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2
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本文引用的文献

1
Arg/Abl2 modulates the affinity and stoichiometry of binding of cortactin to F-actin.Arg/Abl2 调节衔接蛋白(cortactin)与 F-肌动蛋白结合的亲和力和化学计量。
Biochemistry. 2012 Aug 21;51(33):6644-53. doi: 10.1021/bi300722t. Epub 2012 Aug 10.
2
Stoichiometry of Nck-dependent actin polymerization in living cells.活细胞中 Nck 依赖性肌动蛋白聚合的化学计量。
J Cell Biol. 2012 May 28;197(5):643-58. doi: 10.1083/jcb.201111113. Epub 2012 May 21.
3
Cell polarity: quantitative modeling as a tool in cell biology.细胞极性:定量建模作为细胞生物学的工具。
Science. 2012 Apr 13;336(6078):175-9. doi: 10.1126/science.1216380.
4
Spatial modeling of cell signaling networks.细胞信号网络的空间建模
Methods Cell Biol. 2012;110:195-221. doi: 10.1016/B978-0-12-388403-9.00008-4.
5
Stretch-induced actin remodeling requires targeting of zyxin to stress fibers and recruitment of actin regulators.牵张诱导的肌动蛋白重构需要将锌指蛋白靶向到应力纤维,并募集肌动蛋白调节剂。
Mol Biol Cell. 2012 May;23(10):1846-59. doi: 10.1091/mbc.E11-12-1057. Epub 2012 Mar 28.
6
Actin binding to WH2 domains regulates nuclear import of the multifunctional actin regulator JMY.肌动蛋白与 WH2 结构域的结合调节多功能肌动蛋白调节剂 JMY 的核输入。
Mol Biol Cell. 2012 Mar;23(5):853-63. doi: 10.1091/mbc.E11-12-0992. Epub 2012 Jan 19.
7
Cortactin releases the brakes in actin- based motility by enhancing WASP-VCA detachment from Arp2/3 branches.Cortactin 通过增强 WASP-VCA 与 Arp2/3 分支的脱离来释放肌动蛋白基于运动的制动器。
Curr Biol. 2011 Dec 20;21(24):2092-7. doi: 10.1016/j.cub.2011.11.010. Epub 2011 Dec 8.
8
Actin filament severing by cofilin is more important for assembly than constriction of the cytokinetic contractile ring.肌动蛋白丝的断裂由束丝蛋白完成,这对于收缩环的装配比收缩更为重要。
J Cell Biol. 2011 Oct 31;195(3):485-98. doi: 10.1083/jcb.201103067. Epub 2011 Oct 24.
9
A temporal model of cofilin regulation and the early peak of actin barbed ends in invasive tumor cells.肌动蛋白结合蛋白调控的时相模型和侵袭性肿瘤细胞中肌动蛋白突出端的早期峰。
Biophys J. 2011 Apr 20;100(8):1883-92. doi: 10.1016/j.bpj.2011.02.036.
10
Human spire interacts with the barbed end of the actin filament.人源螺旋与肌动蛋白丝的带刺末端相互作用。
J Mol Biol. 2011 Apr 22;408(1):18-25. doi: 10.1016/j.jmb.2010.12.045. Epub 2011 Feb 16.

有不止一种方法来构建大象模型。肌动蛋白细胞骨架的实验驱动建模。

There is more than one way to model an elephant. Experiment-driven modeling of the actin cytoskeleton.

机构信息

Richard D. Berlin Center for Cell Analysis and Modeling, University of Connecticut Health Center, Farmington, Connecticut, USA.

出版信息

Biophys J. 2013 Feb 5;104(3):520-32. doi: 10.1016/j.bpj.2012.12.044.

DOI:10.1016/j.bpj.2012.12.044
PMID:23442903
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3566448/
Abstract

Mathematical modeling has established its value for investigating the interplay of biochemical and mechanical mechanisms underlying actin-based motility. Because of the complex nature of actin dynamics and its regulation, many of these models are phenomenological or conceptual, providing a general understanding of the physics at play. But the wealth of carefully measured kinetic data on the interactions of many of the players in actin biochemistry cries out for the creation of more detailed and accurate models that could permit investigators to dissect interdependent roles of individual molecular components. Moreover, no human mind can assimilate all of the mechanisms underlying complex protein networks; so an additional benefit of a detailed kinetic model is that the numerous binding proteins, signaling mechanisms, and biochemical reactions can be computationally organized in a fully explicit, accessible, visualizable, and reusable structure. In this review, we will focus on how comprehensive and adaptable modeling allows investigators to explain experimental observations and develop testable hypotheses on the intracellular dynamics of the actin cytoskeleton.

摘要

数学建模已经确立了其在研究肌动蛋白基运动的生化和力学机制相互作用方面的价值。由于肌动蛋白动力学及其调节的复杂性,许多此类模型是现象学或概念性的,为发挥作用的物理学提供了一般理解。但是,关于肌动蛋白生物化学中许多参与者相互作用的精心测量的动力学数据丰富,迫切需要创建更详细和准确的模型,使研究人员能够剖析单个分子成分的相互依赖作用。此外,没有人的思维可以吸收复杂蛋白质网络背后的所有机制;因此,详细的动力学模型的另一个好处是,众多的结合蛋白、信号机制和生化反应可以在完全显式、可访问、可视化和可重复使用的结构中进行计算组织。在这篇综述中,我们将重点介绍综合和适应性建模如何使研究人员能够解释实验观察结果,并对肌动蛋白细胞骨架的细胞内动力学提出可测试的假设。