Ryanodine receptors of striated muscles: a complex channel capable of multiple interactions.

No abstract is available for this paper.

• Publication year

  1997

• Venue

  Physiological Reviews

• Publication date

  1997-07-01

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.1152/PHYSREV.1997.77.3.699PMID 9234963
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• Cardiac muscle

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• Biochemical Characterization and Molecular Cloning of Cardiac Triadin (*)

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• The human cardiac muscle ryanodine receptor-calcium release channel: identification, primary structure and topological analysis.

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• Tissue‐specific alternative splicing of mouse brain type ryanodine receptor/calcium release channel mRNA

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• Properties of Ryr3 Ryanodine Receptor Isoform in Mammalian Brain (*)

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• Two structural configurations of the skeletal muscle calcium release channel

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• Enhanced dihydropyridine receptor channel activity in the presence of ryanodine receptor

  1996cited by this paper
• Formation of junctions involved in excitation-contraction coupling in skeletal and cardiac muscle.

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• Functional properties of inositol 1,4,5-trisphosphate receptor and Ca2+ signaling.

  1996cited by this paper
• Differential distribution of ryanodine receptor type 3 (RyR3) gene product in mammalian skeletal muscles.

  1996cited by this paper
• Effects of rapamycin on ryanodine receptor/Ca(2+)-release channels from cardiac muscle.

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• Interaction between Ryanodine and Neomycin Binding Sites on Ca Release Channel from Skeletal Muscle Sarcoplasmic Reticulum (*)

  1996cited by this paper
• Similar Ca2+ dependences of [3H]ryanodine binding to alpha- and beta-ryanodine receptors purified from bullfrog skeletal muscle in an isotonic medium.

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• Binding sites of monoclonal antibodies and dihydropyridine receptor alpha 1 subunit cytoplasmic II-III loop on skeletal muscle triadin fusion peptides.

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• Association of Triadin with the Ryanodine Receptor and Calsequestrin in the Lumen of the Sarcoplasmic Reticulum (*)

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