[en] In a previous issue of this journal, we published a report entitled 'Creation of Stereo-paired Bone Anatomical Charts Using Human Bone Specimens for Radiation Education' To understand how the bone specimen is visualized as an X-ray image, we newly created a bone specimen stereo-paired X-ray anatomical chart by adding the X-ray images of the same bone specimen. When a bone is X-rayed, the surface structure and internal structure of the bone are visualized as a composite image of the difference in X-ray absorption, and each bone becomes a unique X-ray image. Therefore, we took stereo-paired X-ray images of the bone specimens by the same method as the stereo-paired anatomical chart of the bone specimens. Then, we arranged the stereo-paired X-ray images and surface images of the same bone specimen in the one sheet to be readily compared. Similar to the previous bone specimen anatomical charts, these data of X-ray image anatomical chart were also made into an electronic file, so that we can do the three-dimensional observation of bone X-ray images even at the place of radiological examination or at home through electronic media. Until now, none of the specialized anatomy books and pictorial books are available for stereoscopic viewing of bone specimens and bone X-ray images. However, this stereo-paired X-ray image anatomical chart enabled us to learn accurate three-dimensionalization of bones by comparing the bone surface morphology and bone X-ray images. (author)

[en] Highlights: • pH-dependent gating of the KcsA channel is regulated by the CPD. • E146 is the most essential amino acid for pH sensing by the KcsA. • The protonated-mimicking mutant, E146Q, is constitutively open independent of pH. • Minimal rearrangement of the CPD is sufficient for opening of the KcsA. - Abstract: The KcsA channel is a proton-activated potassium channel. We have previously shown that the cytoplasmic domain (CPD) acts as a pH-sensor, and the charged states of certain negatively charged amino acids in the CPD play an important role in regulating the pH-dependent gating. Here, we demonstrate the KcsA channel is constitutively open independent of pH upon mutating E146 to a neutrally charged amino acid. In addition, we found that rearrangement of the CPD following this mutation was not large. Our results indicate that minimal rearrangement of the CPD, particularly around E146, is sufficient for opening of the KcsA channel