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无脊椎动物肌原纤维的分离、电子显微镜观察和 3D 重构。

Isolation, electron microscopy and 3D reconstruction of invertebrate muscle myofilaments.

机构信息

Department of Cell Biology, University of Massachusetts Medical School, 55 Lake Avenue North, Worcester, MA 01655, USA.

出版信息

Methods. 2012 Jan;56(1):33-43. doi: 10.1016/j.ymeth.2011.11.007. Epub 2011 Dec 2.

DOI:10.1016/j.ymeth.2011.11.007
PMID:22155190
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3299862/
Abstract

Understanding the molecular mechanism of muscle contraction and its regulation has been greatly influenced and aided by studies of myofilament structure in invertebrate muscles. Invertebrates are easily obtained and cover a broad spectrum of species and functional specializations. The thick (myosin-containing) filaments from some invertebrates are especially stable and simple in structure and thus much more amenable to structural analysis than those of vertebrates. Comparative studies of invertebrate filaments by electron microscopy and image processing have provided important generalizations of muscle molecular structure and function. This article reviews methods for preparing thick and thin filaments from invertebrate muscle, for imaging filaments by electron microscopy, and for determining their three dimensional structure by image processing. It also highlights some of the key insights into filament function that have come from these studies.

摘要

理解肌肉收缩的分子机制及其调控受到了对无脊椎动物肌肉肌丝结构研究的极大影响和帮助。无脊椎动物容易获得,涵盖了广泛的物种和功能特化。一些无脊椎动物的粗(肌球蛋白含量高)肌丝结构特别稳定且简单,因此比脊椎动物的肌丝更适合结构分析。通过电子显微镜和图像处理对无脊椎动物肌丝的比较研究,为肌肉分子结构和功能提供了重要的概括。本文综述了从无脊椎动物肌肉中制备粗、细肌丝,通过电子显微镜对肌丝成像以及通过图像处理确定其三维结构的方法。本文还重点介绍了这些研究中得出的一些关于肌丝功能的关键见解。

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Three-dimensional reconstruction of tarantula myosin filaments suggests how phosphorylation may regulate myosin activity.狼蛛肌球蛋白丝的三维重建揭示了磷酸化可能如何调节肌球蛋白活性。
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Blebbistatin stabilizes the helical order of myosin filaments by promoting the switch 2 closed state.blebbistatin通过促进开关2关闭状态来稳定肌球蛋白丝的螺旋结构。
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