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双极肌动蛋白束特有的一种多态性。

A polymorphism peculiar to bipolar actin bundles.

作者信息

Francis N R, DeRosier D J

机构信息

Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, Massachusetts 02254.

出版信息

Biophys J. 1990 Sep;58(3):771-6. doi: 10.1016/S0006-3495(90)82419-X.

Abstract

Both muscle and nonmuscle actins produced magnesium paracrystals which we found indistinguishable from one another. Contrary to some previous reports, calcium ions caused no change in filament organization for either type of actin. The most ordered paracrystals consisted of hexagonally packed filaments with opposite polarities. We suggest that this mode of packing permits a form of disorder not previously described, which may account for some puzzling aspects of earlier observations and may prove useful in analyzing actin bundles formed, for example, with erythrocyte band 4.9 protein.

摘要

肌肉肌动蛋白和非肌肉肌动蛋白均产生了镁副晶体,我们发现它们彼此难以区分。与之前的一些报道相反,钙离子对这两种肌动蛋白的丝状体组织均未产生影响。最规则的副晶体由具有相反极性的六边形排列的丝状体组成。我们认为这种排列方式允许一种此前未被描述的无序形式,这可能解释了早期观察中一些令人困惑的方面,并且可能在分析例如由红细胞带4.9蛋白形成的肌动蛋白束时有用。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8536/1281017/5786ab83a845/biophysj00123-0186-a.jpg

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