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Use of Detergents to Study Membrane Rafts: The Good, the Bad, and the Ugly
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H. Shogomori
Published/Copyright:
June 1, 2005
Abstract
Eukaryotic cell membranes contain microdomains called lipid rafts, which are cholesterol-rich domains in which lipid acyl chains are tightly packed and highly extended. A variety of proteins associate preferentially with rafts, and this raft association is important in a wide range of functions. A powerful and widely used method for studying lipid rafts takes advantage of their insolubility in non-ionic detergents. Here we describe the basis of detergent insolubility, and review strengths, limitations, and unresolved puzzles regarding this method.
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Published Online: 2005-06-01
Published in Print: 2003-09-28
Copyright © 2003 by Walter de Gruyter GmbH & Co. KG
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Articles in the same Issue
- Paper of the Year 2002
- Terminal Differentiation of Epithelia
- Use of Detergents to Study Membrane Rafts: The Good, the Bad, and the Ugly
- Protein Structure Similarity as Guiding Principle for Combinatorial Library Design
- The Making of a Professional Secretory Cell: Architectural and Functional Changes in the ER during B Lymphocyte Plasma Cell Differentiation
- No Superoxide Dismutase Activity of Cellular Prion Protein in vivo
- A Nucleosome-Free dG-dC-Rich Sequence Element Promotes Constitutive Transcription of the Essential Yeast RIO1 Gene
- Phosphatidylinositol-3,5-Bisphosphate Is a Potent and Selective Inhibitor of Acid Sphingomyelinase
- Function and Structure of N-Terminal and C-Terminal Domains of Calcineurin B Subunit
- Verification of the Interaction of a Tryparedoxin Peroxidase with Tryparedoxin by ESI-MS/MS
- Kinin-B1 Receptors in Ischaemia-Induced Pancreatitis: Functional Importance and Cellular Localisation
- Bioactivatable, Membrane-Permeant Analogs of Cyclic Nucleotides as Biological Tools for Growth Control of C6 Glioma Cells
- Human Cathepsin H: Deletion of the Mini-Chain Switches Substrate Specificity from Aminopeptidase to Endopeptidase
- Nitridergic Platelet Pathway Activation by Hementerin, a Metalloprotease from the Leech Haementeria depressa
