Both heads of tissue-derived smooth muscle heavy meromyosin bind to actin in the presence of ADP.
about
Cryo-atomic force microscopy of unphosphorylated and thiophosphorylated single smooth muscle myosin molecules.Smooth muscle myosin phosphorylated at single head shows sustained mechanical activity.The kinetics underlying the velocity of smooth muscle myosin filament sliding on actin filaments in vitro.Modeling smooth muscle myosin's two heads: long-lived enzymatic roles and phosphorylation-dependent equilibria.Ionic interactions play a role in the regulatory mechanism of scallop heavy meromyosin.Modification of interface between regulatory and essential light chains hampers phosphorylation-dependent activation of smooth muscle myosinKinetic and motor functions mediated by distinct regions of the regulatory light chain of smooth muscle myosin.The myosin C-loop is an allosteric actin contact sensor in actomyosinNovel sensors of the regulatory switch on the regulatory light chain of smooth muscle Myosin.The myosin cardiac loop participates functionally in the actomyosin interaction.
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Both heads of tissue-derived smooth muscle heavy meromyosin bind to actin in the presence of ADP.
description
2002 nî lūn-bûn
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2002年の論文
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name
Both heads of tissue-derived s ...... actin in the presence of ADP.
@en
Both heads of tissue-derived s ...... actin in the presence of ADP.
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type
label
Both heads of tissue-derived s ...... actin in the presence of ADP.
@en
Both heads of tissue-derived s ...... actin in the presence of ADP.
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prefLabel
Both heads of tissue-derived s ...... actin in the presence of ADP.
@en
Both heads of tissue-derived s ...... actin in the presence of ADP.
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P2860
P356
P1476
Both heads of tissue-derived s ...... actin in the presence of ADP.
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P2093
Zachary S DePew
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P304
P356
10.1074/JBC.M211016200
P407
P577
2002-12-02T00:00:00Z