The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Mechanisms of Proton Conduction and Gating in Influenza M2 Proton Channels from Solid-State NMR
Open accessAbstract
M2 Out of the Envelope: The M2 protein from influenza A virus forms an acid-activated tetrameric proton channel in the viral envelope and is essential for viral replication. Two manuscripts shed light on the functional mechanism of this channel. Sharma et al. (p. 509 ; see the Perspective by Fiorin et al. ) determined the structure of the conductance domain in a lipid bilayer and propose that a histidine and tryptophan from each monomer form a cluster that guides protons through the channel in a mechanism that involves forming and breaking hydrogen bonds between adjacent pairs of histidines. Hu et al. (p. 505 ; see the Perspective by Fiorin et al. ) focused on the structure and dynamics of the proton-selective histidine at high and low pH, proposing that proton conduction involves histidine deprotonation and reprotonation.
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Cites
Luo, W., & Hong, M. (2010) · Journal of the American Chemical Society · doi:10.1021/ja9096219 · Cited by 90
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Metadata
- Authors
- Hu, F., Luo, W., & Hong, M.
- Venue
- Science
- Published
- 2010-10-22
- Volume
- 330
- Issue
- 6003
- Pages
- 505-508
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2013767643
- Cited by
- 325
- References
- 1
- FWCI
- 15.06
- Type
- journal article
- Language
- en
- Open access
- green
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- Hu, F., Luo, W., & Hong, M. (2010). Mechanisms of Proton Conduction and Gating in Influenza M2 Proton Channels from Solid-State NMR. Science. https://doi.org/10.1126/science.1191714
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