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More recently a detailed mutational analysis and continuum electrostatic free energy calculations has strongly supported a model for K2P channels with each subunit contributing two P-domains to a pore, with identical P-domains facing each other through the pore's centre to form a complex with bilateral symmetry and an ion conduction pathway with pseudo-4-fold symmetry [7].
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The results support a model for assembly in which the incorporation of P8 is mediated by intermolecular interactions involving these functional epitopes.
Our results support a model for translocation of VgrG C-terminal effector domains into target cell cytosol by a process that requires trafficking of bacterial cells into an endocytic compartment where translocation is triggered by an unknown signal.
The results support a model for naïve antigen recognition in which large Tyr side-chains establish binding contacts with antigen, and small Ser and Ala side-chains serve as auxiliaries that help to position Tyr in favorable binding conformations.
The data support a model for the RNA degradosome (RNAD), in which the RNase E carboxy-end is proximal to PNPase, more distant to Enolase, and more than 10 nm from RhlB helicase.
Siegmund et al. [3] reported this behavior for their data, supporting a model for multiple CSCs.
Altogether, our data support a model for prolonged TCR-induced inhibition of cell polarization and migration (Figure 8).
Finally, results from a recent study in Drosophila, an organism lacking cellular RDR activity, also support a model for viral siRNA biogenesis from dsRNA precursors [31].
Our data support a model for CTCF-mediated regulation of the rDNA consistent with CTCF acting as a direct transcriptional repressor.
Results from this work and previous studies provide evidence to support a model for the interaction of P and spermatozoa under in vivo conditions.
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Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com