English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

Structural characterization of α-synuclein in an aggregation prone state.

MPS-Authors
/persons/resource/persons14944

Cho,  M. K.
Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons15063

Fernandez,  C. O.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons14824

Becker,  S.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons16093

Zweckstetter,  M.
Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society;

Locator
There are no locators available
Fulltext (public)

587975.pdf
(Publisher version), 722KB

Supplementary Material (public)
There is no public supplementary material available
Citation

Cho, M. K., Nodet, G., Kim, H. K., Jensen, M. R., Bernado, P., Fernandez, C. O., et al. (2009). Structural characterization of α-synuclein in an aggregation prone state. Protein Science, 18(9), 1840-1846. Retrieved from http://www3.interscience.wiley.com/cgi-bin/fulltext/122466284/PDFSTART.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0012-D785-4
Abstract
There is no abstract available