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Spectroscopic studies on invertebrate myosins and light chains.

作者信息

Chantler P D, Szent-Györgyi A G

出版信息

Biochemistry. 1978 Dec 12;17(25):5440-8. doi: 10.1021/bi00618a018.

DOI:10.1021/bi00618a018
PMID:215199
Abstract
摘要

相似文献

1
Spectroscopic studies on invertebrate myosins and light chains.无脊椎动物肌球蛋白和轻链的光谱学研究。
Biochemistry. 1978 Dec 12;17(25):5440-8. doi: 10.1021/bi00618a018.
2
Conformational differences in the myosin-ADP complex in myofibrils and isolated myosin.
FEBS Lett. 1973 Mar 15;30(3):305-8. doi: 10.1016/0014-5793(73)80675-1.
3
Fish myofibrillar protein and lipid interaction in aqueous media as detected by isotope labeling, sucrose gradient centrifugation, polyacrylamide electrophoresis and electron paramagnetic resonance.通过同位素标记、蔗糖梯度离心、聚丙烯酰胺电泳和电子顺磁共振检测水介质中鱼肌原纤维蛋白与脂质的相互作用。
Adv Exp Med Biol. 1977;86A:657-86. doi: 10.1007/978-1-4684-3282-4_40.
4
The use of spin labels in the study of muscle proteins.
Ann N Y Acad Sci. 1973 Dec 31;222:574-87. doi: 10.1111/j.1749-6632.1973.tb15288.x.
5
Fluorescence intensity and UV absorption changes accompanying dissociation and association of regulatory light chain of scallop adductor myosin.扇贝闭壳肌肌球蛋白调节性轻链解离与缔合过程中伴随的荧光强度及紫外吸收变化
J Biochem. 1983 Oct;94(4):1061-6. doi: 10.1093/oxfordjournals.jbchem.a134448.
6
Interaction of skeletal myosin light chains with calcium ions.骨骼肌肌球蛋白轻链与钙离子的相互作用。
Biochemistry. 1978 Jun 13;17(12):2319-25. doi: 10.1021/bi00605a010.
7
Characterization of homologous divalent metal ion binding sites of vertebrate and molluscan myosins using electron paramagnetic resonance spectroscopy.利用电子顺磁共振波谱对脊椎动物和软体动物肌球蛋白的同源二价金属离子结合位点进行表征
J Mol Biol. 1979 May 25;130(3):317-36. doi: 10.1016/0022-2836(79)90544-8.
8
Rotational dynamics of actin-bound intermediates of the myosin adenosine triphosphatase cycle in myofibrils.肌原纤维中肌球蛋白三磷酸腺苷酶循环的肌动蛋白结合中间体的旋转动力学。
Biophys J. 1994 Jul;67(1):250-61. doi: 10.1016/S0006-3495(94)80476-X.
9
Homologous metal-binding sites of myosin regulatory light chains revealed by the paramagnetic manganous ion [proceedings].顺磁性锰离子揭示的肌球蛋白调节轻链的同源金属结合位点[会议论文集]
Biochem Soc Trans. 1978;6(6):1262-4. doi: 10.1042/bst0061262.
10
Demonstration of mechanochemical coupling in systems containing actin, atp and non-aggregating active myosin derivatives.在含有肌动蛋白、三磷酸腺苷(ATP)和非聚集性活性肌球蛋白衍生物的系统中机械化学偶联的证明。
J Mechanochem Cell Motil. 1974 Mar;2(4):295-306.

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Flexibility within the heads of muscle myosin-2 molecules.肌肉肌球蛋白-2 分子头部的灵活性。
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Invertebrate muscles: thin and thick filament structure; molecular basis of contraction and its regulation, catch and asynchronous muscle.
无脊椎动物肌肉:细肌丝和粗肌丝结构;收缩及其调节的分子基础、牵张肌和异步肌。
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4
Conservation of the regulated structure of folded myosin 2 in species separated by at least 600 million years of independent evolution.在经历至少6亿年独立进化的不同物种中,折叠态肌球蛋白2的调控结构得以保留。
Proc Natl Acad Sci U S A. 2008 Apr 22;105(16):6022-6. doi: 10.1073/pnas.0707846105. Epub 2008 Apr 14.
5
Evaluation of the symmetric model for myosin-linked regulation: effect of site-directed mutations in the regulatory light chain on scallop myosin.肌球蛋白相关调节的对称模型评估:调节轻链中定点突变对扇贝肌球蛋白的影响。
Biochem J. 2003 Aug 15;374(Pt 1):89-96. doi: 10.1042/BJ20030404.
6
Microsecond rotational dynamics of spin-labeled myosin regulatory light chain induced by relaxation and contraction of scallop muscle.扇贝肌肉舒张和收缩诱导的自旋标记肌球蛋白调节轻链的微秒级旋转动力学
Biochemistry. 1998 Oct 13;37(41):14428-36. doi: 10.1021/bi9808363.
7
Photolabeling evidence for calcium-induced conformational changes at the ATP binding site of scallop myosin.扇贝肌球蛋白ATP结合位点钙诱导构象变化的光标记证据
Proc Natl Acad Sci U S A. 1993 Jan 1;90(1):35-9. doi: 10.1073/pnas.90.1.35.
8
Properties of the non-specific calcium-binding sites of rabbit skeletal-muscle myosin.兔骨骼肌肌球蛋白非特异性钙结合位点的特性
Biochem J. 1980 Jan 1;185(1):265-8. doi: 10.1042/bj1850265.
9
Influence of myosin heavy chains on the Ca2+-binding properties of light chain, LC2.肌球蛋白重链对轻链LC2钙离子结合特性的影响。
Biochem J. 1981 Mar 1;193(3):925-34. doi: 10.1042/bj1930925.
10
Divalent metal ion binding and subunit interactions in myosins: a critical review.肌球蛋白中二价金属离子结合与亚基相互作用:批判性综述。
J Muscle Res Cell Motil. 1980 Sep;1(3):255-77. doi: 10.1007/BF00711931.