Literature DB >> 4947306

Formation of acto-H-meromyosin and acto-subfragment-1 complexes and their dissociation by adenosine triphosphate.

K Takeuchi, Y Tonomura.   

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Year:  1971        PMID： 4947306     DOI： 10.1093/oxfordjournals.jbchem.a129710

Source DB:  PubMed          Journal:  J Biochem        ISSN： 0021-924X            Impact factor:   3.387


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  3 in total

1.  Formation of a ternary complex: actin, 5'-adenylyl imidodiphosphate, and the subfragments of myosin.

Authors:  L E Greene; E Eisenberg
Journal:  Proc Natl Acad Sci U S A       Date:  1978-01       Impact factor: 11.205

2.  Cooperativity in F-actin: chemical modifications of actin monomers affect the functional interactions of myosin with unmodified monomers in the same actin filament.

Authors:  E Prochniewicz; E Katayama; T Yanagida; D D Thomas
Journal:  Biophys J       Date:  1993-07       Impact factor: 4.033

3.  A novel 36,000-dalton actin-binding protein purified from microfilaments in Physarum plasmodia which aggregates actin filaments and blocks actin-myosin interaction.

Authors:  S Ogihara; Y Tonomura
Journal:  J Cell Biol       Date:  1982-06       Impact factor: 10.539
  3 in total

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