IndraLab

Statements

EIF3F binds MSH4. 15 / 20
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"Since the known hMSH4 domains involved in heterotypic and homotypic interactions are not located in the N-terminal region of hMSH4 [XREF_BIBR, XREF_BIBR, XREF_BIBR], the binding of eIF3f to hMSH4 is unlikely to affect the hMSH4-hMSH5 or the homotypic hMSH4 interactions."
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"To further validate the existence of a direct physical interaction between hMSH4 and eIF3f, we next performed a GST pull-down analysis of recombinant His 6 -hMSH4 and GST-eIF3f proteins."
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"Together, these results indicate that hMSH4 interacts with eIF3f, and the N-terminal regions of both proteins are involved in this interaction."
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"The results of this assay confirmed that hMSH4 directly interacts with eIF3f."
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No evidence text available
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"Here, we demonstrate that hMSH4 interacts with eIF3f - a regulatory subunit of the eIF3 complex that has also been implicated in the regulation of apoptosis and tumorigenesis in humans [XREF_BIBR - XREF_BIBR]."
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"Co-immunoprecipitation (co-IP) with either the anti-Myc or the anti-Flag antibody was performed, and the results of co-IP analysis demonstrate that hMSH4 interacts with eIF3f in human cells."
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No evidence text available
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"The results presented in Figure XREF_FIG A clearly indicated that the interaction between hMSH4 and eIF3f was mediated through the N-terminal region of hMSH4 - most likely involving the first 150 amino acids of hMSH4."
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No evidence text available
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"As shown in Figure XREF_FIG A, yeast two-hybrid analysis demonstrated that hMSH4 specifically interacted with eIF3f."
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"The interaction of MSH4 with eIF3f (a subunit of the eIF3 complex implicated in apoptosis regulation and tumor development), for example, occurs at the region comprising the first 150 amino acids of the N-terminal domain of MSH4 (where rs5745325 is located) and has been demonstrated to foster hMSH4 stabilization and to modulate sensitivity to IR-induced DNA damage [ xref ]."
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No evidence text available
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"HMSH4 interacts with eIF3f."
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