IndraLab

Statements

USP15 inhibits nef. 14 / 14
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"Further, USP15 degraded not only Nef but also HIV-1 structural protein, Gag, thereby substantially inhibiting HIV-1 replication."
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"However, we did not detect significant amounts of USP15 in the nucleus.The above data demonstrated that Nef and USP15 degraded reciprocally and that USP15 mediated degradation of Nef was very pronounc[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Our data indicated that USP15 clearly induced degradation of Nef and other viral structural protein, Gag, in the repeated experiments."
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"Nef could also cause decay of USP15, although Nef mediated degradation of USP15 was weaker than USP15 mediated Nef degradation."
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"The above data demonstrated that Nef and USP15 degraded reciprocally and that USP15 mediated degradation of Nef was very pronounced, compared with Nef mediated decay of USP15."
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"These data indicate that Nef expressed from the wt-HIV-1-, but not from Deltanef-HIV-1-replicating cells, degraded USP15, lowering the amount of intracellular USP15, which in turn vitiated USP15 induc[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"USP15 degraded not only Nef but also Gag, and the USP15 mediated inhibitory effect on wt-HIV-1 replication was more pronounced than on Deltanef-HIV-1 replication (XREF_FIG)."
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"These data evinced that Nef and USP15 are key players in governing intracellular viral and cellular protein stability and thus the HIV-1 and host cell competition, determining the course of disease.Ou[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"These data indicate that Nef expressed from the wt-HIV-1-, but not from Deltanef-HIV-1-replicating cells, degraded USP15, lowering the amount of intracellular USP15, which in turn vitiated USP15 induced degradation of viral proteins and thereby HIV-1 replication, where Nef degrades USP15, but USP15 mediated Nef degradation is more potent (XREF_FIG)."
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"In parallel, replication of wt- and Deltanef-HIV-1 was significantly impaired by USP15, indicating that USP15 degraded not only Nef but also Gag and thus hampered HIV-1 replication."
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"These data establish that USP15 mediated p24 degradation is achieved via both endosomal and proteosomal degradation.These data collectively demonstrated that stability of Nef and USP15 is regulated re[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"In parallel, replication of wt- and Deltanef-HIV-1 (XREF_FIG, below A and B, respectively) was significantly impaired by USP15, indicating that USP15 degraded not only Nef but also Gag and thus hampered HIV-1 replication."
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"Our co-immunoprecipitation analysis demonstrated that Nef interacted with ubiquitin specific protease 15 (USP15), and that USP15, which is known to stabilize cellular proteins, degraded Nef."
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"These data collectively demonstrated that stability of Nef and USP15 is regulated reciprocally, and that USP15 mediated degradation of Nef was more pronounced than Nef mediated degradation of USP15."
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