Flexibility of Acanthamoeba Myosin Rod Minifilaments-Reference-Cited by-同舟云学术

Flexibility of Acanthamoeba Myosin Rod Minifilaments

Published:1999-05-11 Issue:22 Volume:38 Page:7243-7252
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Redowicz M. Jolanta¹,Hammer John A.¹,Bowers Blair¹,Zolkiewski Michal¹,Ginsburg Ann¹,Korn Edward D.¹,Rau Donald C.¹

Affiliation:

1. Laboratory of Cell Biology and Laboratory of Biochemistry, National Heart, Lung, and Blood Institute, and Laboratory of Physical and Structural Biology, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland, 20892

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi982679d

Reference41 articles.

1. Characterization of a second myosin from Acanthamoeba castellanii

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1. Computational simulations reveal that Abl activity controls cohesiveness of actin networks in growth cones;MOL BIOL CELL;2022

2. Computational simulations reveal that Abl activity controls cohesiveness of actin networks in growth cones;Molecular Biology of the Cell;2022-09-15

3. Computational simulations reveal that Abl activity controls cohesiveness of actin networks in growth cones;2021-11-02

4. Stable transfection of Acanthamoeba castellanii;Biochimica et Biophysica Acta (BBA) - Molecular Cell Research;2005-03

5. High flexibility of the actomyosin crossbridge resides in skeletal muscle myosin subfragment-2 as demonstrated by a new single molecule assay;Journal of Structural Biology;2005-02