IndraLab

Statements


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"USP2 directly interacts with cyclin D1 and promotes its stabilization by antagonizing ubiquitin-dependent degradation."

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"We next investigated whether USP2 can directly interact with cyclin D1 upon co-expression of both proteins in 293 cells."

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"Finally, the interaction of USP2 and cyclin D1 was tested in vitro using GST pulldown assays."

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"These data demonstrate a direct interaction between USP2 and cyclin D1."

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"Moreover, USP2 directly interacts with cyclin D1 and promotes its stabilization by antagonizing ubiquitin-dependent degradation."

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"USP2 directly interacts with cyclin D1 to perform deubiquitylation and thereby antagonize proteasome-dependent degradation of cyclin D1."

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"USP2 directly interacted with cyclin D1 and decreased polyubiquitination-dependent degradation [ xref ]."

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"By using co-immunoprecipitation approaches, we tried to determine whether elevation of O -GlcNAcylation favors the binding of USP2 to cyclin D1, as described for BAP1 and PGC1α ( xref )."

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