MgADP Promotes Myosin Head Movement toward Actin at Low [Ca2+] to Increase Force Production and Ca2+-Sensitivity of Contraction in Permeabilized Porcine Myocardial Strips

Autor: Peter O. Awinda, Weikang Ma, Kyrah L. Turner, Jing Zhao, Henry Gong, Mindy S. Thompson, Kenneth S. Campbell, Thomas C. Irving, Bertrand C. W. Tanner

Publikováno v: International Journal of Molecular Sciences, Vol 23, Iss 23, p 15084 (2022)

Myosin cross-bridges dissociate from actin following Mg2+-adenosine triphosphate (MgATP) binding. Myosin hydrolyses MgATP into inorganic phosphate (Pi) and Mg2+-adenosine diphosphate (ADP), and release of these hydrolysis products drives chemo-mechan

Externí odkaz: https://doaj.org/article/4b3d2da720e0436f80c18278c270a1ce

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Downsizing the molecular spring of the giant protein titin reveals that skeletal muscle titin determines passive stiffness and drives longitudinal hypertrophy

Autor: J. D. T. Smith, Maya Adler, Johan Lindqvist, Jochen Gohlke, Joshua Strom, Robbert van der Pijl, Coen A.C. Ottenheijm, Balázs Kiss, Justin Kolb, Henk Granzier, Ambjorn Brynnel, Yaeren Hernandez

Publikováno v: eLife, 7:e40532. eLife Sciences Publications Limited
eLife
Brynnel, A, Hernandez, Y, Kiss, B, Lindqvist, J, Adler, M, Kolb, J, van der Pijl, R, Gohlke, J, Strom, J, Smith, J, Ottenheijm, C & Granzier, H L 2018, ' Downsizing the molecular spring of the giant protein titin reveals that skeletal muscle titin determines passive stiffness and drives longitudinal hypertrophy ', eLife, vol. 7, e40532 . https://doi.org/10.7554/eLife.40532, https://doi.org/10.7554/eLife.40532
eLife, Vol 7 (2018)

Titin, the largest protein known, forms an elastic myofilament in the striated muscle sarcomere. To establish titin’s contribution to skeletal muscle passive stiffness, relative to that of the extracellular matrix, a mouse model was created in whic

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c9eab670756f19aed3db23661d149b05
https://doi.org/10.7554/elife.40532

Troponin I phosphorylation in human myocardium in health and disease

Autor: Paul J.M. Wijnker, Ger J.M. Stienen, Anne M. Murphy, J. van der Velden

Publikováno v: Wijnker, P J M, Murphy, A M, Stienen, G J M & van der Velden, J 2014, ' Troponin I phosphorylation in human myocardium in health and disease ', Netherlands Heart Journal, vol. 22, no. 10, pp. 463-469 . https://doi.org/10.1007/s12471-014-0590-4
Netherlands Heart Journal, 22(10), 463-469. Bohn Stafleu van Loghum
Netherlands Heart Journal

Cardiac troponin I (cTnI) is well known as a biomarker for the diagnosis of myocardial damage. However, because of its central role in the regulation of contraction and relaxation in heart muscle, cTnI may also be a potential target for the treatment

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::00eafa87dd5913187b163a5d2287564f
https://hdl.handle.net/1871.1/f273ea18-5eee-4a85-aa7c-ab6b8df2b1d2