测量处于强直状态的兔骨骼肌肌原纤维中与肌动蛋白结合的肌球蛋白头部的比例。 - Suppr

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超能文献

Measurement of the fraction of myosin heads bound to actin in rabbit skeletal myofibrils in rigor.

作者信息

Lovell S J, Harrington W F

出版信息

J Mol Biol. 1981 Jul 15;149(4):659-74. doi: 10.1016/0022-2836(81)90352-1.

DOI:10.1016/0022-2836(81)90352-1

PMID:6273587

Abstract

摘要

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Measurement of the fraction of myosin heads bound to actin in rabbit skeletal myofibrils in rigor.测量处于强直状态的兔骨骼肌肌原纤维中与肌动蛋白结合的肌球蛋白头部的比例。

J Mol Biol. 1981 Jul 15;149(4):659-74. doi: 10.1016/0022-2836(81)90352-1.

Actin-attached and detached crossbridges in myofibrils: segregation into two populations according to their sensitivity to proteolytic digestion of myosin heavy chain.肌原纤维中附着和分离的横桥：根据其对肌球蛋白重链蛋白水解消化的敏感性分为两类。

J Muscle Res Cell Motil. 1986 Apr;7(2):167-78. doi: 10.1007/BF01753418.

Quantitative determination of myosin and actin in rabbit skeletal muscle.兔骨骼肌中肌球蛋白和肌动蛋白的定量测定。

J Mol Biol. 1983 Jul 25;168(1):123-41. doi: 10.1016/s0022-2836(83)80326-x.

Rigor cross-bridges bind to two actin monomers in thin filaments of rabbit psoas muscle.强直横桥与兔腰大肌细肌丝中的两个肌动蛋白单体结合。

J Mol Biol. 1995 Apr 28;248(2):294-307.

Cross-bridge movement and the conformational state of the myosin hinge in skeletal muscle.骨骼肌中肌球蛋白铰链的横桥运动和构象状态。

J Mol Biol. 1981 Jul 15;149(4):619-40. doi: 10.1016/0022-2836(81)90350-8.

Rotational dynamics of actin-bound myosin heads in active myofibrils.活性肌原纤维中肌动蛋白结合肌球蛋白头部的旋转动力学。

Biochemistry. 1993 Apr 13;32(14):3812-21. doi: 10.1021/bi00065a038.

Binding of myosin to actin in myofibrils during ATP hydrolysis.在ATP水解过程中，肌球蛋白与肌原纤维中的肌动蛋白结合。

Biochemistry. 1989 Feb 7;28(3):1307-13. doi: 10.1021/bi00429a054.

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.

The content of troponin, tropomyosin, actin, and myosin in rabbit skeletal muscle myofibrils.兔骨骼肌肌原纤维中肌钙蛋白、原肌球蛋白、肌动蛋白和肌球蛋白的含量。

Arch Biochem Biophys. 1974 Jun;162(2):436-41. doi: 10.1016/0003-9861(74)90202-1.

Binding of myosin cross-bridges to thin filaments of rabbit skeletal muscle.肌球蛋白横桥与兔骨骼肌细肌丝的结合。

Biochem Biophys Res Commun. 1999 May 19;258(3):628-31. doi: 10.1006/bbrc.1999.0319.

引用本文的文献

Radial stability of the actomyosin filament lattice in isolated skeletal myofibrils studied using atomic force microscopy.使用原子力显微镜研究分离的骨骼肌肌原纤维中肌动球蛋白丝晶格的径向稳定性。

J Physiol Sci. 2013 Jul;63(4):299-310. doi: 10.1007/s12576-013-0268-5. Epub 2013 May 21.

Cardiomyopathy mutations reveal variable region of myosin converter as major element of cross-bridge compliance.心肌病突变揭示肌球蛋白转换器可变区是横桥柔韧性的主要因素。

Biophys J. 2009 Aug 5;97(3):806-24. doi: 10.1016/j.bpj.2009.05.023.

State-dependent radial elasticity of attached cross-bridges in single skinned fibres of rabbit psoas muscle.兔腰大肌单根去皮纤维中附着横桥的状态依赖性径向弹性。

J Physiol. 1993 Feb;461:283-99. doi: 10.1113/jphysiol.1993.sp019514.

Structural features of cross-bridges in isometrically contracting skeletal muscle.等长收缩骨骼肌中横桥的结构特征。

Biophys J. 2002 May;82(5):2536-47. doi: 10.1016/S0006-3495(02)75597-5.

Mutation of the myosin converter domain alters cross-bridge elasticity.肌球蛋白转换器结构域的突变会改变横桥弹性。

Proc Natl Acad Sci U S A. 2002 Mar 19;99(6):3557-62. doi: 10.1073/pnas.062415899.

Backward movements of cross-bridges by application of stretch and by binding of MgADP to skeletal muscle fibers in the rigor state as studied by x-ray diffraction.通过X射线衍射研究发现，在强直状态下，施加拉伸以及使MgADP与骨骼肌纤维结合会导致横桥向后移动。

Biophys J. 1999 Apr;76(4):1770-83. doi: 10.1016/S0006-3495(99)77338-8.

X-ray diffraction studies of cross-bridges weakly bound to actin in relaxed skinned fibers of rabbit psoas muscle.对兔腰大肌松弛去皮纤维中与肌动蛋白弱结合的横桥进行的X射线衍射研究。

Biophys J. 1997 Nov;73(5):2292-303. doi: 10.1016/S0006-3495(97)78261-4.

Biophys J. 1994 Jul;67(1):250-61. doi: 10.1016/S0006-3495(94)80476-X.

State-dependent radial elasticity of attached cross-bridges in single skinned fibres of rabbit psoas muscle.兔腰大肌单根去皮纤维中附着横桥的状态依赖性径向弹性。

J Physiol. 1993 Jun;465:749-65. doi: 10.1113/jphysiol.1993.sp019704.

Parallel inhibition of active force and relaxed fiber stiffness by caldesmon fragments at physiological ionic strength and temperature conditions: additional evidence that weak cross-bridge binding to actin is an essential intermediate for force generation.在生理离子强度和温度条件下，钙调蛋白片段对主动张力和松弛纤维硬度的平行抑制：弱横桥与肌动蛋白结合是力产生的关键中间步骤的更多证据。

Biophys J. 1995 Jun;68(6):2404-18. doi: 10.1016/S0006-3495(95)80423-6.

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