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Insertion of Multi-pass Transmembrane Proteins in the RER01:29

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The rough ER membrane synthesizes, assembles, and embeds transmembrane proteins in diverse topologies. These proteins function as transporters or channels and can remain in the ER membrane or are sent to the Golgi complex, lysosome, and cell membrane.
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Related Experiment Video

Updated: Jun 1, 2026

Purification of the Cystic Fibrosis Transmembrane Conductance Regulator Protein Expressed in Saccharomyces cerevisiae
15:12

Purification of the Cystic Fibrosis Transmembrane Conductance Regulator Protein Expressed in Saccharomyces cerevisiae

Published on: May 10, 2014

CFTR three-dimensional structure.

Robert C Ford1, James Birtley, Mark F Rosenberg

  • 1Faculty of Life Sciences, Manchester Interdisciplinary Biocentre, The University of Manchester, Manchester, UK. bob.ford@manchester.ac.uk

Methods in Molecular Biology (Clifton, N.J.)
|May 20, 2011
PubMed
Summary
This summary is machine-generated.

The Cystic Fibrosis Transmembrane conductance Regulator (CFTR) functions as an ion channel, distinct from other ATP-binding cassette transporters. This review details methods used to study CFTR structure and function.

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Expression and Purification of the Human Lipid-sensitive Cation Channel TRPC3 for Structural Determination by Single-particle Cryo-electron Microscopy

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Last Updated: Jun 1, 2026

Purification of the Cystic Fibrosis Transmembrane Conductance Regulator Protein Expressed in Saccharomyces cerevisiae
15:12

Purification of the Cystic Fibrosis Transmembrane Conductance Regulator Protein Expressed in Saccharomyces cerevisiae

Published on: May 10, 2014

Expression and Purification of the Cystic Fibrosis Transmembrane Conductance Regulator Protein in Saccharomyces cerevisiae
14:56

Expression and Purification of the Cystic Fibrosis Transmembrane Conductance Regulator Protein in Saccharomyces cerevisiae

Published on: March 10, 2012

Expression and Purification of the Human Lipid-sensitive Cation Channel TRPC3 for Structural Determination by Single-particle Cryo-electron Microscopy
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Expression and Purification of the Human Lipid-sensitive Cation Channel TRPC3 for Structural Determination by Single-particle Cryo-electron Microscopy

Published on: January 7, 2019

Area of Science:

  • Membrane protein biophysics
  • Ion channel function
  • Molecular biology

Background:

  • The ATP-binding cassette (ABC) transporter family is well-characterized.
  • CFTR is a unique ABC protein functioning as an ion channel.
  • Understanding CFTR is crucial for cystic fibrosis research.

Purpose of the Study:

  • To review methodologies for studying CFTR.
  • To highlight techniques enabling structural and functional data acquisition for CFTR.
  • To provide insights into CFTR research advancements.

Main Methods:

  • Biophysical techniques for ion channel analysis.
  • Structural biology approaches (e.g., cryo-EM, X-ray crystallography).
  • Biochemical assays for protein characterization.

Main Results:

  • Detailed discussion of various experimental methods applicable to CFTR.
  • Explanation of how these methods yield structural and functional insights.
  • Highlighting the success in characterizing CFTR's unique transport mechanism.

Conclusions:

  • Multiple advanced methods have been successfully applied to study CFTR.
  • These techniques have significantly advanced our understanding of CFTR structure and ion channel activity.
  • Continued application of these methods will further elucidate CFTR function.