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@ARTICLE{Hoffmann:55895,
author = {Hoffmann, S. and Jonas, E. and König, S. and
Preusser-Kunze, A. and Willbold, D.},
title = {{N}ef protein of human immunodeficiency virus type 1 binds
its own myristoylated {N}-terminus},
journal = {Biological chemistry},
volume = {388},
issn = {1431-6730},
address = {Berlin [u.a.]},
publisher = {de Gruyter},
reportid = {PreJuSER-55895},
pages = {181 - 183},
year = {2007},
note = {Record converted from VDB: 12.11.2012},
abstract = {HIV-1 Nef is a small protein (approx. 25 kDa) that is
posttranslationally modified by myristoylation. To explain
its complex activities, a 'Nef-cycle' is discussed, which
postulates different molecular conformations of Nef. Using
recombinant full-length non-myristoylated Nef and synthetic
peptides, we demonstrate by fluorescence titration
experiments that a peptide representing the myristoylated
N-terminus of Nef is specifically bound by Nef. A
non-myristoylated N-terminal fragment of Nef or a
myristoylated control peptide does not bind to Nef. These
results are the first direct experimental evidence of the
existence of a myristate-binding pocket in Nef, a
prerequisite of the postulated 'closed' Nef conformation.},
keywords = {Calorimetry: methods / Gene Products, nef: chemistry /
Humans / Myristic Acid: chemistry / Peptides: chemistry /
Recombinant Proteins: chemistry / Spectrometry, Fluorescence
/ nef Gene Products, Human Immunodeficiency Virus / Gene
Products, nef (NLM Chemicals) / Peptides (NLM Chemicals) /
Recombinant Proteins (NLM Chemicals) / nef Gene Products,
Human Immunodeficiency Virus (NLM Chemicals) / Myristic Acid
(NLM Chemicals) / J (WoSType)},
cin = {INB-2},
ddc = {540},
cid = {I:(DE-Juel1)VDB805},
pnm = {Funktion und Dysfunktion des Nervensystems},
pid = {G:(DE-Juel1)FUEK409},
shelfmark = {Biochemistry $\&$ Molecular Biology},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:17261081},
UT = {WOS:000243978600006},
doi = {10.1515/BC.2007.020},
url = {https://juser.fz-juelich.de/record/55895},
}