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European Heart Journal Advance Access originally published online on January 24, 2006
European Heart Journal 2006 27(7):764-765; doi:10.1093/eurheartj/ehi742
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© The European Society of Cardiology 2006. All rights reserved. For Permissions, please e-mail: journals.permissions@oxfordjournals.org

Functional significance of myofilament protein oxidation

Jolanda van der Velden*

Laboratory for Physiology, Institute for Cardiovascular Research, VU University Medical Center, Amsterdam, The Netherlands

* Corresponding author. Laboratory for Physiology, VUMC, van der Boechorststraat 7, 1081 BT, Amsterdam, The Netherlands, Tel: +31 20 4448113; fax: +31 20 4448255. E-mail address: j.vandervelden@vumc.nl

This editorial refers to ‘Oxidative modification of tropomyosin and myocardial dysfunction following coronary microembolization’{dagger} by M. Canton et al., on page 875

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During muscle contraction, a molecular interaction takes place between the myofilament proteins actin and myosin, which is triggered by a rise in intracellular calcium and is driven by the energy from ATP hydrolysis. The tropomyosin–troponin complex inhibits the actin–myosin interaction at low intracellular-free calcium. This inhibition is released when intracellular-free calcium increases and calcium binding to troponin C takes place resulting in a conformational change of the troponin–tropomyosin complex. Movement . . . [Full Text of this Article]


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Related articles in EHJ:

Oxidative modification of tropomyosin and myocardial dysfunction following coronary microembolization
Marcella Canton, Andreas Skyschally, Roberta Menabò, Kerstin Boengler, Petra Gres, Rainer Schulz, Michael Haude, Raimund Erbel, Fabio Di Lisa, and Gerd Heusch
EHJ 2006 27: 875-881. [Abstract] [FREE Full Text]  



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