On the mechanism for inactivation of cytochalasin binding activity associated with F-actin and spectrin-band 4.1-actin complex by sulfhydryl reagents
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference14 articles.
1. Cytochalasins block actin filament elongation by binding to high affinity sites associated with F-actin.
2. Cytochalasins inhibit nuclei-induced actin polymerization by blocking filament elongation.
3. Mechanism of action of cytochalasin B on actin
4. High affinity binding of [3H]dihydrocytochalasin B to peripheral membrane proteins related to the control of cell shape in the human red cell.
5. Inhibition of actin polymerization by mercurials without removal of bound nucleotide
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1. Effects of domain-specific erythrocyte membrane modulators on acetylcholinesterase and NADH:Cytochrome b5 reductase activities;Archives of Biochemistry and Biophysics;1990-07
2. N-Ethylmaleimide causes mechanical fragility and accumulation of spectrin dimers in the rat erythrocyte membrane;Biochemical and Biophysical Research Communications;1985-07
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