Fibronectins, their fibrillogenesis, and in vivo functions.

Fibronectins, their fibrillogenesis, and in vivo functions.
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纤连蛋白,原纤维生成和体内功能。

DOI:
10.1101/cshperspect.a005041
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发表时间:
2011-07-01
影响因子:
7.2
通讯作者:
DeSimone DW
DeSimone DW
中科院分区:
生物学1区
文献类型:
--
作者:
Schwarzbauer JE;DeSimone DW

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纤维连接蛋白(FN)是一种多结构域蛋白,能够同时与细胞表面受体、胶原、蛋白多糖和其他FN分子结合。其中许多结构域和相互作用也涉及FN二聚体组装成多聚体纤维基质。在纤维形成过程中,FN何时、何地以及如何与其不同的伙伴结合必须加以控制和协调。FN纤维形成过程中的步骤,包括FN的自结合、受体活性和细胞内通路,多年来一直受到密切的研究。本文综述了FN的结构域组织,包括受选择性剪接控制的额外结构域和可变区。我们讨论了FN-FN和细胞-FN的相互作用如何在基质组装的启动和进展中发挥重要作用,使用来自细胞培养和胚胎模型系统的补充结果,增强了我们对这一过程的理解。
Fibronectin (FN) is a multidomain protein with the ability to bind simultaneously to cell surface receptors, collagen, proteoglycans, and other FN molecules. Many of these domains and interactions are also involved in the assembly of FN dimers into a multimeric fibrillar matrix. When, where, and how FN binds to its various partners must be controlled and coordinated during fibrillogenesis. Steps in the process of FN fibrillogenesis including FN self-association, receptor activities, and intracellular pathways have been under intense investigation for years. In this review, the domain organization of FN including the extra domains and variable region that are controlled by alternative splicing are described. We discuss how FN–FN and cell–FN interactions play essential roles in the initiation and progression of matrix assembly using complementary results from cell culture and embryonic model systems that have enhanced our understanding of this process.
DOI: 10.1016/0045-6039(83)90059-3
发表时间: 1983-01-01
期刊: CELL DIFFERENTIATION
影响因子: --
作者:
BOUCAUT, JC;DARRIBERE, T
通讯作者: DARRIBERE, T
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发表时间: 2009
期刊: Angiogenesis
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生物活性合成肽作为胚胎发育的探针:纤连蛋白功能的竞争性肽抑制剂抑制两栖动物胚胎中的胃肠液和鸟类胚胎中神经rest细胞迁移。
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发表时间: 1984-11
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DOI: 10.1074/jbc.272.40.24999
发表时间: 1997-10-03
影响因子: 4.8
作者:
Corbett, SA;Lee, L;Schwarzbauer, JE
通讯作者: Schwarzbauer, JE