Literature DB >> 2736259

35 kDa proteins are not components of vertebrate smooth muscle thin filaments.

W Lehman1.   

Abstract

A 35 kDa protein present in vertebrate smooth muscle and capable of binding to purified actin does not appear to be a constituent of smooth-muscle thin filaments in vivo; instead, it is more likely to be a component easily solubilized from particulate material which then spuriously interacts with actin.

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Year:  1989        PMID: 2736259     DOI: 10.1016/0167-4838(89)90094-0

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  3 in total

1.  Functional interrelationship between calponin and caldesmon.

Authors:  R Makuch; K Birukov; V Shirinsky; R Dabrowska
Journal:  Biochem J       Date:  1991-11-15       Impact factor: 3.857

2.  Calponin and the composition of smooth muscle thin filaments.

Authors:  W Lehman
Journal:  J Muscle Res Cell Motil       Date:  1991-06       Impact factor: 2.698

3.  Calponin is required for agonist-induced signal transduction--evidence from an antisense approach in ferret smooth muscle.

Authors:  H D Je; S S Gangopadhyay; T D Ashworth; K G Morgan
Journal:  J Physiol       Date:  2001-12-01       Impact factor: 5.182

  3 in total

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