Literature DB >> 3956731

Polymerization of beta-like actin from scallop adductor muscle.

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Abstract

Scallop adductor muscle beta-like isoactin differs from rabbit skeletal muscle alpha-actin in the rate, extent and critical concentration of polymerization. The difference is temperature- and [KC1]-dependent. In the presence of DNase I scallop actin was shown to be depolymerized more rapidly than rabbit actin. It was suggested that the polymers formed by beta-actin are less stable than those formed by alpha-actin.

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Year:  1986        PMID： 3956731     DOI： 10.1016/0014-5793(86)80409-4

Source DB:  PubMed          Journal:  FEBS Lett        ISSN： 0014-5793            Impact factor:   4.124


  4 in total

1.  Comparative study of invertebrate actins: antigenic cross-reactivity versus sequence variability.

Authors:  H K Hue; Y Benyamin; C Roustan
Journal:  J Muscle Res Cell Motil       Date:  1989-04       Impact factor: 2.698

2.  Structural and functional variations in skeletal-muscle and scallop muscle actins.

Authors:  H K Hue; J P Labbé; M C Harricane; J C Cavadore; Y Benyamin; C Roustan
Journal:  Biochem J       Date:  1988-12-15       Impact factor: 3.857

Review 3.  Molecular genetics of actin function.

Authors:  E S Hennessey; D R Drummond; J C Sparrow
Journal:  Biochem J       Date:  1993-05-01       Impact factor: 3.857

Review 4.  The remodelling of actin composition as a hallmark of cancer.

Authors:  Rahul Suresh; Roberto J Diaz
Journal:  Transl Oncol       Date:  2021-03-21       Impact factor: 4.243
  4 in total

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