长久而认真地审视钙调蛋白的紧密结合。 - Suppr

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Taking a long, hard look at calmodulin's warm embrace.

作者信息

Török K, Whitaker M

机构信息

Department of Physiology, University College London, UK.

出版信息

Bioessays. 1994 Apr;16(4):221-4. doi: 10.1002/bies.950160402.

DOI:10.1002/bies.950160402

PMID:8031297

Abstract

摘要

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Taking a long, hard look at calmodulin's warm embrace.长久而认真地审视钙调蛋白的紧密结合。

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Calmodulin's warm embrace.钙调蛋白的紧密结合。

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引用本文的文献

Thermodynamics of Calcium binding to the Calmodulin N-terminal domain to evaluate site-specific affinity constants and cooperativity.钙与钙调蛋白N端结构域结合的热力学，以评估位点特异性亲和常数和协同性。

J Biol Inorg Chem. 2015 Jul;20(5):905-19. doi: 10.1007/s00775-015-1275-1. Epub 2015 Jun 13.

Reply: A MAP by Any Other Name Would Still Bind to Microtubules.回复：换个名字的微管相关蛋白（MAP）仍会与微管结合。

Plant Cell. 1994 Dec;6(12):1699-1702. doi: 10.1105/tpc.6.12.1699.

Evidence for Opposing Effects of Calmodulin on Cortical Microtubules.钙调蛋白对皮层微管产生相反作用的证据。

Plant Physiol. 1996 Nov;112(3):1079-1087. doi: 10.1104/pp.112.3.1079.

Sequential assignment of 1H, 15N, 13C resonances and secondary structure of human calmodulin-like protein determined by NMR spectroscopy.通过核磁共振光谱法确定人钙调蛋白样蛋白的1H、15N、13C共振峰的顺序归属及二级结构。

Protein Sci. 1998 Nov;7(11):2421-30. doi: 10.1002/pro.5560071120.

Interaction with calmodulin is required for the function of Spc110p, an essential component of the yeast spindle pole body.与钙调蛋白的相互作用是酵母纺锤体极体的必需组成部分Spc110p发挥功能所必需的。

EMBO J. 1994 Sep 15;13(18):4329-42. doi: 10.1002/j.1460-2075.1994.tb06753.x.

Gain-of-function mutations in a human calmodulin-like protein identify residues critical for calmodulin action in yeast.人类类钙调蛋白中的功能获得性突变确定了酵母中钙调蛋白作用的关键残基。

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