Peptide ligands selected with CD4-induced epitopes on native dualtropic HIV-1 
envelope proteins mimic extracellular coreceptor domains and bind to HIV-1 
gp120 independently of coreceptor usage.

Dervillez, X.; Klaukien, V.; Duerr, R.; Koch, J.; Kreutz, A.; Haarmann, T.; Stoll, M.; Lee, D.; Carlomagno, T.; Schnierle, B.; Moebius, K.; Koenigs, C.; Griesinger, C.; Dietrich, U.

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Peptide ligands selected with CD4-induced epitopes on native dualtropic HIV-1 envelope proteins mimic extracellular coreceptor domains and bind to HIV-1 gp120 independently of coreceptor usage.

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Klaukien, V.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Lee, D.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Carlomagno, T.
Research Group of Liquid NMR Spectroscopy, MPI for biophysical chemistry, Max Planck Society;

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Griesinger, C.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Dervillez, X., Klaukien, V., Duerr, R., Koch, J., Kreutz, A., Haarmann, T., et al. (2010). Peptide ligands selected with CD4-induced epitopes on native dualtropic HIV-1 envelope proteins mimic extracellular coreceptor domains and bind to HIV-1 gp120 independently of coreceptor usage. Journal of Virology, 84(19), 10131-10138.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0012-D54A-B

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