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Molecular dynamic simulations of the binary complex of human tissue factor (TF(1-242) ) and factor VIIa (TF(1-242) /FVIIa) on a 4:1 POPC/POPS lipid bilayer.

作者信息

Lee C J, Wu S, Bartolotti L J, Pedersen L G

机构信息

Department of Chemistry, University of North Carolina, Chapel Hill, NC Department of Chemistry, East Carolina University, Greenville, NC, USA.

出版信息

J Thromb Haemost. 2012 Nov;10(11):2402-5. doi: 10.1111/j.1538-7836.2012.04920.x.

DOI:10.1111/j.1538-7836.2012.04920.x
PMID:22967237
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3537916/
Abstract
摘要

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1
Molecular dynamic simulations of the binary complex of human tissue factor (TF(1-242) ) and factor VIIa (TF(1-242) /FVIIa) on a 4:1 POPC/POPS lipid bilayer.在4:1的POPC/POPS脂质双分子层上对人组织因子（TF(1-242)）与因子VIIa的二元复合物（TF(1-242)/FVIIa）进行分子动力学模拟。
J Thromb Haemost. 2012 Nov;10(11):2402-5. doi: 10.1111/j.1538-7836.2012.04920.x.
2
A molecular dynamics simulation study to understand the effect of cholesterol and tissue factor palmitoylation on tissue factor-factor VIIa-factor Xa ternary complex in different lipid environments.一项分子动力学模拟研究，旨在了解胆固醇和组织因子棕榈酰化对不同脂质环境中组织因子-因子 VIIa-因子 Xa 三元复合物的影响。
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Phospholipid regulates the activation of factor X by tissue factor/factor VIIa (TF/VIIa) via substrate and product interactions.磷脂通过底物和产物相互作用调节组织因子/因子VIIa（TF/VIIa）对因子X的激活。
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Structural model of tissue factor (TF) and TF-factor VIIa complex in a lipid membrane: A combined experimental and computational study.组织因子（TF）与 TF-因子 VIIa 复合物在脂质膜中的结构模型：实验与计算的综合研究。
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Roles of the membrane-interactive regions of factor VIIa and tissue factor. The factor VIIa Gla domain is dispensable for binding to tissue factor but important for activation of factor X.凝血因子VIIa和组织因子的膜相互作用区域的作用。凝血因子VIIa的γ-羧基谷氨酸（Gla）结构域对于与组织因子的结合并非必需，但对凝血因子X的激活很重要。
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Blood clotting reactions on nanoscale phospholipid bilayers.纳米级磷脂双分子层上的血液凝固反应。
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A systematic approach for evaluating the role of surface-exposed loops in trypsin-like serine proteases applied to the 170 loop in coagulation factor VIIa.一种评估表面暴露环在类胰蛋白酶丝氨酸蛋白酶中作用的系统方法，应用于凝血因子VIIa的170环。
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Evolutionary conservation of the allosteric activation of factor VIIa by tissue factor in lamprey.七因子在文昌鱼中通过组织因子的别构激活的进化保守性。
J Thromb Haemost. 2018 Apr;16(4):734-748. doi: 10.1111/jth.13968. Epub 2018 Mar 12.

本文引用的文献

1
Atomic view of calcium-induced clustering of phosphatidylserine in mixed lipid bilayers.原子视角下的混合脂质双层中钙诱导的磷脂酰丝氨酸聚集。
Biochemistry. 2011 Mar 29;50(12):2264-73. doi: 10.1021/bi1013694. Epub 2011 Mar 3.
2
Dynamical view of membrane binding and complex formation of human factor VIIa and tissue factor.人凝血因子 VIIa 和组织因子的膜结合和复合物形成的动力学观点。
J Thromb Haemost. 2010 May;8(5):1044-53. doi: 10.1111/j.1538-7836.2010.03826.x. Epub 2010 Feb 24.
3
Alternatively spliced tissue factor - one cut too many?可变剪接的组织因子——切割过度？
Thromb Haemost. 2007 Jan;97(1):5-8. doi: 10.1160/th06-11-0670.
4
Raising the active site of factor VIIa above the membrane surface reduces its procoagulant activity but not factor VII autoactivation.将因子VIIa的活性位点提升至膜表面上方会降低其促凝血活性，但不会影响因子VII的自身激活。
J Biol Chem. 2006 Sep 8;281(36):26062-8. doi: 10.1074/jbc.M604915200. Epub 2006 Jul 11.
5
Scalable molecular dynamics with NAMD.使用 NAMD 的可扩展分子动力学
J Comput Chem. 2005 Dec;26(16):1781-802. doi: 10.1002/jcc.20289.
6
The tissue factor/factor VIIa/factor Xa complex: a model built by docking and site-directed mutagenesis.组织因子/因子VIIa/因子Xa复合物：通过对接和定点诱变构建的模型。
Proteins. 2003 Nov 15;53(3):640-8. doi: 10.1002/prot.10445.
7
Tissue factor positions and maintains the factor VIIa active site far above the membrane surface even in the absence of the factor VIIa Gla domain. A fluorescence resonance energy transfer study.组织因子即使在缺乏因子VIIaγ-羧基谷氨酸（Gla）结构域的情况下，也能将因子VIIa活性位点定位并维持在膜表面上方很远的位置。一项荧光共振能量转移研究。
J Biol Chem. 1997 Nov 28;272(48):30160-6. doi: 10.1074/jbc.272.48.30160.
8
The location of the active site of blood coagulation factor VIIa above the membrane surface and its reorientation upon association with tissue factor. A fluorescence energy transfer study.凝血因子VIIa活性位点在膜表面上方的位置及其与组织因子结合后的重新定向。一项荧光能量转移研究。
J Biol Chem. 1996 Nov 8;271(45):28168-75. doi: 10.1074/jbc.271.45.28168.
9
Substrate recognition by tissue factor-factor VIIa. Evidence for interaction of residues Lys165 and Lys166 of tissue factor with the 4-carboxyglutamate-rich domain of factor X.组织因子-因子VIIa对底物的识别。组织因子的赖氨酸165和赖氨酸166残基与因子X富含γ-羧基谷氨酸结构域相互作用的证据。
J Biol Chem. 1996 Sep 6;271(36):21752-7. doi: 10.1074/jbc.271.36.21752.
10
The crystal structure of the complex of blood coagulation factor VIIa with soluble tissue factor.凝血因子VIIa与可溶性组织因子复合物的晶体结构
Nature. 1996 Mar 7;380(6569):41-6. doi: 10.1038/380041a0.