共 89 条
Integrin activation by talin, kindlin and mechanical forces
被引:389
作者:

Sun, Zhiqi
论文数: 0 引用数: 0
h-index: 0
机构:
Max Planck Inst Biochem, Martinsried, Germany Max Planck Inst Biochem, Martinsried, Germany

Costell, Mercedes
论文数: 0 引用数: 0
h-index: 0
机构:
Univ Valencia, Valencia, Spain Max Planck Inst Biochem, Martinsried, Germany

Faessler, Reinhard
论文数: 0 引用数: 0
h-index: 0
机构:
Max Planck Inst Biochem, Martinsried, Germany Max Planck Inst Biochem, Martinsried, Germany
机构:
[1] Max Planck Inst Biochem, Martinsried, Germany
[2] Univ Valencia, Valencia, Spain
关键词:
STRUCTURAL BASIS;
NANOSCALE ARCHITECTURE;
ADHESION;
SHARPIN;
CONFORMATION;
RECOGNITION;
TRANSDUCTION;
INFLAMMATION;
EXTENSION;
MEMBRANE;
D O I:
10.1038/s41556-018-0234-9
中图分类号:
Q2 [细胞生物学];
学科分类号:
071009 ;
090102 ;
摘要:
Integrins are the major family of adhesion molecules that mediate cell adhesion to the extracellular matrix. They are essential for embryonic development and influence numerous diseases, including inflammation, cancer cell invasion and metastasis. In this Perspective, we discuss the current understanding of how talin, kindlin and mechanical forces regulate integrin affinity and avidity, and how integrin inactivators function in this framework.
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页码:25 / 31
页数:7
相关论文
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Vanderbilt Univ, Dept Med, Div Nephrol, Nashville, TN 37232 USA Max Planck Inst Biochem, Grp Mol Mechanotransduct, D-82152 Martinsried, Germany

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Tech Univ Munich, Dept Phys, D-85748 Garching, Germany
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Grashoff, Carsten
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