Functional analysis of the R1086H malignant hyperthermia mutation in the DHPR reveals an unexpected influence of the III-IV loop on skeletal muscle EC coupling.

@article{Wei2004FunctionalAO,
  title={Functional analysis of the R1086H malignant hyperthermia mutation in the DHPR reveals an unexpected influence of the III-IV loop on skeletal muscle EC coupling.},
  author={R. Wei{\ss} and K. O'connell and B. Flucher and P. Allen and M. Grabner and R. Dirksen},
  journal={American journal of physiology. Cell physiology},
  year={2004},
  volume={287 4},
  pages={
          C1094-102
        }
}
Malignant hyperthermia (MH) is an inherited pharmacogenetic disorder caused by mutations in the skeletal muscle ryanodine receptor (RyR1) and the dihydropyridine receptor (DHPR) alpha(1S)-subunit. We characterized the effects of an MH mutation in the DHPR cytoplasmic III-IV loop of alpha(1S) (R1086H) on DHPR-RyR1 coupling after reconstitution in dysgenic (alpha(1S) null) myotubes. Compared with wild-type alpha(1S), caffeine-activated Ca(2+) release occurred at approximately fivefold lower… Expand
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References

SHOWING 1-10 OF 58 REFERENCES
Functional Characterization of a Distinct Ryanodine Receptor Mutation in Human Malignant Hyperthermia-susceptible Muscle*
  • 87
  • PDF
Functional Effects of Central Core Disease Mutations in the Cytoplasmic Region of the Skeletal Muscle Ryanodine Receptor
  • 131
  • PDF
Malignant hyperthermia mutation Arg615Cys in the porcine ryanodine receptor alters voltage dependence of Ca2+ release
  • 56
  • Highly Influential
  • PDF
Formation of triads without the dihydropyridine receptor alpha subunits in cell lines from dysgenic skeletal muscle
  • 90
  • PDF
Ryanodine receptor mutations in malignant hyperthermia and central core disease
  • 335
  • Highly Influential
The II-III Loop of the Skeletal Muscle Dihydropyridine Receptor Is Responsible for the Bi-directional Coupling with the Ryanodine Receptor*
  • 184
  • PDF
Conformational coupling of DHPR and RyR1 in skeletal myotubes is influenced by long-range allosterism: evidence for a negative regulatory module.
  • 36
  • PDF
...
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2
3
4
5
...