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  Dynamic structure of lipid-bound synaptobrevin suggests a nucleation-propagation mechanism for trans-SNARE complex formation.

Ellena, J. F., Liang, B. Y., Wiktor, M., Stein, A., Cafiso, D. S., Jahn, R., et al. (2009). Dynamic structure of lipid-bound synaptobrevin suggests a nucleation-propagation mechanism for trans-SNARE complex formation. Proceedings of the National Academy of Sciences of the United States of America, 106(48), 20306-20311. Retrieved from http://www.pnas.org/content/106/48/20306.full.pdf+html.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-0012-D6DF-4 Version Permalink: https://hdl.handle.net/21.11116/0000-0000-337C-C
Genre: Journal Article

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 Creators:
Ellena, J. F., Author
Liang, B. Y., Author
Wiktor, M., Author
Stein, A.1, Author           
Cafiso, D. S., Author
Jahn, R.2, Author           
Tamm, L. K., Author
Affiliations:
1Research Group of Membrane Protein Biochemistry, MPI for Biophysical Chemistry, Max Planck Society, ou_2149675              
2Department of Neurobiology, MPI for biophysical chemistry, Max Planck Society, ou_578595              

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Free keywords: structure; dynamics; membrane fusion; SNARE proteins; NMR
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Language(s): eng - English
 Dates: 2009-12-01
 Publication Status: Issued
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 Rev. Type: -
 Identifiers: eDoc: 447492
URI: http://www.pnas.org/content/106/48/20306.full.pdf+html
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Title: Proceedings of the National Academy of Sciences of the United States of America
Source Genre: Journal
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Pages: - Volume / Issue: 106 (48) Sequence Number: - Start / End Page: 20306 - 20311 Identifier: -