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Changes in the structure of the AIS may result in modifications of the excitability of these neurons, as described previously [ 6, 13].
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This is a highly specialized portion of the axon where action potentials initiate, and we have shown that the structure and maintenance of the AIS are exquisitely sensitive to Cdk5 activity.
DOI: http://dx.doi.org/10.7554/eLife.04581.014 10.7554/eLiFigure81.015 Figure 4 figure supplement 2. The formation of the periodic βIV spectrin structure in the AIS is dependent on βII spectrin.
A schematic of the AIS is shown in Fig. 1.
Network security, optimization problems and distributed computing are some of the AIS's applications.
In the second approach, we used the βIV-spectrin fluorescence distribution to define the extent of the AIS (see Methods) [37], and obtained an AIS index (AISi) from the ratio of YFP fluorescence within the AIS region to YFP fluorescence outside the AIS region (see Methods).
The 2005 updated version of the AIS was used.
Data from mice lacking the cytoskeletal linker protein 4.1B show that this protein is necessary to form the Caspr+ para-AIS barrier, ensuring the compartmentalization of Kv1 channels and the segregation of the AIS, para-AIS and JXP-AIS.
Finally, we demonstrate that protein 4.1B is necessary to form the Caspr-expressing para-AIS barrier and to ensure the proper compartmentalization of Kv1 channels as well as the segregation of the AIS, para-AIS and juxtapara-AIS.
The comparison of the AIS and non-AIS group showed no difference between the two groups in sex, etiology of hydrocephalus and the shunt type.
The composition and structure of the CrN coatings have been studied using X-ray diffraction (XRD), using θ/2θ diffraction mode and Schulz reflection methods, which revealed a preferred orientation of CrN(220) for CrN/Cr/AISI 4140.
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