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本文引用的文献

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Structural analysis of sensor domains from the TMAO-responsive histidine kinase receptor TorS.三甲胺N-氧化物(TMAO)响应性组氨酸激酶受体TorS的传感结构域的结构分析
Structure. 2009 Sep 9;17(9):1195-204. doi: 10.1016/j.str.2009.07.015.
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The core signaling proteins of bacterial chemotaxis assemble to form an ultrastable complex.细菌趋化性的核心信号蛋白组装形成超稳定复合物。
Biochemistry. 2009 Jul 28;48(29):6975-87. doi: 10.1021/bi900641c.
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Structural analysis of ligand stimulation of the histidine kinase NarX.组氨酸激酶NarX的配体刺激的结构分析
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Bacterial chemoreceptors: high-performance signaling in networked arrays.细菌化学感受器:网络化阵列中的高效信号传导
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Sensor complexes regulating two-component signal transduction.调节双组分信号转导的传感器复合体
Curr Opin Struct Biol. 2007 Dec;17(6):706-15. doi: 10.1016/j.sbi.2007.08.019. Epub 2007 Oct 29.
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Structure of the entire cytoplasmic portion of a sensor histidine-kinase protein.传感组氨酸激酶蛋白整个胞质部分的结构
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Tryptophan residues flanking the second transmembrane helix (TM2) set the signaling state of the Tar chemoreceptor.第二跨膜螺旋(TM2)两侧的色氨酸残基决定了Tar化学感受器的信号传导状态。
Biochemistry. 2005 Feb 1;44(4):1268-77. doi: 10.1021/bi048969d.
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Side chains at the membrane-water interface modulate the signaling state of a transmembrane receptor.膜 - 水界面处的侧链调节跨膜受体的信号传导状态。
Biochemistry. 2004 Feb 24;43(7):1763-70. doi: 10.1021/bi0360206.
9
A NarX-Tar chimera mediates repellent chemotaxis to nitrate and nitrite.一种NarX-Tar嵌合体介导对硝酸盐和亚硝酸盐的趋避性化学趋向。
Mol Microbiol. 2002 May;44(3):709-19. doi: 10.1046/j.1365-2958.2002.02902.x.
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Transmembrane signaling in bacterial chemoreceptors.细菌化学感受器中的跨膜信号传导。
Trends Biochem Sci. 2001 Apr;26(4):257-65. doi: 10.1016/s0968-0004(00)01770-9.

活塞再次上升。

The piston rises again.

作者信息

Falke Joseph J, Erbse Annette H

出版信息

Structure. 2009 Sep 9;17(9):1149-51. doi: 10.1016/j.str.2009.08.005.

DOI:10.1016/j.str.2009.08.005
PMID:19748334
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2902780/
Abstract

Previous evidence has indicated that the transmembrane signal in bacterial chemoeceptors is carried by the piston displacement of a membrane-spanning signaling helix. Hendrickson and coworkers (Cheung and Hendrickson, 2009; Moore and Hendrickson, 2009) now provide structural evidence that suggests piston transmembrane signaling is widely conserved in bacterial receptors that control ubiquitous two-component signaling pathways.

摘要

先前的证据表明,细菌化学感受器中的跨膜信号是由跨膜信号螺旋的活塞位移来传递的。亨德里克森及其同事(张和亨德里克森,2009年;摩尔和亨德里克森,2009年)现在提供的结构证据表明,活塞跨膜信号在控制普遍存在的双组分信号通路的细菌受体中广泛保守。