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Journal Article

Anle138b and related compounds are aggregation specific fluorescence markers and reveal high affinity binding to α-synuclein aggregates.

MPS-Authors
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Ryazanov,  S.
Department of NMR-based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Giller,  K.
Department of NMR-based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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

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Leonov,  A.
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;

External Resource

http://www.sciencedirect.com/science/article/pii/S0304416515001609/pdfft?md5=3a90df0aeac5c87263642cdbf192dce7&pid=1-s2.0-S0304416515001609-main.pdf
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2157676.pdf
(Publisher version), 831KB

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Citation

Deeg, A. A., Reiner, A. M., Schmidt, F., Schueder, F., Ryazanov, S., Ruf, V. C., et al. (2015). Anle138b and related compounds are aggregation specific fluorescence markers and reveal high affinity binding to α-synuclein aggregates. Biochimica et Biophysica Acta-General Subjects, 1850(9), 1884-1890. doi:10.1016/j.bbagen.2015.05.021.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0027-7B5D-5
Abstract
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