential drop exists, also plays an essential role for the controlled growth of SWCNTs, while ion damage to the VA-SWCNTs is inherently avoided due to high collision frequency among molecules in atmospheric pressure.
Si thin films with a thickness of 10 nm were deposited on surface-oxidized Si substrates, where a thickness of the oxidized SiO2 layer was 2 μm.
This interest was driven by the unintuitive observation that PNSB require the Calvin cycle (or exogenous electron acceptors) even for photoheterotrophic conditions on substrates where a net CO2 release occurs (see measurements given in Table 2).
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Polystyrene beads are electrophoretically deposited onto a sulfonate derivatized gold substrate where a patterned photoresist layer (first template) is applied.
An applied load anchors the position of a self-assembled pattern relative to the substrate, where a colony boundary resides on the strain gradient region.
The microstructure was dominated by beta-phase, except for the region near the substrate where a limited amount of alpha-precipitates was present due to reheating effect.
A low temperature processing was adopted by You et al. [24] to deposit inverted ITO/PEDOT PSS/CH3NH3PbI3−x Cl x /PCB/Al on a flexible polyethylene terephthalate (PET) substrate, where a PCE of 9.2 % was achieved.
Gaskell et al. [8, 9] finally considered the generalization of the different models to the case of inclined substrates, where gravity plays a significant physical role in the flow dynamics.
APP and Notch (type I transmembrane cell surface receptors) are important γ-secretase substrates where PS plays a significant γ-secretase dependent role in the sequential cleavage in the processing of APP and Notch and stabilizes the β-catenin in Wnt signaling pathway which are γ-secretase independent actions.
Consistent with its role in DNA repair, Type II RNase H enzymes are also able to cleave substrates where there is an RNA DNA base pair mismatch, but at a rate reduced compared to the corresponding perfect duplex [ 31, 32, 46- 48].
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CEO of Professional Science Editing for Scientists @ prosciediting.com