Cap Z(3632) is a contaminant and the major inhibitor of actin neiwork formation in conventional actin preparations
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference6 articles.
1. Identification of a factor in conventional muscle actin preparations which inhibits actin filament self-association
2. Purification and initial characterization of a protein from skeletal muscle that caps the barbed ends of actin filaments.
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4. Chapter 18 Purification of Muscle Actin
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1. Cross-Linked Dimers with Nucleating Activity in Actin Prepared from Muscle Acetone Powder,;Biochemistry;1999-12-09
2. Effects of Chlorpromazine on Actin Polymerization: Slackening of Filament Elongation and Filament Annealing;Archives of Biochemistry and Biophysics;1999-09
3. Quantitation of cap Z in conventional actin preparations and methods for further purification of actin;Cell Motility and the Cytoskeleton;1995
4. Cytochalasin B may shorten actin filaments by a mechanism independent of barbed end capping;Biochemical Pharmacology;1994-05
5. Interaction of thymosin .beta.4 with muscle and platelet actin: implications for actin sequestration in resting platelets;Biochemistry;1992-07-01
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