Inhibition of sliding movement of F-actin by crosslinking emphasizes the role of actin structure in the mechanism of motility.
Prochniewicz, E
Inhibition of sliding movement of F-actin by crosslinking emphasizes the role of actin structure in the mechanism of motility. [electronic resource] - Journal of molecular biology Dec 1990 - 761-72 p. digital
Publication Type: Journal Article
0022-2836
10.1016/0022-2836(90)90397-5 doi
Actins--metabolism
Actomyosin--metabolism
Adenosine Triphosphatases--metabolism
Adenosine Triphosphate--physiology
Animals
Chemical Precipitation
Cross-Linking Reagents
Microscopy, Fluorescence
Movement--physiology
Myosin Subfragments--metabolism
Structure-Activity Relationship
Inhibition of sliding movement of F-actin by crosslinking emphasizes the role of actin structure in the mechanism of motility. [electronic resource] - Journal of molecular biology Dec 1990 - 761-72 p. digital
Publication Type: Journal Article
0022-2836
10.1016/0022-2836(90)90397-5 doi
Actins--metabolism
Actomyosin--metabolism
Adenosine Triphosphatases--metabolism
Adenosine Triphosphate--physiology
Animals
Chemical Precipitation
Cross-Linking Reagents
Microscopy, Fluorescence
Movement--physiology
Myosin Subfragments--metabolism
Structure-Activity Relationship