Structure of the full-length TRPV2 channel by cryo-EM-Reference-Cited by-同舟云学术

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Structure of the full-length TRPV2 channel by cryo-EM

Published:2016-03-29 Issue:1 Volume:7 Page:
ISSN:2041-1723
Container-title:Nature Communications
language:en
Short-container-title:Nat Commun

Author:

Huynh Kevin W.,Cohen Matthew R.,Jiang Jiansen,Samanta Amrita,Lodowski David T.,Zhou Z. Hong,Moiseenkova-Bell Vera Y.

Publisher

Springer Science and Business Media LLC

Subject

General Physics and Astronomy,General Biochemistry, Genetics and Molecular Biology,General Chemistry

Link

http://www.nature.com/articles/ncomms11130.pdf

Reference56 articles.

1. Bootman, M. D. Calcium signaling. Cold Spring Harb. Perspect. Biol. 4, a011171 (2012).

2. Venkatachalam, K. & Montell, C. TRP channels. Annu. Rev. Biochem. 76, 387–417 (2007).

3. Caterina, M. J. et al. The capsaicin receptor: a heat-activated ion channel in the pain pathway. Nature 389, 816–824 (1997).

4. Van Der Stelt, M. & Di Marzo, V. Endovanilloids. Putative endogenous ligands of transient receptor potential vanilloid 1 channels. Eur. J. Biochem. 271, 1827–1834 (2004).

5. Cao, E., Liao, M., Cheng, Y. & Julius, D. TRPV1 structures in distinct conformations reveal activation mechanisms. Nature 504, 113–118 (2013).

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