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Cell probe atomic force microscopy has provided some useful insight into the interactions of bacterial cells with the metal surfaces.
Analysis of latex blend films, made possible by TappingMode™ atomic force microscopy, has provided insight into the interaction properties of hard and soft latex particles.
For more than half a century, electron microscopy has provided crucial insights into the fundamental architecture and function of these organelles, such as the characteristic [9 + 2] microtubule arrangement of the axoneme or the dynein-driven microtubule sliding as the basis of motility.
Recent work utilizing patch clamp and fluorescent microscopy has provided sufficient evidence that the plasma membrane is not spared by USEP [29], [32], [33], [34], [35], [36], [37].
In other cell types, whole cell fluorescence microscopy has provided unprecedented insights into the dynamic roles that actin and microtubules play in shaping the cells and positioning components within them [28]; [29].
Electron microscopy has provided important structural information about protein complexes essential for describing their functional organization.
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Analytical tools, such as atomic force microscopy (AFM), scanning tunneling microscopy (STM) and near-field scanning optical microscopy, have provided revolutionary improvements in our ability to visualise structures and events all the way down to the molecular and atomic scale.
Electron (Aikawa, 1971) and live (Wickham et al., 2003) microscopy have provided evidence for two distinct stages in the release of merozoites from erythrocytes, with the successive rupture of the PVM and of the erythrocyte membrane.
At the same time, electron cryo-microscopy has provided valuable insights into the global shape of the splicing machinery, but compositional and conformational heterogeneity has limited the resolution to 20 30 Å [ 5].
In the past decade, two-photon fluorescence microscopy (2PFM) has provided several advantages in biological research, including high three-dimensional (3D) spatial resolution as a result of the inherent nonlinear dependence of two-photon fluorescence (2PF) on the illumination intensity (1− 4).
Electron microscopy (EM) has provided convincing evidence for the presence of gluten proteins inside vesicles associated with the Golgi apparatus, suggesting that storage proteins may pass through the Golgi in their transport from the ER to the vacuoles (Parker and Hawes, 1982; Kim et al., 1988; Loussert et al., 2008) where they form protein deposits.
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Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com