The Sigma-1 Receptor Binds to the Nav1.5 Voltage-gated Na+ Channel with 4-Fold Symmetry*

@inproceedings{Balasuriya2012TheSR,
  title={The Sigma-1 Receptor Binds to the Nav1.5 Voltage-gated Na+ Channel with 4-Fold Symmetry*},
  author={Dilshan Balasuriya and Andrew P. Stewart and David Crott{\`e}s and Franck Borg{\`e}se and Olivier Soriani and J Michael Edwardson},
  booktitle={The Journal of biological chemistry},
  year={2012}
}
The sigma-1 receptor (Sig1R) is up-regulated in many human tumors and plays a role in the control of cancer cell proliferation and invasiveness. At the molecular level, the Sig1R modulates the activity of various ion channels, apparently through a direct interaction. We have previously shown using atomic force microscopy imaging that the Sig1R binds to the trimeric acid-sensing ion channel 1A with 3-fold symmetry. Here, we investigated the interaction between the Sig1R and the Nav1.5 voltage… CONTINUE READING

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The Sigma-1 Receptor Binds to the Nav1.5 Voltage - gated Na+ Channel with 4-Fold Symmetry*. The sigma-1 receptor ( Sig1R ) is up - regulated in many human tumors and plays a role in the control of cancer cell proliferation and invasiveness .
The Sigma-1 Receptor Binds to the Nav1.5 Voltage - gated Na+ Channel with 4-Fold Symmetry*. The sigma-1 receptor ( Sig1R ) is up - regulated in many human tumors and plays a role in the control of cancer cell proliferation and invasiveness .
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