Elucidation of New Binding Interactions with the Human Tsg101 Protein Using Modified HIV-1 Gag-p6 Derived Peptide Ligands (Q27666254)

1

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Fa Liu

2

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Young Jun Im

3

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Andrew G Stephen

4

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Matthew J Fivash

5

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Abdul A Waheed

6

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Robert J Fisher

8

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James H Hurley

9

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Terrence R Burke

ACS Medicinal Chemistry Letters

10

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publication date

12 May 2011

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published in

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Crystallographic and Functional Analysis of the ESCRT-I /HIV-1 Gag PTAP Interaction

Crossref

volume

2

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issue

5

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page(s)

337-341

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cites work

1 reference

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Structure of the Tsg101 UEV domain in complex with the PTAP motif of the HIV-1 p6 protein

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Overexpression of the N-terminal domain of TSG101 inhibits HIV-1 budding by blocking late domain function

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Tsg101 and the vacuolar protein sorting pathway are essential for HIV-1 budding

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Tsg101, a homologue of ubiquitin-conjugating (E2) enzymes, binds the L domain in HIV type 1 Pr55(Gag)

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HIV-1 and Ebola virus encode small peptide motifs that recruit Tsg101 to sites of particle assembly to facilitate egress

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SAR by oxime-containing peptide libraries: application to Tsg101 ligand optimization

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Protected aminooxyprolines for expedited library synthesis: application to Tsg101-directed proline-oxime containing peptides

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Hydrazone- and hydrazide-containing N-substituted glycines as peptoid surrogates for expedited library synthesis: application to the preparation of Tsg101-directed HIV-1 budding antagonists

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