How cholesterol interacts with membrane proteins: an exploration of cholesterol-binding sites including CRAC, CARC, and tilted domains

@inproceedings{Fantini2013HowCI,
  title={How cholesterol interacts with membrane proteins: an exploration of cholesterol-binding sites including CRAC, CARC, and tilted domains},
  author={Jacques Fantini and Francisco J. Barrantes},
  booktitle={Front. Physiol.},
  year={2013}
}
The plasma membrane of eukaryotic cells contains several types of lipids displaying high biochemical variability in both their apolar moiety (e.g., the acyl chain of glycerolipids) and their polar head (e.g., the sugar structure of glycosphingolipids). Among these lipids, cholesterol is unique because its biochemical variability is almost exclusively restricted to the oxidation of its polar -OH group. Although generally considered the most rigid membrane lipid, cholesterol can adopt a broad… CONTINUE READING
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Integrated methods for the construction of three - dimensional models and computational probing of structure - function relations in G protein - coupled receptors

  • J. Ballesteros, H. Weinstein
  • Methods Neurosci .
  • 1995
Highly Influential
1 Excerpt

Integrated methods for the construction of three-dimensional models and computational probing of structure-function relations in G

  • J. Ballesteros, H. Weinstein
  • 1995
Highly Influential
2 Excerpts

4:31. doi: 10.3389/fphys. 2013.00031 This article was submitted to Frontiers in Membrane Physiology and Biophysics, a specialty of Frontiers in Physiology

  • Front. Physiol
  • 2013

How cholesterol interacts with membrane proteins: an exploration of cholesterol-binding sites including CRAC, CARC, and tilted domains

  • J Citation Fantini, FJ Barrantes
  • 2013

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