2003
DOI: 10.1016/s0378-1119(03)00800-x
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The mouse YAF2 gene generates two distinct transcripts and is expressed in pre-and postimplantation embryos

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Cited by 11 publications
(18 citation statements)
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“…[42][43][44][45][46]. We have shown that, in addition to binding to caspase 8, zYaf2, like its mammalian counterpart (37,41), is capable of interacting with the mammalian Ring1A and Ring1B PcG proteins (data not shown). Accordingly, the apoptosis resulting from Yaf2 deficiency may relate in part to the Yaf2 interaction with PcG proteins and their involvement in these cellular processes.…”
Section: Discussionmentioning
confidence: 91%
“…[42][43][44][45][46]. We have shown that, in addition to binding to caspase 8, zYaf2, like its mammalian counterpart (37,41), is capable of interacting with the mammalian Ring1A and Ring1B PcG proteins (data not shown). Accordingly, the apoptosis resulting from Yaf2 deficiency may relate in part to the Yaf2 interaction with PcG proteins and their involvement in these cellular processes.…”
Section: Discussionmentioning
confidence: 91%
“…The human YAF2 was isolated as an interacting partner for YY1 [246]. Later, it was found that YAF2 also interacts with MYCN [247], MYC [248] and RING1/RNF2 [249]. YAF2 is paralog of RYBP [239] and together they constitute a functionally different cofactor family for YY1 and E4TF1/hGABP transcription factors [250].…”
Section: Core Members Of Ncprcsmentioning
confidence: 99%
“…Alternatively, this suboptimal balance may exhaust the NPC pool, which obscures consequent differentiation events, since Rybp is a moonlighting protein and is involved in such diverse biological functions as ubiquitination [3], apoptosis [36], and transcriptional repression [4], and it may have multiple roles in regulating neural differentiation as well. It further complicates the situation that Yaf2 (the other member of the Rybp/Yaf2 gene family) may compensate for the lack of Rybp at certain extent [37,38].…”
Section: Discussionmentioning
confidence: 99%