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TRDN gene

Known as: TRDN, TRIADIN, TRISK 
National Institutes of Health

Related topics

Related topics

1 relation
Trdn protein, rat

Papers overview

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Highly Cited
2004
Highly Cited
2004
The role of calsequestrin, triadin, and junctin in conferring cardiac ryanodine receptor responsiveness to luminal calcium.
Review
2004
Review
2004
Calsequestrin and the calcium release channel of skeletal and cardiac muscle.
Review
1999
Review
1999
Redox regulation of signal transduction in cardiac and smooth muscle.
In addition to the well-known property of reactive oxygen species (ROS) to cause non-specific cellular damage, the potential role… 
Highly Cited
1998
Highly Cited
1998
Regulation of Ca2+ signaling in transgenic mouse cardiac myocytes overexpressing calsequestrin.
To probe the physiological role of calsequestrin in excitation-contraction coupling, transgenic mice overexpressing cardiac… 
Highly Cited
1998
Highly Cited
1998
Cardiac-specific Overexpression of Mouse Cardiac Calsequestrin Is Associated with Depressed Cardiovascular Function and Hypertrophy in Transgenic Mice*
Calsequestrin is a high capacity Ca2+-binding protein in the sarcoplasmic reticulum (SR) lumen. To elucidate the functional role… 
Highly Cited
1997
Highly Cited
1997
Complex Formation between Junctin, Triadin, Calsequestrin, and the Ryanodine Receptor
Several key proteins have been localized to junctional sarcoplasmic reticulum which are important for Ca2+ release. These include… 
Highly Cited
1995
Highly Cited
1995
Association of Triadin with the Ryanodine Receptor and Calsequestrin in the Lumen of the Sarcoplasmic Reticulum (*)
Triadin is a major membrane protein that is specifically localized in the junctional sarcoplasmic reticulum of skeletal muscle… 
Highly Cited
1995
Highly Cited
1995
Immunolocalization of sarcolemmal dihydropyridine receptor and sarcoplasmic reticular triadin and ryanodine receptor in rabbit ventricle and atrium
The subcellular distribution of sarcolemmal dihydropyridine receptor (DHPR) and sarcoplasmic reticular triadin and Ca2+ release… 
Highly Cited
1995
Highly Cited
1995
Purification, Primary Structure, and Immunological Characterization of the 26-kDa Calsequestrin Binding Protein (Junctin) from Cardiac Junctional Sarcoplasmic Reticulum (*)
Previously we identified a protein of apparent M = 26,000 as the major calsequestrin binding protein in junctional sarcoplasmic… 
Highly Cited
1995
Highly Cited
1995
Raised intracellular [Ca2+] abolishes excitation‐contraction coupling in skeletal muscle fibres of rat and toad.
1. Raising the intracellular [Ca2+] for 10 s at 23 degrees C abolished depolarization‐induced force responses in mechanically… 
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