Enhanced binding of calmodulin to the ryanodine receptor corrects contractile dysfunction in failing hearts | Zendy

Akihiro Hino | Zendy; Masafumi Yano | Zendy; Takayoshi Kato | Zendy; Masakazu Fukuda | Zendy; Takeshi Suetomi | Zendy; Makoto Ono | Zendy; Wakako Murakami | Zendy; Takehisa Susa | Zendy; Shinichi Okuda | Zendy; Masahiro Doi | Zendy; Shigeki Kobayashi | Zendy; Takeshi Yamamoto | Zendy; Noritaka Koseki | Zendy; Hiroyuki Kyushiki | Zendy; Noriaki Ikemoto | Zendy; Masunori Matsuzaki | Zendy

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Enhanced binding of calmodulin to the ryanodine receptor corrects contractile dysfunction in failing hearts

Author(s) -

Akihiro Hino,

Masafumi Yano,

Takayoshi Kato,

Masakazu Fukuda,

Takeshi Suetomi,

Makoto Ono,

Wakako Murakami,

Takehisa Susa,

Shinichi Okuda,

Masahiro Doi,

Shigeki Kobayashi,

Takeshi Yamamoto,

Noritaka Koseki,

Hiroyuki Kyushiki,

Noriaki Ikemoto,

Masunori Matsuzaki

Publication year - 2012

Publication title -

cardiovascular research

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.774

H-Index - 219

eISSN - 1755-3245

pISSN - 0008-6363

DOI - 10.1093/cvr/cvs271

Subject(s) - ryanodine receptor , ryanodine receptor 2 , calmodulin , medicine , myocyte , endocrinology , endoplasmic reticulum , ryr1 , chemistry , calcium , biology , microbiology and biotechnology

The channel function of the cardiac ryanodine receptor (RyR2) is modulated by calmodulin (CaM). However, the involvement of CaM in aberrant Ca(2+) release in diseased hearts remains unclear. Here, we investigated the pathogenic role of defective CaM binding to the RyR2 in the channel dysfunction associated with heart failure.

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