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| Hauptseite > Publikationsdatenbank > Hepatitis C virus NS5A is able to competitively displace c-Myc from the Bin1 SH3 domain in vitro > print |
| Hauptseite > Publikationsdatenbank > Hepatitis C virus NS5A is able to competitively displace c-Myc from the Bin1 SH3 domain in vitro > print |
| 001 | 153336 | ||
| 005 | 20210129213725.0 | ||
| 024 | 7 | _ | |a 10.1002/psc.2618 |2 doi |
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| 037 | _ | _ | |a FZJ-2014-02968 |
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| 245 | _ | _ | |a Hepatitis C virus NS5A is able to competitively displace c-Myc from the Bin1 SH3 domain in vitro |
| 260 | _ | _ | |a New York, NY [u.a.] |c 2014 |b Wiley |
| 336 | 7 | _ | |a Journal Article |b journal |m journal |0 PUB:(DE-HGF)16 |s 1399277072_3029 |2 PUB:(DE-HGF) |
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| 520 | _ | _ | |a We 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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| 700 | 1 | _ | |a Willbold, Dieter |0 P:(DE-Juel1)132029 |b 4 |
| 700 | 1 | _ | |a Schwarten, Melanie |0 P:(DE-Juel1)132019 |b 5 |e Corresponding Author |
| 773 | _ | _ | |a 10.1002/psc.2618 |g Vol. 20, no. 5, p. 334 - 340 |0 PERI:(DE-600)1491819-5 |n 5 |p 334 - 340 |t Journal of peptide science |v 20 |y 2014 |x 1075-2617 |
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