IndraLab

Statements

USP15 binds FHL1. 11 / 11
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"In an effort to find novel protein–protein interactions by computational prediction (to be reported elsewhere) and its biochemical confirmation, we have identified a novel interaction of USP15 with SL[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"In the present study, we have shown that USP15 interacts with SLIM1 and deubiquitinates SLIM1, leading to the stabilization of SLIM1."
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"As shown in Fig. 1 B, purified recombinant USP15 and SLIM1 were also bound to each other under cell-free conditions, indicating that the interaction is direct."
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"In the present study, we have shown that USP15 interacts with SLIM1 and deubiquitinates SLIM1, leading to the stabilization of SLIM1."
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"Thus, the protein levels of SLIM1 are regulated by the Ub-proteasomal system, and USP15 interacts physically and functionally with SLIM1 in mammalian cells.The above results suggest that USP15 may hav[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"We have shown that USP15 interacts physically and functionally with SLIM1, and stabilizes SLIM1 by deubiquitination in the transient expression system in HEK293T cells."
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"Furthermore, USP15C269S, a catalytic-inactive USP15 mutant [16] was unable to bind with SLIM1, suggesting that the region around C269, the core enzymatic domain, was critical for the interaction."
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"Thus, the protein levels of SLIM1 are regulated by the Ub-proteasomal system, and USP15 interacts physically and functionally with SLIM1 in mammalian cells."
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"We have shown that USP15 interacts physically and functionally with SLIM1, and stabilizes SLIM1 by deubiquitination in the transient expression system in HEK293T cells."
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biogrid
No evidence text available
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biogrid
No evidence text available
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