Search results for "l-chicoric acid cancer"


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L cycle regulation. The LxCxE motif and the tripeptide HDP of the J domain of the polyomavirus tumor proteins make direct contacts with the Rb proteins and Hsc70, respectively; together they effect the release of members of the E2F family of transcription factors from their Rb partners to promote cell cycle progression [reviewed in 55]. There is less certainty about the identity of tAg amino acid

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Es and one proline of the CxxxPxC motif located upstream of the CxCxxC clusters did reduce PP2A binding significantly. Additional studies that relied upon peptide inhibition of the tAg-PP2A interaction without destabilizing tAg suggested that the CxCxxC clusters might indeed influence tAg binding to the A subunit [23,25]. Two recent X-ray crystallographic studies indicate the CxCxxC clusters and

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Rvation will require additional investigation to determine if enhanced PP2A binding is associated with a transformed phenotype. It should be noted that to detect PP2A binding in this study, we employed antibodies that recognized the catalytic subunit of PP2A. PP2A is found abundantly as either a holoenzyme consisting of the AC core plus a regulatory B subunit, or as the AC core alone. High levels

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Phosphatase activity of PP2A in studies involving a second known binding partner of tAg, the JCV agnoprotein [40]. We were surprised to identify two LxCxE motifs that had been overlooked in the unique region of the JCV tAg; one of these sites is also found in BKV but neither site resides in the corresponding SV40, WUV, KIV or MCV polyomavirus proteins. As predicted, JCV tAg binds members of the r