Position of Mercenaria regulatory light-chain Cys50 site on the surface of myosin visualized by electron microscopy
Author:
Funder
American Heart Association
National Institutes of Health
Publisher
Elsevier BV
Subject
Molecular Biology,Structural Biology
Reference38 articles.
1. Interaction of skeletal myosin light chains with calcium ions
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3. Cross-linking between translationally equivalent sites on the two heads of myosin. Relationship to energy transfer results between the same pair of sites.
4. Regulatory light-chains and scallop myosin: Full dissociation, reversibility and co-operative effects
5. Interhead fluorescence energy transfer between probes attached to translationally equivalent sites on the regulatory light chains of scallop myosin
Cited by 4 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. Invertebrate muscles: Thin and thick filament structure; molecular basis of contraction and its regulation, catch and asynchronous muscle;Progress in Neurobiology;2008-10
2. Mapping single cysteine mutants of light chain 2 in chicken skeletal myosin.;Journal of Biological Chemistry;1992-10
3. On the relationship between distance information derived from cross-linking and from resonance energy transfer, with specific reference to sites located on myosin heads;Biophysical Journal;1991-06
4. Proximity relationships between sites on myosin and actin. Resonance energy transfer determination of the following distances, using a hybrid myosin: those between Cys-55 on the Mercenaria regulatory light chain, SH-1 on the Aequipecten myosin heavy chain, and Cys-374 of actin;Biochemistry;1991-04
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