在有和没有5'-三磷酸腺苷的情况下，砂囊平滑肌肌球蛋白亚片段1与肌动蛋白的结合。 - Suppr

Suppr

超能文献

Binding of gizzard smooth muscle myosin subfragment 1 to actin in the presence and absence of adenosine 5'-triphosphate.

作者信息

Greene L E, Sellers J R, Eisenberg E, Adelstein R S

出版信息

Biochemistry. 1983 Feb 1;22(3):530-5. doi: 10.1021/bi00272a002.

DOI:10.1021/bi00272a002

PMID:6838810

Abstract

摘要

相似文献

Binding of gizzard smooth muscle myosin subfragment 1 to actin in the presence and absence of adenosine 5'-triphosphate.在有和没有5'-三磷酸腺苷的情况下，砂囊平滑肌肌球蛋白亚片段1与肌动蛋白的结合。

Biochemistry. 1983 Feb 1;22(3):530-5. doi: 10.1021/bi00272a002.

Comparison of effects of smooth and skeletal muscle tropomyosins on interactions of actin and myosin subfragment 1.平滑肌和骨骼肌原肌球蛋白对肌动蛋白与肌球蛋白亚片段1相互作用的影响比较

Biochemistry. 1984 Aug 28;23(18):4150-5. doi: 10.1021/bi00313a022.

Dissociation of acto-H-meromyosin and that of acto-subfragment-1 induced by adenyl-5'-yl-imidodiphosphate: evidence for a ternary complex of F-actin, myosin head, and substrate.腺苷-5'-亚氨二磷酸诱导的肌动蛋白-H-肌球蛋白重酶解肌球蛋白以及肌动蛋白-亚片段1的解离：F-肌动蛋白、肌球蛋白头部和底物三元复合物的证据

J Biochem. 1980 Dec;88(6):1643-51. doi: 10.1093/oxfordjournals.jbchem.a133140.

The binding of myosin subfragment 1 to actin can be measured by proteolytic rates method.肌球蛋白亚片段1与肌动蛋白的结合可以通过蛋白水解速率法来测定。

J Biol Chem. 1987 Mar 25;262(9):4124-8.

Chemical crosslinking of myosin subfragment-1 to F-actin in the presence of nucleotide.在核苷酸存在的情况下，肌球蛋白亚片段-1与F-肌动蛋白的化学交联。

J Biochem. 1984 Aug;96(2):337-47. doi: 10.1093/oxfordjournals.jbchem.a134843.

Interaction of isozymes of myosin subfragment 1 with actin: effect of ionic strength and nucleotide.肌球蛋白亚片段1同工酶与肌动蛋白的相互作用：离子强度和核苷酸的影响

Biochemistry. 1984 Oct 9;23(21):4885-9. doi: 10.1021/bi00316a011.

Caldesmon inhibits skeletal actomyosin subfragment-1 ATPase activity and the binding of myosin subfragment-1 to actin.钙调蛋白抑制骨骼肌肌动球蛋白亚片段-1的ATP酶活性以及肌球蛋白亚片段-1与肌动蛋白的结合。

J Biol Chem. 1987 Apr 25;262(12):5711-6.

Chicken-gizzard actin. Interaction with skeletal-muscle myosin.鸡胗肌动蛋白。与骨骼肌肌球蛋白的相互作用。

Eur J Biochem. 1980 May;106(1):305-12.

Temperature-modulated binding of ADP and adenyl-5'-yl imidodiphosphate to myosin subfragment 1 studied by calorimetric titration.通过量热滴定研究ADP和腺苷-5'-亚氨基二磷酸与肌球蛋白亚片段1的温度调制结合。

J Biol Chem. 1981 Nov 25;256(22):11503-8.

Effect of tryptic digestion of myosin subfragment-1 on its binding to F-actin.肌球蛋白亚片段-1的胰蛋白酶消化对其与F-肌动蛋白结合的影响。

J Biochem. 1984 May;95(5):1343-8. doi: 10.1093/oxfordjournals.jbchem.a134741.

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Diffusion of myosin light chain kinase on actin: A mechanism to enhance myosin phosphorylation rates in smooth muscle.肌球蛋白轻链激酶在肌动蛋白上的扩散：一种提高平滑肌中肌球蛋白磷酸化速率的机制。

J Gen Physiol. 2015 Oct;146(4):267-80. doi: 10.1085/jgp.201511483.

Loop 1 dynamics in smooth muscle myosin: isoform specific differences modulate ADP release.平滑肌肌球蛋白中的环 1 动力学：同工型特异性差异调节 ADP 释放。

J Muscle Res Cell Motil. 2011 Aug;32(1):49-61. doi: 10.1007/s10974-011-9251-z. Epub 2011 Jun 5.

Folding and regulation in myosins II and V.肌球蛋白II和V的折叠与调控

J Muscle Res Cell Motil. 2007;28(7-8):363-70. doi: 10.1007/s10974-008-9134-0. Epub 2008 Apr 22.

cGMP-mediated phosphorylation of heat shock protein 20 may cause smooth muscle relaxation without myosin light chain dephosphorylation in swine carotid artery.环磷酸鸟苷（cGMP）介导的热休克蛋白20磷酸化可能导致猪颈动脉平滑肌舒张，而不伴有肌球蛋白轻链去磷酸化。

J Physiol. 2000 May 1;524 Pt 3(Pt 3):865-78. doi: 10.1111/j.1469-7793.2000.00865.x.

Cross-bridge attachment during high-speed active shortening of skinned fibers of the rabbit psoas muscle: implications for cross-bridge action during maximum velocity of filament sliding.兔腰大肌去皮肤肌纤维高速主动缩短过程中的横桥附着：对细丝滑动最大速度时横桥作用的启示。

Biophys J. 2000 Mar;78(3):1458-73. doi: 10.1016/S0006-3495(00)76699-9.

The effect of thin filament activation on the attachment of weak binding cross-bridges: A two-dimensional x-ray diffraction study on single muscle fibers.细肌丝激活对弱结合横桥附着的影响：对单根肌纤维的二维X射线衍射研究

Biophys J. 1999 Mar;76(3):1494-513. doi: 10.1016/S0006-3495(99)77309-1.

Coupling of protein surface hydrophobicity change to ATP hydrolysis by myosin motor domain.肌球蛋白运动结构域将蛋白质表面疏水性变化与ATP水解相偶联。

Biophys J. 1997 Jan;72(1):18-23. doi: 10.1016/S0006-3495(97)78643-0.

Time-resolved electron microscopic analysis of the behavior of myosin heads on actin filaments after photolysis of caged ATP.对笼锁ATP光解后肌球蛋白头部在肌动蛋白丝上行为的时间分辨电子显微镜分析。

J Cell Biol. 1993 Jun;121(5):1053-64. doi: 10.1083/jcb.121.5.1053.

Enhanced force generation by smooth muscle myosin in vitro.体外平滑肌肌球蛋白产生增强的力量。

Proc Natl Acad Sci U S A. 1994 Jan 4;91(1):202-5. doi: 10.1073/pnas.91.1.202.

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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