Literature DB >> 4231746

Dependence of activity of myofibrillar ATPase on sarcomere length and calcium ion concentration.

Y Hayashi, Y Tonomura.   

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Year:  1968        PMID： 4231746     DOI： 10.1093/oxfordjournals.jbchem.a128736

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


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  5 in total

Review 1.  The substructure of myosin and the reaction mechanism of its adenosine triphosphatase.

Authors:  Y Tonomura; A Inoue
Journal:  Mol Cell Biochem       Date:  1974-12-20       Impact factor: 3.396

2.  ATPase activity in rapidly activated skinned muscle fibres.

Authors:  P J Griffiths; K Güth; H J Kuhn; J C Rüegg
Journal:  Pflugers Arch       Date:  1980-09       Impact factor: 3.657

3.  Mechanochemical coupling in muscle: attempts to measure simultaneously shortening and ATPase rates in myofibrils.

Authors:  C Lionne; F Travers; T Barman
Journal:  Biophys J       Date:  1996-02       Impact factor: 4.033

4.  Dissociation of force from myofibrillar MgATPase and stiffness at short sarcomere lengths in rat and toad skeletal muscle.

Authors:  D G Stephenson; A W Stewart; G J Wilson
Journal:  J Physiol       Date:  1989-03       Impact factor: 5.182

5.  Effect of cross-bridge kinetics on apparent Ca2+ sensitivity.

Authors:  P W Brandt; R N Cox; M Kawai; T Robinson
Journal:  J Gen Physiol       Date:  1982-06       Impact factor: 4.086
  5 in total

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