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	High resolution crystal structures of free thrombin in the presence of K+ reveal the molecular basis of monovalent cation selectivity and an inactive slow form
	Carrell CJ; Bush LA; Mathews FS; Di Cera E
刊名	Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena
	2006
期号	3页码:177-184
关键词	thrombin allostery monovalent cation activated enzyme serine protease structure SERINE PROTEASES DIALKYLGLYCINE DECARBOXYLASE 3-DIMENSIONAL STRUCTURE SUBSTRATE RECOGNITION POTASSIUM AFFECTS CHAPERONE HSC70 ALPHA-THROMBIN NA+ BINDING ACTIVE-SITE SPECIFICITY
URL标识	查看原文
内容类型	期刊论文
URI标识	http://www.corc.org.cn/handle/1471x/6272942
专题	山东大学
作者单位	1.Univ Washington, Sch Med, Dept Biochem & Mol Biophys, St Louis, MO 63110 USA 2.State Key Laboratory of Coordination Chemistry
推荐引用方式 GB/T 7714	Carrell CJ,Bush LA,Mathews FS,et al. High resolution crystal structures of free thrombin in the presence of K+ reveal the molecular basis of monovalent cation selectivity and an inactive slow form[J]. Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena,2006(3):177-184.
APA	Carrell CJ,Bush LA,Mathews FS,&Di Cera E.(2006).High resolution crystal structures of free thrombin in the presence of K+ reveal the molecular basis of monovalent cation selectivity and an inactive slow form.Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena(3),177-184.
MLA	Carrell CJ,et al."High resolution crystal structures of free thrombin in the presence of K+ reveal the molecular basis of monovalent cation selectivity and an inactive slow form".Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena .3(2006):177-184.

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