Literature DB >> 6255164

Identification of the divalent metal ion binding domain of myosin regulatory light chains using spin-labelling techniques.

C R Bagshaw, J Kendrick-Jones.   

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Year:  1980        PMID： 6255164     DOI： 10.1016/0022-2836(80)90392-7

Source DB:  PubMed          Journal:  J Mol Biol        ISSN： 0022-2836            Impact factor:   5.469


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  6 in total

Review 1.  Invertebrate muscles: thin and thick filament structure; molecular basis of contraction and its regulation, catch and asynchronous muscle.

Authors:  Scott L Hooper; Kevin H Hobbs; Jeffrey B Thuma
Journal:  Prog Neurobiol       Date:  2008-06-20       Impact factor: 11.685

Review 2.  Divalent metal ion binding and subunit interactions in myosins: a critical review.

Authors:  C R Bagshaw
Journal:  J Muscle Res Cell Motil       Date:  1980-09       Impact factor: 2.698

3.  The kinetics of bivalent metal ion dissociation from myosin subfragments.

Authors:  A J Bennett; C R Bagshaw
Journal:  Biochem J       Date:  1986-01-01       Impact factor: 3.857

4.  8-Anilino-1-naphthalenesulphonate, a fluorescent probe for the regulatory light chain binding site of scallop myosin.

Authors:  A J Bennett; N Patel; C Wells; C R Bagshaw
Journal:  J Muscle Res Cell Motil       Date:  1984-04       Impact factor: 2.698

5.  The mechanism of regulatory light chain dissociation from scallop myosin.

Authors:  A J Bennett; C R Bagshaw
Journal:  Biochem J       Date:  1986-01-01       Impact factor: 3.857

6.  The Dictyostelium class I myosin, MyoD, contains a novel light chain that lacks high-affinity calcium-binding sites.

Authors:  Marc A De La Roche; Sheu-Fen Lee; Graham P Côté
Journal:  Biochem J       Date:  2003-09-15       Impact factor: 3.857
  6 in total

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