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Purification of myosin I and myosin I heavy chain kinase from Acanthamoeba castellanii.

作者信息

Lynch T J, Brzeska H, Baines I C, Korn E D

出版信息

Methods Enzymol. 1991;196:12-23. doi: 10.1016/0076-6879(91)96004-b.

DOI:10.1016/0076-6879(91)96004-b
PMID:1851936
Abstract
摘要

相似文献

1
Purification of myosin I and myosin I heavy chain kinase from Acanthamoeba castellanii.从卡氏棘阿米巴中纯化肌球蛋白I和肌球蛋白I重链激酶。
Methods Enzymol. 1991;196:12-23. doi: 10.1016/0076-6879(91)96004-b.
2
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Autophosphorylation-independent activation of Acanthamoeba myosin I heavy chain kinase by plasma membranes.质膜对棘阿米巴肌球蛋白I重链激酶的非自磷酸化依赖性激活
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4
Acanthamoeba myosin I heavy chain kinase is activated by phosphatidylserine-enhanced phosphorylation.棘阿米巴肌球蛋白I重链激酶通过磷脂酰丝氨酸增强的磷酸化作用被激活。
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5
Purification and characterization of a myosin I heavy chain kinase from Acanthamoeba castellanii.来自卡氏棘阿米巴的肌球蛋白I重链激酶的纯化与鉴定
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6
Purification and characterization of a myosin heavy chain kinase from Dictyostelium discoideum.盘基网柄菌肌球蛋白重链激酶的纯化与特性分析
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7
Purification and characterization of a calmodulin-dependent myosin heavy chain kinase from intestinal brush border.来自肠刷状缘的钙调蛋白依赖性肌球蛋白重链激酶的纯化与特性分析
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Immunolocalization of myosin I heavy chain kinase in Acanthamoeba castellanii and binding of purified kinase to isolated plasma membranes.肌球蛋白I重链激酶在卡氏棘阿米巴中免疫定位及纯化激酶与分离的质膜的结合
J Cell Biol. 1991 Oct;115(1):109-19. doi: 10.1083/jcb.115.1.109.
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Inhibition of Acanthamoeba myosin I heavy chain kinase by Ca(2+)-calmodulin.钙调蛋白对棘阿米巴肌球蛋白I重链激酶的抑制作用。
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Purification of myosin from Ehrlich ascites tumour cells (phosphorylation of its light chain and heavy chain).
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引用本文的文献

1
Kinetic and equilibrium analysis of the myosin ATPase.肌球蛋白ATP酶的动力学与平衡分析
Methods Enzymol. 2009;455:157-92. doi: 10.1016/S0076-6879(08)04206-7.
2
Acanthamoeba myosin IC colocalizes with phosphatidylinositol 4,5-bisphosphate at the plasma membrane due to the high concentration of negative charge.由于高浓度的负电荷，棘阿米巴肌球蛋白IC在质膜处与磷脂酰肌醇4,5-二磷酸共定位。
J Biol Chem. 2008 Nov 14;283(46):32014-23. doi: 10.1074/jbc.M804828200. Epub 2008 Sep 4.
3
Myosin I heavy chain kinase: cloning of the full-length gene and acidic lipid-dependent activation by Rac and Cdc42.
肌球蛋白I重链激酶：全长基因的克隆以及Rac和Cdc42介导的酸性脂质依赖性激活
Proc Natl Acad Sci U S A. 1999 Jan 19;96(2):394-9. doi: 10.1073/pnas.96.2.394.
4
Analysis of the regulatory phosphorylation site in Acanthamoeba myosin IC by using site-directed mutagenesis.利用定点诱变分析棘阿米巴肌球蛋白IC中的调节性磷酸化位点。
Proc Natl Acad Sci U S A. 1998 Dec 22;95(26):15200-5. doi: 10.1073/pnas.95.26.15200.
5
Three-dimensional structure of Acanthamoeba castellanii myosin-IB (MIB) determined by cryoelectron microscopy of decorated actin filaments.通过对肌动蛋白丝进行标记的冷冻电子显微镜技术确定的卡氏棘阿米巴肌球蛋白-IB（MIB）的三维结构。
J Cell Biol. 1998 Apr 6;141(1):155-62. doi: 10.1083/jcb.141.1.155.
6
Arp2/3 complex from Acanthamoeba binds profilin and cross-links actin filaments.来自棘阿米巴原虫的Arp2/3复合物结合肌动蛋白结合蛋白并交联肌动蛋白丝。
Mol Biol Cell. 1998 Apr;9(4):841-52. doi: 10.1091/mbc.9.4.841.
7
Identification by mass spectrometry of the phosphorylated residue responsible for activation of the catalytic domain of myosin I heavy chain kinase, a member of the PAK/STE20 family.通过质谱鉴定负责激活肌球蛋白I重链激酶催化结构域的磷酸化残基，肌球蛋白I重链激酶是PAK/STE20家族的成员。
Proc Natl Acad Sci U S A. 1997 Aug 5;94(16):8503-8. doi: 10.1073/pnas.94.16.8503.
8
The amino acid sequence of the light chain of Acanthamoeba myosin IC.棘阿米巴肌球蛋白IC轻链的氨基酸序列。
J Muscle Res Cell Motil. 1997 Jun;18(3):395-8. doi: 10.1023/a:1018686428955.
9
p21-activated kinase has substrate specificity similar to Acanthamoeba myosin I heavy chain kinase and activates Acanthamoeba myosin I.p21激活激酶具有与棘阿米巴肌球蛋白I重链激酶相似的底物特异性，并能激活棘阿米巴肌球蛋白I。
Proc Natl Acad Sci U S A. 1997 Feb 18;94(4):1092-5. doi: 10.1073/pnas.94.4.1092.
10
Biochemical kinetic characterization of the Acanthamoeba myosin-I ATPase.棘阿米巴肌球蛋白-I ATP酶的生化动力学特性
J Cell Biol. 1996 Mar;132(6):1053-60. doi: 10.1083/jcb.132.6.1053.