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Export of Misfolded Proteins out of the ER01:32

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After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...
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According to the theory of resonance, if two or more Lewis structures with the same arrangement of atoms can be written for a molecule, ion, or radical, the actual distribution of electrons is an average of that shown by the various Lewis structures.
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Updated: Jan 4, 2026

Single-Molecule Förster Resonance Energy Transfer Methods for Real-Time Investigation of the Holliday Junction Resolution by GEN1
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hERG Function in Light of Structure.

Gail A Robertson1, João H Morais-Cabral2

  • 1Department of Neuroscience, School of Medicine and Public Health, University of Wisconsin-Madison, Madison, Wisconsin.

Biophysical Journal
|November 1, 2019
PubMed
Summary
This summary is machine-generated.

The human ether-a-go-go-related gene1 (hERG) channel

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Area of Science:

  • Biophysics
  • Molecular Biology
  • Cardiology

Background:

  • The human ether-a-go-go-related gene1 (hERG) ion channel is a critical target for long QT syndrome.
  • Understanding hERG's unique biophysical properties is essential for cardiac safety and drug development.

Purpose of the Study:

  • To provide a biophysical perspective on the unique structural and functional aspects of the hERG channel.
  • To integrate recent structural data with functional insights and identify key unanswered questions.

Main Methods:

  • Analysis of recent high-resolution X-ray crystallography and cryo-electron microscopy structures.
  • Integration of structural findings with existing functional and biochemical data.

Main Results:

  • Revealed unique structural features: "nonswapped" transmembrane architecture, an "intrinsic ligand," and hydrophobic pockets near a small pore cavity.
  • Advanced understanding of drug block and inactivation mechanisms.

Conclusions:

  • hERG's unique structure presents a complex challenge for understanding its specific function.
  • Further investigation is required to fully elucidate hERG channel mechanisms and drug interactions.