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000153336 041__ $$aEnglish
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000153336 1001_ $$0P:(DE-Juel1)131990$$aAladag, Amine$$b0
000153336 245__ $$aHepatitis C virus NS5A is able to competitively displace c-Myc from the Bin1 SH3 domain in vitro
000153336 260__ $$aNew York, NY [u.a.]$$bWiley$$c2014
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000153336 520__ $$aWe studied the interaction of the SH3 domain of Bin1 with a 15-mer peptide of HCV NS5A and show its potency to competitively displace a 15-mer human c-Myc fragment, which is a physiological ligand of Bin1, using NMR spectroscopy. Fluorescence spectroscopy and ITC were employed to determine the affinity of Bin1 SH3 to NS5A(347–361), yielding a submicromolar affinity to NS5A. Our study compares the binding dynamics and affinities of the relevant regions for binding of c-Myc and NS5A to Bin1 SH3. The result gives further insights into the potential role of NS5A in Bin1-mediated apoptosis.Copyright © 2014 European Peptide Society and John Wiley & Sons, Ltd.
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000153336 7001_ $$0P:(DE-Juel1)132003$$aHoffmann, Silke$$b1
000153336 7001_ $$0P:(DE-Juel1)132023$$aStoldt, Matthias$$b2
000153336 7001_ $$0P:(DE-Juel1)144486$$aBösing, Christina$$b3
000153336 7001_ $$0P:(DE-Juel1)132029$$aWillbold, Dieter$$b4
000153336 7001_ $$0P:(DE-Juel1)132019$$aSchwarten, Melanie$$b5$$eCorresponding Author
000153336 773__ $$0PERI:(DE-600)1491819-5$$a10.1002/psc.2618$$gVol. 20, no. 5, p. 334 - 340$$n5$$p334 - 340$$tJournal of peptide science$$v20$$x1075-2617$$y2014
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