F-actin-myosin-subfragment-1 (S1) Interactions. Identification of the Refractory State of S1 with the S1 Dimer
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1995.00524.x/fullpdf
Reference19 articles.
1. MgATPase activity of myosin subfragment 1
2. Rabbit skeletal myosin heads in solution, as observed by ultracentrifugation and freeze-fracture electron microscopy: dimerization and maximum chord
3. Cross-bridge model of muscle contraction. Quantitative analysis
4. Single myosin molecule mechanics: piconewton forces and nanometre steps
5. Interaction of heavy meromyosin and subfragment 1 with actin. Physical measurements in the presence and absence of adenosine triphosphate
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1. Water and Muscle Contraction;International Journal of Molecular Sciences;2008-08-18
2. Steady-state kinetics of MgATP splitting by native myosin RLC-free subfragment 1;Biochimica et Biophysica Acta (BBA) - General Subjects;2001-05
3. The myosin motor: muscle contraction and in vitro movement;Biochimica et Biophysica Acta (BBA) - General Subjects;2000-04
4. Myosin thick filaments from adult rabbit skeletal muscles;Biochimica et Biophysica Acta (BBA) - General Subjects;1999-11
5. Dimerization of Native Myosin LC2(RLC)-Free Subfragment 1 from Adult Rabbit Skeletal Muscle;Biochemistry;1998-10-01
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