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1. Ludwig-Maximilians-Universität München

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2. Multi-element isotope dilution (ID) sector field ICP-MS: a novel technique that leads to new perspectives on the trace element systematics of ocean island basalts


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3. Analysis of the Ion Channel Gating Mechanism in Solution by Nuclear Magnetic Resonance (NMR) Spectroscopy ; BioStruct Symposium 2013


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4. Analysis of the Ion Channel Gating Mechanism in Solution by Nuclear Magnetic Resonance (NMR) Spectroscopy ; EMBO Conference on Allosteric interactions in cell signaling and...

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http://juser.fz-juelich.de/record/136520
http://www.allostery2013.org/  

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5. Structural insights into conformational changes of a cyclic nucleotide-binding domain in solution from Mesorhizobium loti K1 channel

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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3076860
http://www.ncbi.nlm.nih.gov/pubmed/21430265  
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6. Solution structure of the Mesorhizobium loti K1 channel cyclic nucleotide-binding domain in complex with cAMP

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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2727438
http://www.ncbi.nlm.nih.gov/pubmed/19465888  
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7. Insights into the Mechanism of Ligand Binding to Octopine Dehydrogenase from Pecten maximus by NMR and Crystallography

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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2924402
http://www.ncbi.nlm.nih.gov/pubmed/20808820  
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8. Analysis of the Bin1 SH3 interaction with peptides derived from the hepatitis C virus protein NS5A and c-Myc reveals that NS5A can competitively displace c-Myc in vitro

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9. Analysis of the Bin1 SH3 interaction with peptides derived from the hepatitis C virus protein NS5A and c-Myc reveals that NS5A can competitively displace c-Myc in vitro

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10. Analysis of the Bin1 SH3 interaction with peptides derived from the hepatitis C virus protein NS5A and c-Myc reveals that NS5A can competitively displace c-Myc in vitro ; 1st...

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http://juser.fz-juelich.de/record/186004
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4118443/  

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