RanBP2 regulates the anti-retroviral activity of TRIM5α by SUMOylation at a predicted phosphorylated SUMOylation motif

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RanBP2 regulates the anti-retroviral activity of TRIM5α by SUMOylation at a predicted phosphorylated SUMOylation motif

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scientific article published on 15 November 2018

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wetenschappelijk artikel

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наукова стаття, опублікована у 2018

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RanBP2 regulates the anti-retr ...... osphorylated SUMOylation motif

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RanBP2 regulates the anti-retr ...... osphorylated SUMOylation motif

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RanBP2 regulates the anti-retr ...... osphorylated SUMOylation motif

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RanBP2 regulates the anti-retr ...... osphorylated SUMOylation motif

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RanBP2 regulates the anti-retr ...... osphorylated SUMOylation motif

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RanBP2 regulates the anti-retr ...... osphorylated SUMOylation motif

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RanBP2 regulates the anti-retr ...... osphorylated SUMOylation motif

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Aude Boulay

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Débora M Portilho

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Gillian Butler-Browne

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Jacques Dutrieux

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Stéphane Oddos

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P2860

HIV-1 capsid-cyclophilin interactions determine nuclear import pathway, integration targeting and replication efficiency

Identification of host proteins required for HIV infection through a functional genomic screen

Human MX2 is an interferon-induced post-entry inhibitor of HIV-1 infection

MX2 is an interferon-induced inhibitor of HIV-1 infection

The SUMO E3 ligase RanBP2 promotes modification of the HDAC4 deacetylase

PIASy, a nuclear matrix-associated SUMO E3 ligase, represses LEF1 activity by sequestration into nuclear bodies

Misdelivery at the Nuclear Pore Complex-Stopping a Virus Dead in Its Tracks

The SUMO pathway: emerging mechanisms that shape specificity, conjugation and recognition.

The nucleoporin RanBP2 has SUMO1 E3 ligase activity

The polycomb protein Pc2 is a SUMO E3

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scholarly article

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10.1038/S42003-018-0198-0

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English

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2018-11-15T00:00:00Z

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30456314

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phosphorylation

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6237768

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