Consequences of reacting the thiols of myosin subfragment 1
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00590a020
Reference30 articles.
1. Studies on “active centers” of L-myosin
2. Electron paramagnetic resonance and nanosecond fluorescence depolarization studies on creatine-phosphokinase interaction with myosin and its fragments
3. Spectrophotometric Study of the Reaction of Protein Sulfhydryl Groups with Organic Mercurials
4. Conformational change accompanying modification of myosin ATPase
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1. SH1 (Cysteine 717) of Smooth Muscle Myosin: Its Role in Motor Function;Biochemistry;1999-08-19
2. Kinetic Investigation of the Ligand Dependence of Rabbit Skeletal Muscle Myosin Subfragment 1 Cys-697 and Cys-707 Reactivities;Biochemistry;1997-09-01
3. Effect of lysine methylation and other ATPase modulators on the active site of myosin subfragment 1.;Proceedings of the National Academy of Sciences;1994-08-30
4. Cross-linking myosin subfragment 1 Cys-697 and Cys-707 modifies ATP and actin binding site interactions;Biophysical Journal;1993-09
5. Antibody and peptide probes of interactions between the SH1-SH2 region of myosin subfragment 1 and actin's N-terminus;Biochemistry;1992-11
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