肌联蛋白和伴肌动蛋白的结构与功能。
Structure and function of titin and nebulin.
作者信息
Keller T C
机构信息
Department of Biological Science, Florida State University, Tallahassee 32306-3050, USA.
出版信息
Curr Opin Cell Biol. 1995 Feb;7(1):32-8. doi: 10.1016/0955-0674(95)80042-5.
PMID:7755987
Abstract
Recent investigations of titin anchorage and elasticity have been supplemented with in vitro expression studies on isolated domains of titin and nebulin. These have yielded new insights into the molecular basis of the functions of these proteins in muscle. The characterization of a cellular (non-muscle) isoform of titin has extended the functional relevance of this family of proteins beyond the realm of muscle.
摘要
近期对肌联蛋白的锚定和弹性的研究，已通过对肌联蛋白和伴肌动蛋白的分离结构域进行体外表达研究得到补充。这些研究为这些蛋白质在肌肉中发挥功能的分子基础带来了新的见解。对肌联蛋白一种细胞（非肌肉）异构体的表征，将该蛋白质家族的功能相关性扩展到了肌肉领域之外。
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