肌球蛋白与肌动蛋白结合的限制因素。 - Suppr

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超能文献

Constraints on the attachment of myosin to actin.

作者信息

Tregear R

机构信息

AFRC Institute of Animal Physiology & Genetics Research, Babraham, Cambridge.

出版信息

J Muscle Res Cell Motil. 1988 Aug;9(4):293-5. doi: 10.1007/BF01773872.

DOI:10.1007/BF01773872

PMID:3220948

Abstract

摘要

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本文引用的文献

Fraction of myosin heads bound to thin filaments in rigor fibrils from insect flight and vertebrate muscles.来自昆虫飞行肌和脊椎动物肌肉的强直原纤维中与细肌丝结合的肌球蛋白头部比例。

Nature. 1981 Oct 22;293(5834):664-6. doi: 10.1038/293664a0.

Geometrical constraints affecting crossbridge formation in insect flight muscle.影响昆虫飞行肌中横桥形成的几何约束

J Muscle Res Cell Motil. 1984 Feb;5(1):3-24. doi: 10.1007/BF00713149.

The structure and disposition of crossbridges in deep-etched fish muscle.深蚀刻鱼肌肉中横桥的结构与分布

J Muscle Res Cell Motil. 1984 Aug;5(4):363-86. doi: 10.1007/BF00818256.

Three-dimensional reconstruction of rigor insect flight muscle from tilted thin sections.基于倾斜薄片的昆虫僵直飞行肌肉的三维重建

Nature. 1984;310(5975):285-91. doi: 10.1038/310285a0.

Orientation of spin-labeled myosin heads in glycerinated muscle fibers.甘油化肌纤维中自旋标记肌球蛋白头部的取向

Biophys J. 1980 Dec;32(3):891-906. doi: 10.1016/S0006-3495(80)85024-7.

All myosin heads form bonds with actin in rigor rabbit skeletal muscle.在尸僵的兔骨骼肌中，所有肌球蛋白头部均与肌动蛋白形成键。

Biochemistry. 1980 May 13;19(10):2265-9. doi: 10.1021/bi00551a042.

Induced changes in orientation of the cross-bridges of glycerinated insect flight muscle.甘油处理的昆虫飞行肌横桥取向的诱导变化。

Nature. 1965 Sep 18;207(5003):1276-80. doi: 10.1038/2071276a0.

Structure of insect fibrillar flight muscle in the presence and absence of ATP.有ATP和无ATP情况下昆虫纤维状飞行肌肉的结构

J Mol Biol. 1972 Sep 14;70(1):85-104. doi: 10.1016/0022-2836(72)90165-9.

Rigor crossbridge structure in tilted single filament layers and flared-X formations from insect flight muscle.来自昆虫飞行肌肉的倾斜单丝层和喇叭形-X 结构中的强直横桥结构。

J Mol Biol. 1985 Sep 5;185(1):145-76. doi: 10.1016/0022-2836(85)90188-3.

Actomyosin structure in contracting muscle detected by rapid freezing.

Nature. 1985;317(6033):182-4. doi: 10.1038/317182a0.

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