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@ARTICLE{Stangler:59381,
author = {Stangler, T. and Tran, T. and Hoffmann, S. and Schmidt, H.
and Jonas, E. and Willbold, D.},
title = {{C}ompetitive displacement of full-length {HIV}-1 {N}ef
from the {H}ck {SH}3 domain by a high-affinity artificial
peptide},
journal = {Biological chemistry},
volume = {388},
issn = {1431-6730},
address = {Berlin [u.a.]},
publisher = {de Gruyter},
reportid = {PreJuSER-59381},
pages = {611 - 615},
year = {2007},
note = {Record converted from VDB: 12.11.2012},
abstract = {We studied the interaction of the artificial 12-aa
proline-rich peptide PD1 with the SH3 domain of the
hematopoietic cell kinase Hck and the peptide's potency in
competitively displacing HIV-1 Nef from the Hck SH3 domain.
PD1 was obtained from a phage display screen and exhibits
exceptional affinity for the Hck SH3 domain (K(d)=0.23
microM). Competition experiments using NMR spectroscopy
demonstrate that the peptide even displaces Nef from Hck SH3
and allow for estimation of the Nef-Hck SH3 dissociation
constant (K(d)=0.44 microM), the strongest SH3 ligand
interaction known so far. Consequences of this study for
novel antiviral concepts are discussed.},
keywords = {Binding, Competitive / Gene Products, nef: metabolism /
Humans / Peptides: metabolism / Protein Binding /
Proto-Oncogene Proteins c-hck: metabolism / nef Gene
Products, Human Immunodeficiency Virus / src Homology
Domains / Gene Products, nef (NLM Chemicals) / Peptides (NLM
Chemicals) / nef Gene Products, Human Immunodeficiency Virus
(NLM Chemicals) / HCK protein, human (NLM Chemicals) /
Proto-Oncogene Proteins c-hck (NLM Chemicals) / J (WoSType)},
cin = {INB-2 / JARA-SIM},
ddc = {540},
cid = {I:(DE-Juel1)VDB805 / I:(DE-Juel1)VDB1045},
pnm = {Funktion und Dysfunktion des Nervensystems},
pid = {G:(DE-Juel1)FUEK409},
shelfmark = {Biochemistry $\&$ Molecular Biology},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:17552908},
UT = {WOS:000247141500007},
doi = {10.1515/BC.2007.075},
url = {https://juser.fz-juelich.de/record/59381},
}