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肉豆蔻酰化蛋白与膜的静电相互作用:简单的物理学,复杂的生物学。

Electrostatic interaction of myristoylated proteins with membranes: simple physics, complicated biology.

作者信息

Murray D, Ben-Tal N, Honig B, McLaughlin S

机构信息

Department of Physiology and Biophysics, SUNY Stony Brook 11794-8661, USA.

出版信息

Structure. 1997 Aug 15;5(8):985-9. doi: 10.1016/s0969-2126(97)00251-7.

DOI:10.1016/s0969-2126(97)00251-7
PMID:9309215
Abstract

Cell membrane association by several important peripheral proteins, such as Src, MARCKS, HIV-1 Gag, and K-Ras, requires nonspecific electrostatic interactions between a cluster of basic residues on the protein and acidic phospholipids in the plasma membrane. A simple theoretical model based on the nonlinear Poisson-Boltzmann equation describes well the experimentally measured electrostatic association between such proteins and the cell membrane.

摘要

几种重要的外周蛋白,如Src、MARCKS、HIV-1 Gag和K-Ras与细胞膜的结合,需要蛋白质上一簇碱性残基与质膜中酸性磷脂之间的非特异性静电相互作用。基于非线性泊松-玻尔兹曼方程的一个简单理论模型很好地描述了此类蛋白质与细胞膜之间实验测量的静电结合。

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Electrostatic interaction of myristoylated proteins with membranes: simple physics, complicated biology.肉豆蔻酰化蛋白与膜的静电相互作用:简单的物理学,复杂的生物学。
Structure. 1997 Aug 15;5(8):985-9. doi: 10.1016/s0969-2126(97)00251-7.
2
The myristoyl-electrostatic switch: a modulator of reversible protein-membrane interactions.肉豆蔻酰静电开关:可逆蛋白质-膜相互作用的调节剂。
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Electrostatics and the membrane association of Src: theory and experiment.静电学与Src的膜结合:理论与实验
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The MARCKS family of protein kinase-C substrates.蛋白激酶C底物的MARCKS家族。
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Phosphorylation reverses the membrane association of peptides that correspond to the basic domains of MARCKS and neuromodulin.磷酸化作用会逆转与肌醇蛋白激酶C底物(MARCKS)和神经调节蛋白的碱性结构域相对应的肽段与膜的结合。
Biophys J. 1994 Jul;67(1):227-37. doi: 10.1016/S0006-3495(94)80473-4.
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Binding of acylated peptides and fatty acids to phospholipid vesicles: pertinence to myristoylated proteins.酰化肽和脂肪酸与磷脂囊泡的结合:与肉豆蔻酰化蛋白的相关性。
Biochemistry. 1993 Oct 5;32(39):10436-43. doi: 10.1021/bi00090a020.
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Binding of basic peptides to membranes produces lateral domains enriched in the acidic lipids phosphatidylserine and phosphatidylinositol 4,5-bisphosphate: an electrostatic model and experimental results.碱性肽与膜的结合产生富含酸性脂质磷脂酰丝氨酸和磷脂酰肌醇4,5 - 二磷酸的侧向结构域:一个静电模型及实验结果。
Biophys J. 1998 Feb;74(2 Pt 1):731-44. doi: 10.1016/S0006-3495(98)73998-0.
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Structural Thermodynamics of myr-Src(2-19) Binding to Phospholipid Membranes.肉豆蔻酰化Src蛋白(2-19)与磷脂膜结合的结构热力学
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Binding of myristoylated alanine-rich protein kinase C substrate to phosphoinositides attenuates the phosphorylation by protein kinase C.豆蔻酰化富含丙氨酸的蛋白激酶C底物与磷酸肌醇的结合减弱了蛋白激酶C的磷酸化作用。
Arch Biochem Biophys. 1996 Feb 15;326(2):193-201. doi: 10.1006/abbi.1996.0065.
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Interactions of myristoylated alanine-rich C kinase substrate (MARCKS)-related protein with a novel solid-supported lipid membrane system (TRANSIL).富含肉豆蔻酰化丙氨酸的蛋白激酶C底物(MARCKS)相关蛋白与新型固体支持脂质膜系统(TRANSIL)的相互作用。
Anal Biochem. 1999 Mar 15;268(2):343-53. doi: 10.1006/abio.1998.3080.

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