Interaction of Cap Z with actin. The NH2-terminal domains of the alpha 1 and beta subunits are not required for actin capping, and alpha 1 beta and alpha 2 beta heterodimers bind differentially to actin.-Reference-Cited by-同舟云学术

Interaction of Cap Z with actin. The NH2-terminal domains of the alpha 1 and beta subunits are not required for actin capping, and alpha 1 beta and alpha 2 beta heterodimers bind differentially to actin.

Published:1994-03 Issue:9 Volume:269 Page:6992-6998
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Casella J.F.,Torres M.A.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference20 articles.

1. Purification and initial characterization of a protein from skeletal muscle that caps the barbed ends of actin filaments.

2. Cap Z(36/32), a barbed end actin-capping protein, is a component of the Z-line of skeletal muscle.

3. Ca2+-independent F-actin Capping Proteins

4. Identification of a widespread nuclear actin binding protein

5. Purification, characterization, and immunofluorescence localization of Saccharomyces cerevisiae capping protein

Cited by 28 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Traceable stimulus-dependent rapid molecular changes in dendritic spines in the brain;Scientific Reports;2020-09-17

2. Variants in CAPZA2, a member of an F-actin capping complex, cause intellectual disability and developmental delay;Human Molecular Genetics;2020-04-27

3. Actin capping proteins, CapZ (β-actinin) and tropomodulin in amphioxus striated muscle;Gene;2012-11

4. Capzb2 Interacts with β-Tubulin to Regulate Growth Cone Morphology and Neurite Outgrowth;PLoS Biology;2009-10-06

5. Muscle Giants: Molecular Scaffolds in Sarcomerogenesis;Physiological Reviews;2009-10