Zobrazeno 1 - 10
of 39
pro vyhledávání: '"Daniel A. Pasek"'
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.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::78404ea88e6d2d9f7b54181373815385
http://europepmc.org/articles/PMC8408527
http://europepmc.org/articles/PMC8408527
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8c9ccc67b1da51aaa6e742620cb35fd7
https://doi.org/10.1152/ajpcell.00052.2019
https://doi.org/10.1152/ajpcell.00052.2019
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ccb4002d5378c1c3b4f62ef9660c7eae
https://doi.org/10.1074/jbc.ra118.004453
https://doi.org/10.1074/jbc.ra118.004453
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/
Autor:
Gerhard Meissner, Daniel A. Pasek, Ying Wang, Venkat R. Chirasani, Le Xu, David D. Mowrey, Nikolay V. Dokholyan
Publikováno v:
Journal of Biological Chemistry. 293:2015-2028
The ryanodine receptor ion channel RyR1 is present in skeletal muscle and has a large cytoplasmic N-terminal domain and smaller C-terminal pore-forming domain comprising six transmembrane helices, a pore helix, and a selectivity filter. The RyR1 S6 p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::adcd5c375c8d9cdf21a03a5c72772f1e
https://doi.org/10.1074/jbc.m117.803247
https://doi.org/10.1074/jbc.m117.803247
Publikováno v:
Cell Calcium. 66:62-70
The mammalian ryanodine receptor Ca2+ release channel (RyR) has a single conserved high affinity calmodulin (CaM) binding domain. However, the skeletal muscle RyR1 is activated and cardiac muscle RyR2 is inhibited by CaM at submicromolar Ca2+. This s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::32d393da500f980255837fa44403d6c3
https://doi.org/10.1016/j.ceca.2017.05.013
https://doi.org/10.1016/j.ceca.2017.05.013
Publikováno v:
Biophysical Journal. 120:280a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::469a8e8ab08fc342d64769d23a92bf81
https://doi.org/10.1016/j.bpj.2020.11.1783
https://doi.org/10.1016/j.bpj.2020.11.1783
Autor:
Le, Xu, Venkat R, Chirasani, Jordan S, Carter, Daniel A, Pasek, Nikolay V, Dokholyan, Naohiro, Yamaguchi, Gerhard, Meissner
Publikováno v:
The Journal of biological chemistry. 293(50)
Cryo-electron micrograph studies recently have identified a Ca(2+)-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, elect
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::d0ce6973df3753353ea445b21d620291
https://pubmed.ncbi.nlm.nih.gov/30341173
https://pubmed.ncbi.nlm.nih.gov/30341173
Autor:
Naohiro Yamaguchi, Gerhard Meissner, Venkat R. Chirasani, Hannah G. Addis, Jordan S. Carter, Le Xu, Daniel A. Pasek, Nikolay V. Dokholyan
Publikováno v:
Biophysical Journal. 116:520a-521a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f9f7413794d71c1f8764ce0101ec2646
https://doi.org/10.1016/j.bpj.2018.11.2807
https://doi.org/10.1016/j.bpj.2018.11.2807