.png){kind=icon}
返回
Actin Structure and Function
.png){kind=icon}
OA
AI
DOI：10.1146/annurev-biophys-042910-155359.png)
.png){kind=icon}
.png){kind=icon}
分享.png){kind=icon}
收藏
摘要
En 中文
Actin is the most abundant protein in most eukaryotic cells. It is highly conserved and participates in more protein-protein interactions than any known protein. These properties, along with its ability to transition between monomeric (G-actin) and filamentous (F-actin) states under the control of nucleotide hydrolysis, ions, and a large number of actin-binding proteins, make actin a critical player in many cellular functions, ranging from cell motility and the maintenance of cell shape and polarity to the regulation of transcription. Moreover, the interaction of filamentous actin with myosin forms the basis of muscle contraction. Owing to its central role in the cell, the actin cytoskeleton is also disrupted or taken over by numerous pathogens. Here we review structures of G-actin and F-actin and discuss some of the interactions that control the polymerization and disassembly of actin.
Keyword:
X-ray crystallography
electron microscopy
fiber diffraction
actin-binding-proteins
AI总结
对已上传原文的论文进行重点信息的提取，主要内容包括：简要概述、研究摘要、背景介绍、关键亮点、图文解析、展望与总结。
期刊
IF:
13.7
论文数:
361
被引数:
4.2K
机构
引用论文
分享收藏Structural basis for the recruitment of profilin-actin complexes during filament elongation by Ena/VASPEna/VASP在细丝伸长过程中招募profilin-肌动蛋白复合物的结构基础.png)
EMBO JOURNALOAAI
EMBO JOURNALIF8.3
OAAI分享收藏Molecular structure of the ParM polymer and the mechanism leading to its nucleotide-driven dynamic instabilityEMBO JOURNALOAAI
EMBO JOURNALIF8.3
OAAI分享收藏
查看更多内容