Critical Amino Acid Residues Determine the Binding Affinity and the Ca2+ Release Efficacy of Maurocalcine in Skeletal Muscle Cells

This publication has 24 references indexed in Scilit:

• Maurocalcine and Peptide A Stabilize Distinct Subconductance States of Ryanodine Receptor Type 1, Revealing a Proportional Gating Mechanism
  Journal of Biological Chemistry, 2003
• Imperatoxin A (IpTx_a) from Pandinus imperator stimulates [³H]ryanodine binding to RyR3 channels
  FEBS Letters, 2001
• Altered inhibition of the rat skeletal ryanodine receptor/calcium release channel by magnesium in the presence of ATP.
  Pflügers Archiv - European Journal of Physiology, 2001
• Chemical synthesis and characterization of maurocalcine, a scorpion toxin that activates Ca2+ release channel/ryanodine receptors
  Published by Wiley ,2000
• Activation of Ryanodine Receptors by Imperatoxin A and a Peptide Segment of the II-III Loop of the Dihydropyridine Receptor
  Journal of Biological Chemistry, 1999
• Protein–protein interactions in intracellular Ca2+-release channel function
  Biochemical Journal, 1999
• Identification of the Minimum Essential Region in the II-III Loop of the Dihydropyridine Receptor α₁ Subunit Required for Activation of Skeletal Muscle-Type Excitation−Contraction Coupling
  Biochemistry, 1998
• Primary structure and synthesis of Imperatoxin A (IpTx_a), a peptide activator of Ca²⁺ release channels/ryanodine receptors
  FEBS Letters, 1997
• Peptide Probe of Ryanodine Receptor Function IMPERATOXIN A, A PEPTIDE FROM THE VENOM OF THE SCORPION PANDINUS IMPERATOR, SELECTIVELY ACTIVATES SKELETAL-TYPE RYANODINE RECEPTOR ISOFORMS
  Journal of Biological Chemistry, 1995
• Scorpion toxins targeted against the sarcoplasmic reticulum Ca(2+)-release channel of skeletal and cardiac muscle.
  Proceedings of the National Academy of Sciences, 1992