JOURNAL ARTICLE

Bidirectional movement of actin filaments along tracks of heavy meromyosin and native thick filaments

Yoko Y. Toyoshima

Year: 1991 Journal:   Journal of Cell Science Vol: 1991 (Supplement_14)Pages: 83-85   Publisher: The Company of Biologists

Abstract

ABSTRACT Flexibility of the myosin molecule was studied by an in vitro motility assay in terms of the direction of actin movement. Actin filaments can move in both directions on tracks of heavy meromyosin made on a nitrocellulose surface, and, furthermore, along the native thick filaments passing over their central bare zone. These observations indicate that the myosin molecule has a considerable flexibility in interacting with actin filaments.

Keywords:
Heavy meromyosin Myosin Biology Actin Treadmilling Biophysics Meromyosin Motility Flexibility (engineering) Myosin head Actin remodeling Cell biology Protein filament Microfilament Cytoskeleton Actin cytoskeleton Myosin light-chain kinase Biochemistry Cell

Metrics

8
Cited By
0.71
FWCI (Field Weighted Citation Impact)
9
Refs
0.71
Citation Normalized Percentile
Is in top 1%
Is in top 10%

Citation History

Topics

Cardiomyopathy and Myosin Studies
Health Sciences →  Medicine →  Cardiology and Cardiovascular Medicine
Force Microscopy Techniques and Applications
Physical Sciences →  Physics and Astronomy →  Atomic and Molecular Physics, and Optics
Cellular Mechanics and Interactions
Life Sciences →  Biochemistry, Genetics and Molecular Biology →  Cell Biology

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