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3D structure, ligand binding, autoinhibition, aggregation, and cellular distribution of wild-type, mutant, and labeled alpha-synuclein

MPG-Autoren
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Bertoncini,  C. W.
Department of Molecular Biology, MPI for biophysical chemistry, Max Planck Society;

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Cherny,  D. I.
Department of Molecular Biology, MPI for biophysical chemistry, Max Planck Society;

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

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

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Hoyer,  W.
Department of Molecular Biology, MPI for biophysical chemistry, Max Planck Society;

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Jares-Erijman,  E. A.
Department of Molecular Biology, MPI for biophysical chemistry, Max Planck Society;

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Jovin,  T. M.
Department of Molecular Biology, MPI for biophysical chemistry, Max Planck Society;

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Marsh,  D.
Department of Spectroscopy and Photochemical Kinetics, MPI for biophysical chemistry, Max Planck Society;

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Rasia,  R. M.
Department of Molecular Biology, MPI for biophysical chemistry, Max Planck Society;

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Roberti,  M. J.
Department of Molecular Biology, MPI for biophysical chemistry, Max Planck Society;

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Subramaniam,  V.
Department of Molecular Biology, MPI for biophysical chemistry, Max Planck Society;

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

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Zitation

Bertoncini, C. W., Cherny, D. I., Fernandez, C. O., Garfinkel, E., Griesinger, C., Hoyer, W., et al. (2005). 3D structure, ligand binding, autoinhibition, aggregation, and cellular distribution of wild-type, mutant, and labeled alpha-synuclein. Biophysical Journal, 88(1), 396A-396A.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0012-EA6A-7
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