Zobrazeno 1 - 10
of 227
pro vyhledávání: '"Gerhard, Meissner"'
Publikováno v:
Proteins
Ryanodine receptor 1 (RyR1) is an intracellular calcium ion (Ca(2+)) release channel required for skeletal muscle contraction. Although cryo-electron microscopy identified binding sites of three coactivators Ca(2+), ATP and caffeine (CFF), the mechan
Publikováno v:
The Journal of Biological Chemistry
Ryanodine receptor type 1 (RyR1) releases Ca2+ ions from the sarcoplasmic reticulum of skeletal muscle cells to initiate muscle contraction. Multiple endogenous and exogenous effectors regulate RyR1, such as ATP, Ca2+, caffeine (Caf), and ryanodine.
Ryanodine receptor 1 (RyR1) is an intracellular calcium ion (Ca2+) release channel required for skeletal muscle contraction. Although cryo-electron microscopy identified binding sites of three coactivators Ca2+, ATP and caffeine (CFF), the mechanism
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5cdcf2594ec96555bda367f880364f29
https://doi.org/10.22541/au.162006886.62484150/v1
https://doi.org/10.22541/au.162006886.62484150/v1
Autor:
Venkat R. Chirasani, Hannah G. Addis, Naohiro Yamaguchi, Gerhard Meissner, Daniel A. Pasek, Le Xu, Nikolay V. Dokholyan
Publikováno v:
American Journal of Physiology-Cell Physiology. 317:C358-C365
Cryoelectron microscopy and mutational analyses have shown that type 1 ryanodine receptor (RyR1) amino acid residues RyR1-E3893, -E3967, and -T5001 are critical for Ca2+-mediated activation of skeletal muscle Ca2+ release channel. De novo missense mu
Autor:
Asima Chakraborty, Daniel A Pasek, Tai-Qin Huang, Angela C Gomez, Naohiro Yamaguchi, Mark E Anderson, Gerhard Meissner
Publikováno v:
PLoS ONE, Vol 9, Iss 8, p e104338 (2014)
In cardiac muscle, the release of calcium ions from the sarcoplasmic reticulum through ryanodine receptor ion channels (RyR2s) leads to muscle contraction. RyR2 is negatively regulated by calmodulin (CaM) and by phosphorylation of Ca2+/CaM-dependent
Externí odkaz:
https://doaj.org/article/2c7ef560bb6e49e5aa3ee8fb6c33ffea
Autor:
Gerhard Meissner, Jordan S. Carter, Venkat R. Chirasani, Nikolay V. Dokholyan, Naohiro Yamaguchi, Le Xu, Daniel A. Pasek
Publikováno v:
Journal of Biological Chemistry. 293:19501-19509
Cryo-electron micrograph studies recently have identified a Ca2+-binding site in the 2,200-kDa ryanodine receptor ion channel (RyR1) in skeletal muscle. To clarify the role of this site in regulating RyR1 activity, here we applied mutational, electro
Autor:
Gerhard Meissner
Publikováno v:
Encyclopedia of Biological Chemistry III ISBN: 9780128220405
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7b572d4e04caac814b8c9bfa4e47f782
https://doi.org/10.1016/b978-0-12-809633-8.21370-8
https://doi.org/10.1016/b978-0-12-809633-8.21370-8
Publikováno v:
PLoS ONE, Vol 8, Iss 1, p e54208 (2013)
Activation of the skeletal muscle ryanodine receptor (RyR1) complex results in the rapid release of Ca(2+) from the sarcoplasmic reticulum and muscle contraction. Dissociation of the small FK506 binding protein 12 subunit (FKBP12) increases RyR1 acti
Externí odkaz:
https://doaj.org/article/a58e27370f7c4e348e00418674e4863b
Autor:
Gerhard Meissner, Fanny Kortüm, Nikolay V. Dokholyan, Peter Meinecke, Frederike L. Harms, Le Xu, Kerstin Kutsche, Daniel A. Pasek, Venkat R. Chirasani
Publikováno v:
Cell Calcium
Ryanodine receptor ion channels (RyR1s) release Ca(2+) ions from the sarcoplasmic reticulum to regulate skeletal muscle contraction. By whole-exome sequencing, we identified the heterozygous RYR1 variant c.14767_14772del resulting in the in-frame del
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a9088e70c471e70d60d1a88f6f81a981
https://europepmc.org/articles/PMC7216825/
https://europepmc.org/articles/PMC7216825/