A general amphipathic α-helical motif for sensing membrane curvature-Reference-Cited by-同舟云学术

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A general amphipathic α-helical motif for sensing membrane curvature

Published:2007-01-14 Issue:2 Volume:14 Page:138-146
ISSN:1545-9993
Container-title:Nature Structural & Molecular Biology
language:en
Short-container-title:Nat Struct Mol Biol

Author:

Drin Guillaume,Casella Jean-François,Gautier Romain,Boehmer Thomas,Schwartz Thomas U,Antonny Bruno

Publisher

Springer Science and Business Media LLC

Subject

Molecular Biology,Structural Biology

Link

http://www.nature.com/articles/nsmb1194.pdf

Reference48 articles.

1. Dunne, S.J., Cornell, R.B., Johnson, J.E., Glover, N.R. & Tracey, A.S. Structure of the membrane binding domain of CTP:phosphocholine cytidylyltransferase. Biochemistry 35, 11975–11984 (1996).

2. Antonny, B., Beraud-Dufour, S., Chardin, P. & Chabre, M. N-terminal hydrophobic residues of the G-protein ADP-ribosylation factor-1 insert into membrane phospholipids upon GDP to GTP exchange. Biochemistry 36, 4675–4684 (1997).

3. Jao, C.C., Der-Sarkissian, A., Chen, J. & Langen, R. Structure of membrane-bound alpha-synuclein studied by site-directed spin labeling. Proc. Natl. Acad. Sci. USA 101, 8331–8336 (2004).

4. Dathe, M. & Wieprecht, T. Structural features of helical antimicrobial peptides: their potential to modulate activity on model membranes and biological cells. Biochim. Biophys. Acta 1462, 71–87 (1999).

5. Lee, M.C. et al. Sar1p N-terminal helix initiates membrane curvature and completes the fission of a COPII vesicle. Cell 122, 605–617 (2005).

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